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Relevant bibliographies by topics / NADP-bound

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Academic literature on the topic 'NADP-bound'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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Journal articles on the topic "NADP-bound"

1

GAETANI, Gian F., Anna M. FERRARIS, Paola SANNA, and Henry N. KIRKMAN. "A novel NADPH:(bound) NADP+ reductase and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase." Biochemical Journal 385, no. 3 (January 24, 2005): 763–68. http://dx.doi.org/10.1042/bj20041495.

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Many catalases have the shared property of containing bound NADPH and being susceptible to inactivation by their own substrate, H2O2. The presence of additional (unbound) NADPH effectively prevents bovine liver and human erythrocytic catalase from becoming compound II, the reversibly inactivated state of catalase, and NADP+ is known to be generated in the process. The function of the bound NADPH, which is tightly bound in bovine liver catalase, has been unknown. The present study with bovine liver catalase and [14C]NADPH and [14C]NADH revealed that unbound NADPH or NADH are substrates for an internal reductase and transhydrogenase reaction respectively; the unbound NADPH or NADH cause tightly bound NADP+ to become NADPH without becoming tightly bound themselves. This and other results provide insight into the function of tightly bound NADPH.

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2

Kondo, Hisanori, and Midori Murakami. "Crystal Structures of the Putative Isocitrate Dehydrogenase from Sulfolobus tokodaii Strain 7 in the Apo and NADP+-Bound Forms." Archaea 2018 (December 19, 2018): 1–9. http://dx.doi.org/10.1155/2018/7571984.

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Isocitrate dehydrogenase is a catabolic enzyme that acts during the third step of the tricarboxylic acid cycle. The hypothetical protein ST2166 from the archaeon Sulfolobus tokodaii was isolated and crystallized. It shares high primary structure homology with prokaryotic NADP+-dependent IDHs, suggesting that these enzymes share a common enzymatic mechanism. The crystal structure of ST2166 was determined at 2.0 Å resolution in the apo form, and then the structure of the crystal soaked with NADP+ was also determined at 2.4 Å resolution, which contained NADP+ bound at the putative active site. Comparisons between the structures of apo and NADP+-bound forms and NADP-IDHs from other prokaryotes suggest that prokaryotic NADP-IDHs recognize their cofactors using conserved Lys335, Tyr336, and Arg386 in ST2166 at the opening cleft before the domain closure.

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3

Verma, Rajni, Jonathan M. Ellis, and Katie R. Mitchell-Koch. "Dynamic Preference for NADP/H Cofactor Binding/Release in E. coli YqhD Oxidoreductase." Molecules 26, no. 2 (January 7, 2021): 270. http://dx.doi.org/10.3390/molecules26020270.

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YqhD, an E. coli alcohol/aldehyde oxidoreductase, is an enzyme able to produce valuable bio-renewable fuels and fine chemicals from a broad range of starting materials. Herein, we report the first computational solution-phase structure-dynamics analysis of YqhD, shedding light on the effect of oxidized and reduced NADP/H cofactor binding on the conformational dynamics of the biocatalyst using molecular dynamics (MD) simulations. The cofactor oxidation states mainly influence the interdomain cleft region conformations of the YqhD monomers, involved in intricate cofactor binding and release. The ensemble of NADPH-bound monomers has a narrower average interdomain space resulting in more hydrogen bonds and rigid cofactor binding. NADP-bound YqhD fluctuates between open and closed conformations, while it was observed that NADPH-bound YqhD had slower opening/closing dynamics of the cofactor-binding cleft. In the light of enzyme kinetics and structural data, simulation findings have led us to postulate that the frequently sampled open conformation of the cofactor binding cleft with NADP leads to the more facile release of NADP while increased closed conformation sampling during NADPH binding enhances cofactor binding affinity and the aldehyde reductase activity of the enzyme.

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4

Verma, Rajni, Jonathan M. Ellis, and Katie R. Mitchell-Koch. "Dynamic Preference for NADP/H Cofactor Binding/Release in E. coli YqhD Oxidoreductase." Molecules 26, no. 2 (January 7, 2021): 270. http://dx.doi.org/10.3390/molecules26020270.

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Abstract:

YqhD, an E. coli alcohol/aldehyde oxidoreductase, is an enzyme able to produce valuable bio-renewable fuels and fine chemicals from a broad range of starting materials. Herein, we report the first computational solution-phase structure-dynamics analysis of YqhD, shedding light on the effect of oxidized and reduced NADP/H cofactor binding on the conformational dynamics of the biocatalyst using molecular dynamics (MD) simulations. The cofactor oxidation states mainly influence the interdomain cleft region conformations of the YqhD monomers, involved in intricate cofactor binding and release. The ensemble of NADPH-bound monomers has a narrower average interdomain space resulting in more hydrogen bonds and rigid cofactor binding. NADP-bound YqhD fluctuates between open and closed conformations, while it was observed that NADPH-bound YqhD had slower opening/closing dynamics of the cofactor-binding cleft. In the light of enzyme kinetics and structural data, simulation findings have led us to postulate that the frequently sampled open conformation of the cofactor binding cleft with NADP leads to the more facile release of NADP while increased closed conformation sampling during NADPH binding enhances cofactor binding affinity and the aldehyde reductase activity of the enzyme.

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5

Lobley, Carina M. C., Alessio Ciulli, Heather M. Whitney, Glyn Williams, Alison G. Smith, Chris Abell, and Tom L. Blundell. "The Crystal Structure ofEscherichia coliKetopantoate Reductase with NADP+Bound†,‡." Biochemistry 44, no. 25 (June 2005): 8930–39. http://dx.doi.org/10.1021/bi0502036.

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6

OKUDA, Keiko, Itaru URABE, and Hirosuke OKADA. "Synthesis of poly(ethylene glycol)-bound NADP by selective modification at the 6-amino group of NADP." European Journal of Biochemistry 151, no. 1 (August 1985): 33–38. http://dx.doi.org/10.1111/j.1432-1033.1985.tb09065.x.

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7

Padyana, Anil K., and Stephen K. Burley. "Crystal Structure of Shikimate 5-Dehydrogenase (SDH) Bound to NADP." Structure 11, no. 8 (August 2003): 1005–13. http://dx.doi.org/10.1016/s0969-2126(03)00159-x.

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8

Brito, Rui M. M., Frederick B. Rudolph, and Paul R. Rosevear. "Conformation of NADP+ bound to a type II dihydrofolate reductase." Biochemistry 30, no. 6 (February 12, 1991): 1461–69. http://dx.doi.org/10.1021/bi00220a003.

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9

Anderlund, Mikael, Torben L. Nissen, Jens Nielsen, John Villadsen, Jan Rydström, Bärbel Hahn-Hägerdal, and Morten C. Kielland-Brandt. "Expression of the Escherichia coli pntA andpntB Genes, Encoding Nicotinamide Nucleotide Transhydrogenase, in Saccharomyces cerevisiae and Its Effect on Product Formation during Anaerobic Glucose Fermentation." Applied and Environmental Microbiology 65, no. 6 (June 1, 1999): 2333–40. http://dx.doi.org/10.1128/aem.65.6.2333-2340.1999.

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ABSTRACT We studied the physiological effect of the interconversion between the NAD(H) and NADP(H) coenzyme systems in recombinantSaccharomyces cerevisiae expressing the membrane-bound transhydrogenase from Escherichia coli. Our objective was to determine if the membrane-bound transhydrogenase could work in reoxidation of NADH to NAD+ in S. cerevisiaeand thereby reduce glycerol formation during anaerobic fermentation. Membranes isolated from the recombinant strains exhibited reduction of 3-acetylpyridine-NAD+ by NADPH and by NADH in the presence of NADP+, which demonstrated that an active enzyme was present. Unlike the situation in E. coli, however, most of the transhydrogenase activity was not present in the yeast plasma membrane; rather, the enzyme appeared to remain localized in the membrane of the endoplasmic reticulum. During anaerobic glucose fermentation we observed an increase in the formation of 2-oxoglutarate, glycerol, and acetic acid in a strain expressing a high level of transhydrogenase, which indicated that increased NADPH consumption and NADH production occurred. The intracellular concentrations of NADH, NAD+, NADPH, and NADP+were measured in cells expressing transhydrogenase. The reduction of the NADPH pool indicated that the transhydrogenase transferred reducing equivalents from NADPH to NAD+.

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10

Liu, Si-Qi, Hongjun Jin, Albert Zacarias, Sanjay Srivastava, and Aruni Bhatnagar. "Binding of Pyridine Nucleotide Coenzymes to the β-Subunit of the Voltage-sensitive K+Channel." Journal of Biological Chemistry 276, no. 15 (January 17, 2001): 11812–20. http://dx.doi.org/10.1074/jbc.m008259200.

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The β-subunit of the voltage-sensitive K+(Kv) channels belongs to the aldo-keto reductase superfamily, and the crystal structure of Kvβ2 shows NADP bound in its active site. Here we report that Kvβ2 displays a high affinity for NADPH (Kd= 0.1 μm) and NADP+(Kd= 0.3 μm), as determined by fluorometric titrations of the recombinant protein. The Kvβ2 also bound NAD(H) but with 10-fold lower affinity. The site-directed mutants R264E and N333W did not bind NADPH, whereas, theKdNADPHof Q214R was 10-fold greater than the wild-type protein. TheKdNADPHwas unaffected by the R189M, W243Y, W243A, or Y255F mutation. The tetrameric structure of the wild-type protein was retained by the R264E mutant, indicating that NADPH binding is not a prerequisite for multimer formation. A C248S mutation caused a 5-fold decrease inKdNADPH, shifted the pKaofKdNADPHfrom 6.9 to 7.4, and decreased the ionic strength dependence of NADPH binding. These results indicate that Arg-264 and Asn-333 are critical for coenzyme binding, which is regulated in part by Cys-248. The binding of both NADP(H) and NAD(H) to the protein suggests that several types of Kvβ2-nucleotide complexes may be formedin vivo.

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Dissertations / Theses on the topic "NADP-bound"

1

Naylor, Claire. "X-ray crystallographic studies of glucose 6-phosphate dehydrogenase." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.360467.

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Book chapters on the topic "NADP-bound"

1

Matthijs, Hans C. P., Sean J. Coughlan, and Geoffrey Hind. "Ferredoxin-NADP+ Oxidoreductase: Studies on the Thylakoid Membrane Bound Enzyme." In Progress in Photosynthesis Research, 545–48. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3535-8_129.

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2

Nielsen, Hanne Linde, Birgitte Andersen, and Henrik Vibe Scheller. "Ferredoxin:NADP+ Reductase Bound to the PSI-E Subunit of Photosystem I is Inefficient in NADP+-Reduction but Catalyzes the Reduction of Quinones." In Photosynthesis: from Light to Biosphere, 1825–28. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_427.

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3

"Two Bound Forms of Ferredoxin-NADP Reductase in Chloroplast Thylakoids." In Flavins and Flavoproteins 1993, 413–22. De Gruyter, 1994. http://dx.doi.org/10.1515/9783110885774-070.

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