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Journal articles on the topic 'Zinc metalloenzyme'

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Published: 4 June 2021

Last updated: 20 February 2023

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1

Stoecker, Walter, Russell L. Wolz, Robert Zwilling, Daniel J. Strydom, and David S. Auld. "Astacus protease, a zinc metalloenzyme." Biochemistry 27, no. 14 (July 12, 1988): 5026–32. http://dx.doi.org/10.1021/bi00414a012.

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2

Vallee, B. L. "Zinc metalloenzyme structure and function." Journal of Inorganic Biochemistry 36, no. 3-4 (August 1989): 299. http://dx.doi.org/10.1016/0162-0134(89)84446-0.

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3

Haeggström, Jesper Z., Anders Wetterholm, Robert Shapiro, Bert L. Vallee, and Bengt Samuelsson. "Leukotriene A4 hydrolase: A zinc metalloenzyme." Biochemical and Biophysical Research Communications 172, no. 3 (November 1990): 965–70. http://dx.doi.org/10.1016/0006-291x(90)91540-9.

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4

Hadianawala, Murtuza, and Bhaskar Datta. "Design and development of sulfonylurea derivatives as zinc metalloenzyme modulators." RSC Advances 6, no. 11 (2016): 8923–29. http://dx.doi.org/10.1039/c5ra27341b.

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5

Millian, Norman S., and Timothy A. Garrow. "Human Betaine–Homocysteine Methyltransferase Is a Zinc Metalloenzyme." Archives of Biochemistry and Biophysics 356, no. 1 (August 1998): 93–98. http://dx.doi.org/10.1006/abbi.1998.0757.

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6

González, Julio C., Katrina Peariso, James E. Penner-Hahn, and Rowena G. Matthews. "Cobalamin-Independent Methionine Synthase fromEscherichia coli: A Zinc Metalloenzyme†." Biochemistry 35, no. 38 (January 1996): 12228–34. http://dx.doi.org/10.1021/bi9615452.

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7

Brothers, Edward N., Dimas Suarez, David W. Deerfield, and Kenneth M. Merz. "PM3-compatible zinc parameters optimized for metalloenzyme active sites." Journal of Computational Chemistry 25, no. 14 (2004): 1677–92. http://dx.doi.org/10.1002/jcc.20086.

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8

Tanaka, Tomoaki, and Eiji Ichishima. "Molecular properties of aminopeptidase ey as a zinc-metalloenzyme." International Journal of Biochemistry 25, no. 11 (November 1993): 1681–88. http://dx.doi.org/10.1016/0020-711x(93)90528-m.

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9

Shapir, Nir, Charlotte Pedersen, Omer Gil, Lisa Strong, Jennifer Seffernick, Michael J. Sadowsky, and Lawrence P. Wackett. "TrzN from Arthrobacter aurescens TC1 Is a Zinc Amidohydrolase." Journal of Bacteriology 188, no. 16 (August 15, 2006): 5859–64. http://dx.doi.org/10.1128/jb.00517-06.

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ABSTRACT TrzN, the broad-specificity triazine hydrolase from Arthrobacter and Nocardioides spp., is reportedly in the amidohydrolase superfamily of metalloenzymes, but previous studies suggested that a metal was not required for activity. To help resolve that conundrum, a double chaperone expression system was used to produce multimilligram quantities of functionally folded, recombinant TrzN. The TrzN obtained from Escherichia coli (trzN) cells cultured with increasing zinc in the growth medium showed corresponding increases in specific activity, and enzyme obtained from cells grown with 500 μM zinc showed maximum activity. Recombinant TrzN contained 1 mole of Zn per mole of TrzN subunit. Maximally active TrzN was not affected by supplementation with most metals nor by EDTA, consistent with previous observations (E. Topp, W. M. Mulbry, H. Zhu, S. M. Nour, and D. Cuppels, Appl. Environ. Microbiol. 66:3134-3141, 2000) which had led to the conclusion that TrzN is not a metalloenzyme. Fully active native TrzN showed a loss of greater than 90% of enzyme activity and bound zinc when treated with the metal chelator 8-hydroxyquinoline-5-sulfonic acid. While exogenously added zinc or cobalt restored activity to metal-depleted TrzN, cobalt supported lower activity than did zinc. Iron, manganese, nickel, and copper did not support TrzN activity. Both Zn- and Co-TrzN showed different relative activities with different s-triazine substrates. Co-TrzN showed a visible absorption spectrum characteristic of other members of the amidohydrolase superfamily replaced with cobalt.

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10

Álvarez-Santos, Silvia, Àngels González-Lafont, and José M. Lluch. "Effect of the hydrogen bond network in carbonic anhydrase II zinc binding site. A theoretical study." Canadian Journal of Chemistry 76, no. 7 (July 1, 1998): 1027–32. http://dx.doi.org/10.1139/v98-098.

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The hydrogen bond network influence on the carbonic anhydrase II (CAII) zinc binding site has been studied theoretically by using the semiempirical AM1 method. To this aim, quantum mechanical reduced models of wild-type CAII and several CAII variants have been constructed. We have shown that, when a direct metal ligand donates a hydrogen bond to an indirect metal ligand, the first-shell residues enhance their electrostatic interaction with the zinc cation. Thus, the hydrogen-bond network is able to modulate the zinc binding affinity and the zinc-water pKa.Key words: hydrogen bond network, carbonic anhydrase II, Zn2+ metalloenzyme ligands.

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11

Khare, Sagar D., Yakov Kipnis, Per Jr Greisen, Ryo Takeuchi, Yacov Ashani, Moshe Goldsmith, Yifan Song, et al. "Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis." Nature Chemical Biology 8, no. 3 (February 5, 2012): 294–300. http://dx.doi.org/10.1038/nchembio.777.

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12

O’Young, Jason, Nicole Sukdeo, and John F. Honek. "Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme." Archives of Biochemistry and Biophysics 459, no. 1 (March 2007): 20–26. http://dx.doi.org/10.1016/j.abb.2006.11.024.

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13

PROUDFOOT, Amanda E. I., Laurence GOFFIN, Mark A. PAYTON, Timothy N. C. WELLS, and Alain R. BERNARD. "In vivo and in vitro folding of a recombinant metalloenzyme, phosphomannose isomerase." Biochemical Journal 318, no. 2 (September 1, 1996): 437–42. http://dx.doi.org/10.1042/bj3180437.

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Phosphomannose isomerase (PMI) catalyses the interconversion of mannose 6-phosphate and fructose 6-phosphate in prokaryotic and eukaryotic cells. The enzyme is a metalloenzyme which contains 1 mol of zinc per mol of enzyme. Heterologous expression of the cDNA coding for the Candida albicans enzyme in the prokaryotic host Escherichia coli results in an expression level of up to 30% of total E. coli protein. Ten percent of recombinant PMI is expressed in the soluble fraction and 90% in inclusion bodies. Inclusion of a high level of zinc in the fermentation medium resulted in a fourfold increase in soluble protein. Co-expression of the bacterial chaperones, GroES and GroEL, resulted in a proportional twofold increase in soluble PMI while causing an overall decrease in the PMI expression level. Folding denatured PMI in vitro required reductant and zinc ions. The yield of renatured protein was increased by folding in the presence of GroEL and DnaK in an ATP-independent manner. The refolding yield of denatured soluble enzyme from a guanidine solution was threefold higher than that of folding monomerized inclusion body protein solubilized in guanidine hydrochloride. This suggests that a proportion of recombinant protein expressed in E. coli inclusion bodies may be irreversibly denatured.

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14

D’Ordine, Robert L., Rebecca S. Linger, Carolyn J. Thai, and V. Jo Davisson. "Catalytic Zinc Site and Mechanism of the Metalloenzyme PR-AMP Cyclohydrolase." Biochemistry 51, no. 29 (July 9, 2012): 5791–803. http://dx.doi.org/10.1021/bi300391m.

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15

Pettigrew, D. W., R. R. Bidigare, B. J. Mehta, M. I. Williams, and E. G. Sander. "Dihydro-orotase from Clostridium oroticum. Purification and reversible removal of essential zinc." Biochemical Journal 230, no. 1 (August 15, 1985): 101–8. http://dx.doi.org/10.1042/bj2300101.

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A new purification procedure involving five column-chromatography steps is described for dihydro-orotase (L-5,6-dihydro-orotate amidohydrolase, EC 3.5.2.3) from Clostridium oroticum (A.T.C.C. 25750). The native purified enzyme is a dimer of Mr 102 000 and contains 4.0 +/- 0.3 g-atoms of zinc/mol of dimer. These observations agree with those reported previously [Taylor, Taylor, Balch & Gilchrist (1976) J. Bacteriol. 127, 863-873]. It is conclusively demonstrated that dihydro-orotase is a zinc metalloenzyme. Zinc is reversibly removed by treatment with chelators in phosphate buffer at pH 6.5, as demonstrated by atomic absorption spectrophotometry and decrease of enzyme activity. The specific activity is linearly dependent on zinc content. Addition of ZnSO4 to the chelator-treated enzyme results in regain of the normal complement of zinc and enzyme activity. Kinetic properties of the reconstituted enzyme are indistinguishable from those of the native enzyme. The amino acid composition of the homogeneous enzyme suggests that the zinc atoms occupy different environments.

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16

Komai, Michio, Tomoko Goto, Hitoshi Suzuki, Tomohiko Takeda, and Yuji Furukawa. "Zinc deficiency and taste dysfunction; Contribution of carbonic anhydrase, a zinc-metalloenzyme, to normal taste sensation." BioFactors 12, no. 1-4 (2000): 65–70. http://dx.doi.org/10.1002/biof.5520120111.

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17

May, Oliver, Martin Siemann, Michael G. Siemann, and Christoph Syldatk. "The hydantoin amidohydrolase from Arthrobacter aurescens DSM 3745 is a zinc metalloenzyme." Journal of Molecular Catalysis B: Enzymatic 5, no. 1-4 (September 1998): 367–70. http://dx.doi.org/10.1016/s1381-1177(98)00060-5.

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18

Wetterholm, Anders, Juan F. Medina, Olof Rådmark, Robert Shapiro, Jesper Z. Haeggström, Bert L. Vallee, and Bengt Samuelsson. "Recombinant mouse leukotriene A4 hydrolase: a zinc metalloenzyme with dual enzymatic activities." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1080, no. 2 (October 1991): 96–102. http://dx.doi.org/10.1016/0167-4838(91)90134-l.

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19

Ruzicka, Frank J., Joseph E. Wedekind, Jeongmin Kim, Ivan Rayment, and Perry A. Frey. "Galactose-1-phosphate Uridylyltransferase from Escherichia coli, a Zinc and Iron Metalloenzyme." Biochemistry 34, no. 16 (April 25, 1995): 5610–17. http://dx.doi.org/10.1021/bi00016a036.

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20

Ohno, H., K. Yamashita, R. Doi, K. Yamamura, T. Kondo, and N. Taniguchi. "Exercise-induced changes in blood zinc and related proteins in humans." Journal of Applied Physiology 58, no. 5 (May 1, 1985): 1453–58. http://dx.doi.org/10.1152/jappl.1985.58.5.1453.

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Effects of cycle ergometer exercise (approximately 75% maximum ventilatory O2 consumption for 30 min) on the concentrations of zinc and related proteins in erythrocytes and/or plasma were studied on 11 sedentary male students. Lower concentrations of total zinc and of zinc derived from carbonic anhydrase I type (CA-I) in erythrocytes were observed immediately after exercise, but they disappeared after 30 min of rest. The change in total zinc concentration in erythrocytes correlated well with that in CA-I concentration immediately after exercise, as well as after rest. The concentration of carbonic anhydrase II type (CA-II)-derived zinc did not vary substantially at any time. On the other hand, there were significant increases in the plasma concentrations of total zinc and of alpha 2-macroglobulin (alpha 2-MG)-bound zinc immediately after exercise, whereas no such effect was noted in albumin-bound zinc. A positive correlation was found between total zinc and alpha 2-MG concentrations in plasma immediately after exercise. In addition, the change in the activity of alkaline phosphatase, a zinc metalloenzyme, correlated well with that in the total zinc concentration in plasma. These results suggest that a brief physical exercise induces the movement of zinc into plasma.

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21

Robinson, Sophia G., Philip T. Burns, Amanda M. Miceli, Kyle A. Grice, Caitlin E. Karver, and Lihua Jin. "Calorimetric studies of the interactions of metalloenzyme active site mimetics with zinc-binding inhibitors." Dalton Transactions 45, no. 29 (2016): 11817–29. http://dx.doi.org/10.1039/c6dt01675h.

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The binding of drugs to metalloenzymes is an intricate process that involves several interactions, including binding of the drug to the enzyme active site metal, as well as multiple interactions between the drug and the enzyme residues.

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22

Tsuchiya, Hironori. "Gustatory and Saliva Secretory Dysfunctions in COVID-19 Patients with Zinc Deficiency." Life 12, no. 3 (February 28, 2022): 353. http://dx.doi.org/10.3390/life12030353.

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Given the ever-progressing studies on coronavirus disease 2019 (COVID-19), it is critical to update our knowledge about COVID-19 symptomatology and pathophysiology. In the present narrative review, oral symptoms were overviewed using the latest data and their pathogenesis was hypothetically speculated. PubMed, LitCovid, ProQuest, and Google Scholar were searched for relevant studies from 1 April 2021 with a cutoff date of 31 January 2022. The literature search indicated that gustatory dysfunction and saliva secretory dysfunction are prevalent in COVID-19 patients and both dysfunctions persist after recovery from the disease, suggesting the pathogenic mechanism common to these cooccurring symptoms. COVID-19 patients are characterized by hypozincemia, in which zinc is possibly redistributed from blood to the liver at the expense of zinc in other tissues. If COVID-19 induces intracellular zinc deficiency, the activity of zinc-metalloenzyme carbonic anhydrase localized in taste buds and salivary glands may be influenced to adversely affect gustatory and saliva secretory functions. Zinc-binding metallothioneins and zinc transporters, which cooperatively control cellular zinc homeostasis, are expressed in oral tissues participating in taste and saliva secretion. Their expression dysregulation associated with COVID-19-induced zinc deficiency may have some effect on oral functions. Zinc supplementation is expected to improve oral symptoms in COVID-19 patients.

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23

Studer, Sabine, Douglas A. Hansen, Zbigniew L. Pianowski, Peer R. E. Mittl, Aaron Debon, Sharon L. Guffy, Bryan S. Der, Brian Kuhlman, and Donald Hilvert. "Evolution of a highly active and enantiospecific metalloenzyme from short peptides." Science 362, no. 6420 (December 13, 2018): 1285–88. http://dx.doi.org/10.1126/science.aau3744.

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Primordial sequence signatures in modern proteins imply ancestral origins tracing back to simple peptides. Although short peptides seldom adopt unique folds, metal ions might have templated their assembly into higher-order structures in early evolution and imparted useful chemical reactivity. Recapitulating such a biogenetic scenario, we have combined design and laboratory evolution to transform a zinc-binding peptide into a globular enzyme capable of accelerating ester cleavage with exacting enantiospecificity and high catalytic efficiency (kcat/KM~ 106M−1s−1). The simultaneous optimization of structure and function in a naïve peptide scaffold not only illustrates a plausible enzyme evolutionary pathway from the distant past to the present but also proffers exciting future opportunities for enzyme design and engineering.

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24

Jackman, Jane E., Christian R. H. Raetz, and Carol A. Fierke. "UDP-3-O-(R-3-Hydroxymyristoyl)-N-acetylglucosamine Deacetylase ofEscherichiacoliIs a Zinc Metalloenzyme†." Biochemistry 38, no. 6 (February 1999): 1902–11. http://dx.doi.org/10.1021/bi982339s.

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25

Beck, Jennifer L., Lyndal A. McConachie, Andrew C. Summors, Wilfred N. Arnold, John De Jersey, and Burt Zerner. "Properties of a purple phosphatase from red kidney bean: a zinc-iron metalloenzyme." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 869, no. 1 (January 1986): 61–68. http://dx.doi.org/10.1016/0167-4838(86)90310-9.

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26

Temperini, Claudia, Alessio Innocenti, Andrea Scozzafava, and Claudiu T. Supuran. "N-Hydroxyurea—A versatile zinc binding function in the design of metalloenzyme inhibitors." Bioorganic & Medicinal Chemistry Letters 16, no. 16 (August 2006): 4316–20. http://dx.doi.org/10.1016/j.bmcl.2006.05.068.

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27

Jalilehvand, Farideh, Natalie Sisombath, Bonnie Leung, and Vicky Mah. "Silver(I) and Lead(II) Complex Formation with Thiolates." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C719. http://dx.doi.org/10.1107/s2053273314092808.

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Lead toxicity is frequently attributed to the displacement of essential metals such as zinc. Lead(II) ions mainly inhibit the enzymatic activity of ALAD, a key zinc-containing metalloenzyme in the heme biosynthetic pathway with much higher affinity to bind to Pb(II) than Zn(II) ions via its cysteinyl residues. Also for silver(I) ions the interaction with thiol-containing species such as cysteine and glutathione plays a key role in bacterial inactivation and Ag(I) antimicrobial activity. We will present the results of our investigations on Pb(II) and Ag(I) complex formation with small thiol-containing molecules of biological interest such as cysteine, penicillamine, N-acetylcysteine and glutathione, using a combination of different techniques, including X-ray absorption fine structure (XAFS) spectroscopy, multinuclear NMR (207Pb, 109Ag) and X-ray crystallography.

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28

Urbaniak, Michael D., Arthur Crossman, Tunhan Chang, Terry K. Smith, Daan M. F. van Aalten, and Michael A. J. Ferguson. "TheN-Acetyl-D-glucosaminylphosphatidylinositol De-N-acetylase of Glycosylphosphatidylinositol Biosynthesis Is a Zinc Metalloenzyme." Journal of Biological Chemistry 280, no. 24 (April 6, 2005): 22831–38. http://dx.doi.org/10.1074/jbc.m502402200.

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29

Patturajan, Meera, Mayalagu Sevugan, and Dipankar Chatterji. "DNA-Dependent RNA Polymerase II from Candida Species Is a Multiple Zinc-Containing Metalloenzyme." International Union of Biochemistry and Molecular Biology: Life 48, no. 2 (August 1, 1999): 163–68. http://dx.doi.org/10.1080/152165499307170.

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30

Patturajan, Meera, Mayalagu Sevugan, and Dipankar Chatterji. "DNA-Dependent RNA Polymerase II from Candida Species Is a Multiple Zinc-Containing Metalloenzyme." IUBMB Life 48, no. 2 (August 1, 1999): 163–68. http://dx.doi.org/10.1080/713803489.

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31

Sahin, H., R. Aliyazicioglu, O. Yildiz, S. Kolayli, A. Innocenti, and C. T. Supuran. "Honey, polen, and propolis extracts show potent inhibitory activity against the zinc metalloenzyme carbonic anhydrase." Journal of Enzyme Inhibition and Medicinal Chemistry 26, no. 3 (August 5, 2010): 440–44. http://dx.doi.org/10.3109/14756366.2010.503610.

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32

Giastas, Petros, Athena Andreou, Athanasios Papakyriakou, Dimitris Koutsioulis, Stavroula Balomenou, Socrates J. Tzartos, Vassilis Bouriotis, and Elias E. Eliopoulos. "Structures of the Peptidoglycan N-Acetylglucosamine Deacetylase Bc1974 and Its Complexes with Zinc Metalloenzyme Inhibitors." Biochemistry 57, no. 5 (January 5, 2018): 753–63. http://dx.doi.org/10.1021/acs.biochem.7b00919.

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33

Murphy, B. P., and R. F. Pratt. "A thiono-β-lactam substrate for the β-lactamase II of Bacillus cereus. Evidence for direct interaction between the essential metal ion and substrate." Biochemical Journal 258, no. 3 (March 15, 1989): 765–68. http://dx.doi.org/10.1042/bj2580765.

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An 8-thionocephalosporin was shown to be a substrate of the beta-lactamase II of Bacillus cereus, a zinc metalloenzyme. Although it is a poorer substrate, as judged by the Kcat./Km parameter, than the corresponding 8-oxocephalosporin, the discrimination against sulphur decreased when the bivalent metal ion in the enzyme active site was varied in the order Mn2+ (the manganese enzyme catalysed the hydrolysis of the oxo compound but not that of the thiono compound), Zn2+, Co2+ and Cd2+. This result is taken as evidence for kinetically significant direct contact between the active-site metal ion of beta-lactamase II and the beta-lactam carbonyl heteroatom. No evidence was obtained, however, for accumulation of an intermediate with such co-ordination present.

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34

Haeggström, Jesper Z., Pär Nordlund, and Marjolein M. G. M. Thunnissen. "Functional Properties and Molecular Architecture of Leukotriene A4 Hydrolase, a Pivotal Catalyst of Chemotactic Leukotriene Formation." Scientific World JOURNAL 2 (2002): 1734–49. http://dx.doi.org/10.1100/tsw.2002.810.

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The leukotrienes are a family of lipid mediators involved in inflammation and allergy. Leukotriene B4is a classical chemoattractant, which triggers adherence and aggregation of leukocytes to the endothelium at only nM concentrations. In addition, leukotriene B4modulates immune responses, participates in the host defense against infections, and is a key mediator of PAF-induced lethal shock. Because of these powerful biological effects, leukotriene B4 is implicated in a variety of acute and chronic inflammatory diseases, e.g., nephritis, arthritis, dermatitis, and chronic obstructive pulmonary disease. The final step in the biosynthesis of leukotriene B4is catalyzed by leukotriene A4hydrolase, a unique bifunctional zinc metalloenzyme with an anion-dependent aminopeptidase activity. Here we describe the most recent developments regarding our understanding of the function and molecular architecture of leukotriene A4hydrolase.

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35

Han, Jin-Suk, and Kazuhiko Ishikawa. "Active site of Zn2+-dependentsn-glycerol-1-phosphate dehydrogenase fromAeropyrum pernixK1." Archaea 1, no. 5 (2005): 311–17. http://dx.doi.org/10.1155/2005/257264.

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The enzymesn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) is key to the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. This enzyme catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate. To date, no information about the active site and catalytic mechanism of this enzyme has been reported. Using the sequence and structural information for glycerol dehydrogenase, we constructed six mutants (D144N, D144A, D191N, H271A, H287A and D191N/H271A) of Gro1PDH fromAeropyrum pernixK1 and examined their characteristics to clarify the active site of this enzyme. The enzyme was found to be a zinc-dependent metalloenzyme, containing one zinc ion for every monomer protein that was essential for activity. Site-directed mutagenesis of D144 increased the activity of the enzyme. Mutants D144N and D144A exhibited low affinity for the substrates and higher activity than the wild type, but their affinity for the zinc ion was the same as that of the wild type. Mutants D191N, H271A and H287A had a low affinity for the zinc ion and a low activity compared with the wild type. The double mutation, D191N/ H271A, had no enzyme activity and bound no zinc. From these results, it was clarified that residues D191, H271 and H287 participate in the catalytic activity of the enzyme by binding the zinc ion, and that D144 has an effect on substrate binding. The structure of the active site of Gro1PDH fromA. pernixK1 seems to be similar to that of glycerol dehydrogenase, despite the differences in substrate specificity and biological role.

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36

Reiss, Y., M. S. Brown, and J. L. Goldstein. "Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme." Journal of Biological Chemistry 267, no. 9 (March 1992): 6403–8. http://dx.doi.org/10.1016/s0021-9258(18)42709-3.

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37

Izrael-Zivkovic, Lidija, Gordana Gojgic-Cvijovic, and Ivanka Karadzic. "Isolation and partial characterization of protease from Pseudomonas aeruginosa ATCC 27853." Journal of the Serbian Chemical Society 75, no. 8 (2010): 1041–52. http://dx.doi.org/10.2298/jsc100125088i.

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Enzymatic characteristics of a protease from medically important, referent strain of Pseudomonas aeruginosa ATCC 27853 were determined. According to SDS PAGE and gel filtration it was estimated that molecular mass of the purified enzyme was about 15 kDa. Other enzymatic properties were found to be: pH optimum 7.1, pH stability between pH 6.5 and pH 10; temperature optimum around 60?C while the enzyme was stable at 60?C for 30 min. The inhibition of the enzyme was observed with the metal chelators such as EDTA and 1,10- phenanthroline, suggesting that the protease is a metalloenzyme. Further more it was determined that enzyme contains one mole of zinc ion per mole of enzyme. The protease is stable in the presence of different organic solvents, which enable potential use for synthesis of peptides.

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38

Huwiler, Simona G., Claudia Löffler, Sebastian E. L. Anselmann, Hans-Joachim Stärk, Martin von Bergen, Jennifer Flechsler, Reinhard Rachel, and Matthias Boll. "One-megadalton metalloenzyme complex inGeobacter metallireducensinvolved in benzene ring reduction beyond the biological redox window." Proceedings of the National Academy of Sciences 116, no. 6 (January 23, 2019): 2259–64. http://dx.doi.org/10.1073/pnas.1819636116.

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Reversible biological electron transfer usually occurs between redox couples at standard redox potentials ranging from +0.8 to −0.5 V. Dearomatizing benzoyl-CoA reductases (BCRs), key enzymes of the globally relevant microbial degradation of aromatic compounds at anoxic sites, catalyze a biological Birch reduction beyond the negative limit of this redox window. The structurally characterized BamBC subunits of class II BCRs accomplish benzene ring reduction at an active-site tungsten cofactor; however, the mechanism and components involved in the energetic coupling of endergonic benzene ring reduction have remained hypothetical. We present a 1-MDa, membrane-associated, Bam[(BC)2DEFGHI]2complex from the anaerobic bacteriumGeobacter metallireducensharboring 4 tungsten, 4 zinc, 2 selenocysteines, 6 FAD, and >50 FeS cofactors. The results suggest that class II BCRs catalyze electron transfer to the aromatic ring, yielding a cyclic 1,5-dienoyl-CoA via two flavin-based electron bifurcation events. This work expands our knowledge of energetic couplings in biology by high-molecular-mass electron bifurcating machineries.

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39

Selvaraj, Ramesh K. "387 Effect of trace minerals (25-hydroxycholecalciferol, Zinc and Manganese) supplementation on the immune responses of livestock." Journal of Animal Science 98, Supplement_4 (November 3, 2020): 169. http://dx.doi.org/10.1093/jas/skaa278.310.

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Abstract Micronutrients such as 25-hydroxycholecalciferol, zinc and manganese are included in livestock feed to achieve optimal growth and improved immune function. Vitamin D (cholecalciferol) modulates immune responses. The effect of Vitamin D on immune cells depends on the subtype of immune cells. Monocytes and macrophages constitutively express Vitamin D receptor and hence 1, 25-dihydroxycholecalciferol increases maturation and the microbicidal activity of macrophages by increasing the production of nitric oxide, antimicrobial proteins and inflammatory cytokines and eventually acts to stimulate the innate immune system. On the other hand, 1,25-dihydroxycholecalciferol suppresses the action of adaptive immune responses by inducing T regulatory cells and increasing the production of IL-10. Superoxide dismutases (SOD) catalyzes conversion of superoxide radicals to oxygen and hydrogen peroxide and is considered a major antioxidant defense system in livestock. SOD is a metalloenzyme with zinc, copper, and manganese as a cofactor. Though trace minerals have traditionally been supplemented in animal diets as inorganic salts such as zinc sulfate and manganese sulfate, other forms of trace minerals have recently been promoted owing to better stability, bioavailability and absorption. Feeding layer diets marginally deficient in zinc and manganese as sulfates decreased the SOD activity, spleen, IL-1 and cathelicidin relative mRNA levels and supplementing zinc and manganese as hydroxychloride (OHCl) reversed the decrease in SOD activity, spleen IL-1 and cathelicidin relative mRNA levels. Feeding broiler diets low in zinc and manganese as sulfates decreased SOD activity, while supplementing the feed with ZnOHCl reversed the decrease in SOD. Increasing the MnOHCl in birds fed higher amounts of ZnOHCl further increased the SOD activity suggesting synergistic effects between ZnOHCl and MnOHCl on SOD activity and IL-1 production. In conclusion, micronutrients act to modify the immune response in livestock, and the form of micronutrients fed can increase the bioavailability of the micronutrients to improve the immune response.

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Huang, Kai-Fa, Yi-Liang Liu, and Andrew H. J. Wang. "Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: A single zinc metalloenzyme." Protein Expression and Purification 43, no. 1 (September 2005): 65–72. http://dx.doi.org/10.1016/j.pep.2005.02.020.

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41

Krosky, Daniel J., Richard Alm, Mikael Berg, Gilles Carmel, Peter J. Tummino, Bo Xu, and Wei Yang. "Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1594, no. 2 (February 2002): 297–306. http://dx.doi.org/10.1016/s0167-4838(01)00319-3.

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Singh, Manoj Kumar, Zhen T. Chu, and Arieh Warshel. "Simulating the Catalytic Effect of a Designed Mononuclear Zinc Metalloenzyme that Catalyzes the Hydrolysis of Phosphate Triesters." Journal of Physical Chemistry B 118, no. 42 (October 13, 2014): 12146–52. http://dx.doi.org/10.1021/jp507592g.

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43

Basbous, Jihane, Antoine Aze, Laurent Chaloin, Rana Lebdy, Dana Hodroj, Cyril Ribeyre, Marion Larroque, et al. "Dihydropyrimidinase protects from DNA replication stress caused by cytotoxic metabolites." Nucleic Acids Research 48, no. 4 (December 19, 2019): 1886–904. http://dx.doi.org/10.1093/nar/gkz1162.

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Abstract Imbalance in the level of the pyrimidine degradation products dihydrouracil and dihydrothymine is associated with cellular transformation and cancer progression. Dihydropyrimidines are degraded by dihydropyrimidinase (DHP), a zinc metalloenzyme that is upregulated in solid tumors but not in the corresponding normal tissues. How dihydropyrimidine metabolites affect cellular phenotypes remains elusive. Here we show that the accumulation of dihydropyrimidines induces the formation of DNA–protein crosslinks (DPCs) and causes DNA replication and transcriptional stress. We used Xenopus egg extracts to recapitulate DNA replication invitro. We found that dihydropyrimidines interfere directly with the replication of both plasmid and chromosomal DNA. Furthermore, we show that the plant flavonoid dihydromyricetin inhibits human DHP activity. Cellular exposure to dihydromyricetin triggered DPCs-dependent DNA replication stress in cancer cells. This study defines dihydropyrimidines as potentially cytotoxic metabolites that may offer an opportunity for therapeutic-targeting of DHP activity in solid tumors.

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Farsa, Oldřich, Veronika Ballayová, Radka Žáčková, Peter Kollar, Tereza Kauerová, and Peter Zubáč. "Aminopeptidase N Inhibitors as Pointers for Overcoming Antitumor Treatment Resistance." International Journal of Molecular Sciences 23, no. 17 (August 29, 2022): 9813. http://dx.doi.org/10.3390/ijms23179813.

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Aminopeptidase N (APN), also known as CD13 antigen or membrane alanyl aminopeptidase, belongs to the M1 family of the MA clan of zinc metallopeptidases. In cancer cells, the inhibition of aminopeptidases including APN causes the phenomenon termed the amino acid deprivation response (AADR), a stress response characterized by the upregulation of amino acid transporters and synthetic enzymes and activation of stress-related pathways such as nuclear factor kB (NFkB) and other pro-apoptotic regulators, which leads to cancer cell death by apoptosis. Recently, APN inhibition has been shown to augment DR4-induced tumor cell death and thus overcome resistance to cancer treatment with DR4-ligand TRAIL, which is available as a recombinant soluble form dulanermin. This implies that APN inhibitors could serve as potential weapons for overcoming cancer treatment resistance. In this study, a series of basically substituted acetamidophenones and the semicarbazones and thiosemicarbazones derived from them were prepared, for which APN inhibitory activity was determined. In addition, a selective anti-proliferative activity against cancer cells expressing APN was demonstrated. Our semicarbazones and thiosemicarbazones are the first compounds of these structural types of Schiff bases that were reported to inhibit not only a zinc-dependent aminopeptidase of the M1 family but also a metalloenzyme.

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Kim, Jin Kyun, Carrie L. Lomelino, Balendu Sankara Avvaru, Brian P. Mahon, Robert McKenna, SangYoun Park, and Chae Un Kim. "Active-site solvent replenishment observed during human carbonic anhydrase II catalysis." IUCrJ 5, no. 1 (January 1, 2018): 93–102. http://dx.doi.org/10.1107/s2052252517017626.

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Human carbonic anhydrase II (hCA II) is a zinc metalloenzyme that catalyzes the reversible hydration/dehydration of CO2/HCO3 −. Although hCA II has been extensively studied to investigate the proton-transfer process that occurs in the active site, its underlying mechanism is still not fully understood. Here, ultrahigh-resolution crystallographic structures of hCA II cryocooled under CO2 pressures of 7.0 and 2.5 atm are presented. The structures reveal new intermediate solvent states of hCA II that provide crystallographic snapshots during the restoration of the proton-transfer water network in the active site. Specifically, a new intermediate water (WI′) is observed next to the previously observed intermediate water WI, and they are both stabilized by the five water molecules at the entrance to the active site (the entrance conduit). Based on these structures, a water network-restructuring mechanism is proposed, which takes place at the active site after the nucleophilic attack of OH− on CO2. This mechanism explains how the zinc-bound water (WZn) and W1 are replenished, which are directly responsible for the reconnection of the His64-mediated proton-transfer water network. This study provides the first `physical' glimpse of how a water reservoir flows into the hCA II active site during its catalytic activity.

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46

Nishimura, Atsuhisa, Hiroshi Oyama, Takatoshi Hamada, Katsunori Nobuoka, Takashi Shin, Sawao Murao, and Kohei Oda. "Molecular Cloning, Sequencing, and Expression inEscherichia coli of the Gene Encoding a Novel 5-Oxoprolinase without ATP-Hydrolyzing Activity from Alcaligenes faecalis N-38A." Applied and Environmental Microbiology 66, no. 8 (August 1, 2000): 3201–5. http://dx.doi.org/10.1128/aem.66.8.3201-3205.2000.

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ABSTRACT The gene encoding a novel 5-oxoprolinase without ATP-hydrolyzing activity from Alcaligenes faecalis N-38A was cloned and characterized. The coding region of this gene is 1,299 bp long. The predicted primary protein is composed of 433 amino acid residues, with a 31-amino-acid signal peptide. The mature protein is composed of 402 amino acid residues with a molecular mass of 46,163 Da. The derived amino acid sequence of the enzyme showed no significant sequence similarity to any other proteins reported so far. The 5-oxoprolinase gene was expressed in Escherichia coli by using a regulatory expression system with an isopropyl-β-d-thiogalactopyranoside-inducibletac promoter, and its expression level was approximately 16 mg per liter. The purified enzyme has the same characteristics as the authentic enzyme, except for the amino terminus, which has three additional amino acids. The enzyme was markedly inhibited byp-chloromercuribenzoic acid, EDTA,o-phenanthroline, HgCl2, and CuSO4. The EDTA-inactivated enzyme was completely restored by the addition of Zn2+ or Co2+. In addition, the enzyme was found to contain 1 g-atom of zinc per mol of protein. These results suggest that the 5-oxoprolinase produced by A. faecalis N-38A is a zinc metalloenzyme.

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Mulrooney, Scott B., and Robert P. Hausinger. "Metal Ion Dependence of Recombinant Escherichia coli Allantoinase." Journal of Bacteriology 185, no. 1 (January 1, 2003): 126–34. http://dx.doi.org/10.1128/jb.185.1.126-134.2003.

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ABSTRACT Allantoinase is a suspected dinuclear metalloenzyme that catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid. Recombinant Escherichia coli allantoinase purified from overproducing cultures amended with 2.5 mM zinc, 1 mM cobalt, or 1 mM nickel ions was found to possess ∼1.4 Zn, 0.0 Co, 0.0 Ni, and 0.4 Fe; 0.1 Zn, 1.0 Co, 0.0 Ni, and 0.2 Fe; and 0.0 Zn, 0.0 Co, 0.6 Ni, and 0.1 Fe per subunit, respectively, whereas protein obtained from nonamended cultures contains near stoichiometric levels of iron. We conclude that allantoinase is incompletely activated in the recombinant cells, perhaps due to an insufficiency of a needed accessory protein. Enzyme isolated from nonsupplemented cultures possesses very low activity (k cat = 34.7 min−1) compared to the zinc-, cobalt-, and nickel-containing forms of allantoinase (k cat values of 5,000 and 28,200 min−1 and 200 min−1, respectively). These rates and corresponding Km values (17.0, 19.5, and 80 mM, respectively) are significantly greater than those that have been reported previously. Absorbance spectroscopy of the cobalt species reveals a band centered at 570 nm consistent with five-coordinate geometry. Dithiothreitol is a competitive inhibitor of the enzyme, with significant Ki differences for the zinc and cobalt species (237 and 795 μM, respectively). Circular dichroism spectroscopy revealed that the zinc enzyme utilizes only the S isomer of allantoin, whereas the cobalt allantoinase prefers the S isomer, but also hydrolyzes the R isomer at about 1/10 the rate. This is the first report for metal content of allantoinase from any source.

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Toyoshima, Manabu, Xuguang Jiang, Tadayuki Ogawa, Tetsuo Ohnishi, Shogo Yoshihara, Shabeesh Balan, Takeo Yoshikawa, and Nobutaka Hirokawa. "Enhanced carbonyl stress induces irreversible multimerization of CRMP2 in schizophrenia pathogenesis." Life Science Alliance 2, no. 5 (October 2019): e201900478. http://dx.doi.org/10.26508/lsa.201900478.

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Enhanced carbonyl stress underlies a subset of schizophrenia, but its causal effects remain elusive. Here, we elucidated the molecular mechanism underlying the effects of carbonyl stress in iPS cells in which the gene encoding zinc metalloenzyme glyoxalase I (GLO1), a crucial enzyme for the clearance of carbonyl stress, was disrupted. The iPS cells exhibited significant cellular and developmental deficits, and hyper-carbonylation of collapsing response mediator protein 2 (CRMP2). Structural and biochemical analyses revealed an array of multiple carbonylation sites in the functional motifs of CRMP2, particularly D-hook (for dimerization) and T-site (for tetramerization), which are critical for the activity of the CRMP2 tetramer. Interestingly, carbonylated CRMP2 was stacked in the multimer conformation by irreversible cross-linking, resulting in loss of its unique function to bundle microtubules. Thus, the present study revealed that the enhanced carbonyl stress stemmed from the genetic aberrations results in neurodevelopmental deficits through the formation of irreversible dysfunctional multimer of carbonylated CRMP2.

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Kalinin, Stanislav, Anna Malkova, Tatiana Sharonova, Vladimir Sharoyko, Alexander Bunev, Claudiu T. Supuran, and Mikhail Krasavin. "Carbonic Anhydrase IX Inhibitors as Candidates for Combination Therapy of Solid Tumors." International Journal of Molecular Sciences 22, no. 24 (December 14, 2021): 13405. http://dx.doi.org/10.3390/ijms222413405.

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Combination therapy is becoming imperative for the treatment of many cancers, as it provides a higher chance of avoiding drug resistance and tumor recurrence. Among the resistance-conferring factors, the tumor microenvironment plays a major role, and therefore, represents a viable target for adjuvant therapeutic agents. Thus, hypoxia and extracellular acidosis are known to select for the most aggressive and resilient phenotypes and build poorly responsive regions of the tumor mass. Carbonic anhydrase (CA, EC 4.2.1.1) IX isoform is a surficial zinc metalloenzyme that is proven to play a central role in regulating intra and extracellular pH, as well as modulating invasion and metastasis processes. With its strong association and distribution in various tumor tissues and well-known druggability, this protein holds great promise as a target to pharmacologically interfere with the tumor microenvironment by using drug combination regimens. In the present review, we summarized recent publications revealing the potential of CA IX inhibitors to intensify cancer chemotherapy and overcome drug resistance in preclinical settings.

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Holt, Jason A., Edward P. Garvey, J. David Becherer, William J. Hoekstra, Robert J. Schotzinger, and Christopher M. Yates. "SE-7552, a Highly Selective, Non-Hydroxamate Inhibitor of Histone Deacetylase-6 Blocks Multiple Myeloma Growth In Vivo." Blood 132, Supplement 1 (November 29, 2018): 3215. http://dx.doi.org/10.1182/blood-2018-99-113066.

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Abstract Despite recent advances, disease progression and treatment resistance in multiple myeloma (MM) remains a significant challenge. Current therapies include proteasome inhibitors, immunomodulatory agents, monoclonal antibodies and more recently histone deacetylase (HDAC) inhibitors. Many HDAC inhibitors have progressed into clinical development, however, there has been limited success with the approval of only three pan-HDAC inhibitors (SAHA, belinostat and panobinostat) and the class I selective inhibitor, romidepsin. A challenge to the development of HDAC inhibitors has been the management of toxicities, many of which are dose limiting. Some of these toxicities can be attributed to the use of the hydroxamate, a potent zinc binding group that has been associated with toxicity and poor pharmacokinetic (PK) properties. The very tight binding potency of the hydroxamate to zinc also leads to limited HDAC isoform selectivity and thus further predisposes to toxicity. HDAC6, a member of the class IIb HDAC family, is a target of high interest and has significant therapeutic potential in oncology, particularly MM. It has a unique protein structure and is predominantly located in the cytoplasm where it has multiple non-histone protein substrates including α-tubulin, HSP90, cortactin, and Foxp3. Here, we describe the identification of a highly selective, non-hydroxamate HDAC6 inhibitor with excellent PK properties capable of inhibiting MM growth in vivo. Extensive medicinal chemistry exploration and optimization led to the discovery of a zinc-binding group that was associated with excellent potency and selectivity for HDAC6. Additional optimization of the chemical scaffold led to the identification of SE-7552, a compound with an IC50 of 33nM against HDAC6 and greater than 850-fold selectivity versus all other known HDAC isozymes. SE-7552 demonstrated superior PK compared to hydroxamate-based HDAC inhibitors, with a maximum exposure of 597 ng/ml and a half-life of 7.2 hours after a single oral dose of 5 mg/kg in the mouse. To characterize inhibition of HDAC6 in vivo, acetylated α-tubulin (a biomarker for HDAC6 inhibition) was measured in the spleen of mice treated with SE-7552 or the hydroxamate-based HDAC6 inhibitor, ricolinostat. After a single oral dose of SE-7552 at 30 mg/kg, levels of acetylated α-tubulin were increased for over 24 hours, whereas ricolinostat at a 50 mg/kg IP dose showed increased levels for less than 8 hours. In the same study, SE-7552 had no effect on the acetylation of H3 (a biomarker for inhibition of Class I HDACs), whereas ricolinostat increased the levels of acetylated H3. Based on the positive in vitro and in vivo profile, SE-7552 was progressed into pre-clinical rodent models of MM. Since previously studied HDAC6 inhibitors were not able to significantly inhibit MM growth as monotherapy, SE-7552 was co-administered with either pomalidomide or bortezomib. In a subcutaneous MM model using human H929 MM cells, SE-7552 dosed orally at 10 mg/kg daily in combination with pomalidomide dosed at 1 mg/kg IP daily significantly delayed tumor growth in comparison to pomalidomide alone (p < 0.01), as well as enhanced the survival of the mice. Utilizing human MM.1S cells that can be quantified by luminescence, a disseminated model of MM was conducted in which SE-7552 dosed orally at 10 mg/kg daily in combination with bortezomib dosed at 1.5 mg/kg IP once a week significantly delayed tumor growth compared to bortezomib alone (p < 0.05). In summary, we have identified a non-hydroxamate HDAC6 inhibitor, SE-7552, with superior selectivity and pharmacokinetics compared to current HDAC6 inhibitors. SE-7552 demonstrated high levels of selectivity in an in vivo biomarker study and blocked MM growth in two pre-clinical models when co-administered with current MM therapies. Disclosures Holt: Selenity Therapeutics: Employment, Equity Ownership, Patents & Royalties: METALLOENZYME INHIBITOR COMPOUNDS, U.S. Patent Application No.: 15/917,555 (March 9, 2018). Garvey:Selenity Therapeutics: Employment, Equity Ownership. Becherer:Selenity Therapeutics: Employment, Equity Ownership. Hoekstra:Selenity Therapeutics: Employment, Equity Ownership, Patents & Royalties: METALLOENZYME INHIBITOR COMPOUNDS, U.S. Patent Application No.: 15/917,555 (March 9, 2018). Schotzinger:Mycovia Pharma: Membership on an entity's Board of Directors or advisory committees; Innocrin Pharma: Equity Ownership, Membership on an entity's Board of Directors or advisory committees; Selenity Therapeutics: Employment, Equity Ownership, Membership on an entity's Board of Directors or advisory committees, Patents & Royalties: METALLOENZYME INHIBITOR COMPOUNDS, U.S. Patent Application No.: 15/917,555 (March 9, 2018). Yates:Selenity Therapeutics: Employment, Equity Ownership, Patents & Royalties: METALLOENZYME INHIBITOR COMPOUNDS, U.S. Patent Application No.: 15/917,555 (March 9, 2018).

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