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Journal articles on the topic 'Triosephosphate isomerases'

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Published: 4 June 2021

Last updated: 2 February 2022

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1

Walden, H., G. Taylor, H. Lilie, T. Knura, and R. Hensel. "Triosephosphate isomerase of the hyperthermophile Thermoproteus tenax: thermostability is not everything." Biochemical Society Transactions 32, no. 2 (April 1, 2004): 305. http://dx.doi.org/10.1042/bst0320305.

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The triosephosphate isomerase of the hyperthermophilic crenarchaeum Thermoproteus tenax (TtxTIM) represents a homomeric tetramer. Unlike the triosephosphate isomerases of other hyperthermophiles, however, the association of the TtxTIM tetramers is looser, allowing a reversible dissociation into inactive dimers. The dimer/tetramer equilibrium of TtxTIM is shifted to the tetrameric state through a specific interaction with glycerol-1-phosphate dehydrogenase of T. tenax, suggesting that higher oligomerization of the TtxTIM serves functional rather than stabilizing purposes.

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2

Áabrahám, Magdolna, A. Alexin, and B. Szajáni. "Immobilized triosephosphate isomerases a comparative study." Applied Biochemistry and Biotechnology 36, no. 1 (July 1992): 1–12. http://dx.doi.org/10.1007/bf02950771.

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3

Zhang, Y., K. U. Yuksel, and R. W. Gracy. "Terminal Marking of Avian Triosephosphate Isomerases by Deamidation and Oxidation." Archives of Biochemistry and Biophysics 317, no. 1 (February 1995): 112–20. http://dx.doi.org/10.1006/abbi.1995.1142.

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4

Del Buono, Daniele, Bhakti Prinsi, Luca Espen, and Luciano Scarponi. "Triosephosphate Isomerases in Italian Ryegrass (Lolium multiflorum): Characterization and Susceptibility to Herbicides." Journal of Agricultural and Food Chemistry 57, no. 17 (September 9, 2009): 7924–30. http://dx.doi.org/10.1021/jf901681q.

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5

FIGUEROA-ANGULO, ELISA E., PRISCILA ESTRELLA-HERNÁNDEZ, HOLJES SALGADO-LUGO, ADRIÁN OCHOA-LEYVA, ARMANDO GÓMEZ PUYOU, SILVIA S. CAMPOS, GABRIELA MONTERO-MORAN, et al. "Cellular and biochemical characterization of two closely related triosephosphate isomerases from Trichomonas vaginalis." Parasitology 139, no. 13 (August 29, 2012): 1729–38. http://dx.doi.org/10.1017/s003118201200114x.

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SUMMARYThe glycolytic enzyme triosephosphate isomerase catalyses the isomerization between glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Here we report that Trichomonas vaginalis contains 2 fully functional tpi genes. Both genes are located in separated chromosomal context with different promoter regulatory elements and encode ORFs of 254 amino acids; the only differences between them are the character of 4 amino acids located in α-helices 1, 2 and 8. Semi-quantitative RT-PCR assays showed that tpi2 transcript is approximately 3·3-fold more abundant than tpi1. Using an anti-TvTIM2 polyclonal antibody it was demonstrated that TIM proteins have a cytoplasmic localization and both enzymes are able to complement an Escherichia coli strain carrying a deletion of its endogenous tpi gene. Both TIM proteins assemble as dimers and their secondary structure assessment is essentially identical to TIM from Saccharomyces cerevisiae. The kinetic catalytic constants of the recombinant enzymes using glyceraldehyde-3-phosphate as substrate are similar to the catalytic constants of TIMs from other organisms including parasitic protozoa. As T. vaginalis depends on glycolysis for ATP production, we speculate 2 possible reasons to maintain a duplicated tpi copy on its genome: an increase in gene dosage or an early event of neofunctionalization of TIM as a moonlighting protein.

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6

Aguirre, Yolanda, Nallely Cabrera, Beatriz Aguirre, Ruy Pérez-Montfort, Alejandra Hernandez-Santoyo, Horacio Reyes-Vivas, Sergio Enríquez-Flores, et al. "Different contribution of conserved amino acids to the global properties of triosephosphate isomerases." Proteins: Structure, Function, and Bioinformatics 82, no. 2 (October 18, 2013): 323–35. http://dx.doi.org/10.1002/prot.24398.

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7

Blacklow, Stephen C., and Jeremy R. Knowles. "How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases." Biochemistry 29, no. 17 (May 1990): 4099–108. http://dx.doi.org/10.1021/bi00469a012.

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8

Wierenga, R. K., T. V. Borcher, and M. E. M. Noble. "Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues." FEBS Letters 307, no. 1 (July 27, 1992): 34–39. http://dx.doi.org/10.1016/0014-5793(92)80897-p.

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9

Rodríguez-Bolaños, Monica, Nallely Cabrera, and Ruy Perez-Montfort. "Identification of the critical residues responsible for differential reactivation of the triosephosphate isomerases of two trypanosomes." Open Biology 6, no. 10 (October 2016): 160161. http://dx.doi.org/10.1098/rsob.160161.

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The reactivation of triosephosphate isomerase (TIM) from unfolded monomers induced by guanidine hydrochloride involves different amino acids of its sequence in different stages of protein refolding. We describe a systematic mutagenesis method to find critical residues for certain physico-chemical properties of a protein. The two similar TIMs of Trypanosoma brucei and Trypanosoma cruzi have different reactivation velocities and efficiencies. We used a small number of chimeric enzymes, additive mutants and planned site-directed mutants to produce an enzyme from T. brucei with 13 mutations in its sequence, which reactivates fast and efficiently like wild-type (WT) TIM from T. cruzi , and another enzyme from T. cruzi, with 13 slightly altered mutations, which reactivated slowly and inefficiently like the WT TIM of T. brucei . Our method is a shorter alternative to random mutagenesis, saturation mutagenesis or directed evolution to find multiple amino acids critical for certain properties of proteins.

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10

GAO, Xiu-Gong, Georgina GARZA-RAMOS, Emma SAAVEDRA-LIRA, Nallely CABRERA, Marietta T. de GÓMEZ-PUYOU, Ruy PEREZ-MONTFORT, and Armando GÓMEZ-PUYOU. "Reactivation of triosephosphate isomerase from three trypanosomatids and human: effect of Suramin." Biochemical Journal 332, no. 1 (May 15, 1998): 91–96. http://dx.doi.org/10.1042/bj3320091.

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The reactivation of the homodimeric triosephosphate isomerases (TIMs) from Trypanosoma brucei, T. cruzi, Leishmania mexicana and humans was determined after their denaturation with guanidine hydrochloride. In the range of 2–32 µg of T. brucei TIM per ml and 0.2–5 µg of the other enzymes per ml, the rate and extent of TIM reactivation depended on protein concentration, indicating that at these protein concentrations, the rate-limiting step of reactivation is monomer association and not monomer folding. The rate of monomer association was more than one order of magnitude lower in the T. brucei enzyme than in the other three enzymes. Suramin is a drug of choice in the treatment of sleeping sickness, but its mechanism of action is not known. At micromolar concentrations, Suramin inhibited the reactivation of the four enzymes, but the extent of inhibition by Suramin decreased with increasing protein concentration as consequence of a diminution of the life time of the folded monomer. Since the life time of the monomer of T. brucei TIM is longer than that of the other enzymes, Suramin is a more effective inhibitor of the reactivation of TIM from T. brucei, particularly at monomer concentrations above 1 µg of protein per ml (monomer concentration approx. 37 nM). Compounds that are structurally related to Suramin also inhibit TIM reactivation; their effect was about five times more pronounced in the enzyme from T. brucei than in human TIM.

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11

Iwahara, Kazunobu, Reiji Takahashi, Tatsuya Naomi, Makoto Kida, Rie Miyamoto, and Tatsuaki Tokuyama. "Purification and comparison of triosephosphate isomerases from ammonia-oxidizing bacteria isolated from terrestrial and marine environments." Journal of Bioscience and Bioengineering 91, no. 6 (January 2001): 603–6. http://dx.doi.org/10.1016/s1389-1723(01)80182-1.

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12

Henze, Katrin, Claus Schnarrenberger, Josef Kellermann, and William Martin. "Chloroplast and cytosolic triosephosphate isomerases from spinach: purification, microsequencing and cDNA cloning of the chloroplast enzyme." Plant Molecular Biology 26, no. 6 (December 1994): 1961–73. http://dx.doi.org/10.1007/bf00019506.

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13

García-Torres, Itzhel, Nallely Cabrera, Alfredo Torres-Larios, Mónica Rodríguez-Bolaños, Selma Díaz-Mazariegos, Armando Gómez-Puyou, and Ruy Perez-Montfort. "Identification of Amino Acids that Account for Long-Range Interactions in Two Triosephosphate Isomerases from Pathogenic Trypanosomes." PLoS ONE 6, no. 4 (April 18, 2011): e18791. http://dx.doi.org/10.1371/journal.pone.0018791.

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14

Guzmán-Luna, Valeria, Andrea G. Quezada, A. Jessica Díaz-Salazar, Nallely Cabrera, Ruy Pérez-Montfort, and Miguel Costas. "The effect of specific proline residues on the kinetic stability of the triosephosphate isomerases of two trypanosomes." Proteins: Structure, Function, and Bioinformatics 85, no. 4 (February 3, 2017): 571–79. http://dx.doi.org/10.1002/prot.25231.

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15

Rodríguez-Bolaños, Monica, Nallely Cabrera, and Ruy Perez-Montfort. "Correction to ‘Identification of the critical residues responsible for differential reactivation of the triosephosphate isomerases of two trypanosomes’." Open Biology 6, no. 11 (November 2016): 160294. http://dx.doi.org/10.1098/rsob.160294.

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16

Lara-González, Samuel, Priscila Estrella-Hernández, Adrián Ochoa-Leyva, María del Carmen Portillo-Téllez, Luis A. Caro-Gómez, Elisa E. Figueroa-Angulo, Holjes Salgado-Lugo, et al. "Structural and thermodynamic folding characterization of triosephosphate isomerases from Trichomonas vaginalis reveals the role of destabilizing mutations following gene duplication." Proteins: Structure, Function, and Bioinformatics 82, no. 1 (August 31, 2013): 22–33. http://dx.doi.org/10.1002/prot.24333.

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17

Delboni, Luis F., Shekhar C. Mande, Stewart Turley, WIM G. J. Hol, Françoise Rentier-Delrue, Véronique Mainfroid, Joseph A. Martial, and Frederique M. D. Vellieux. "Crystal structure of recombinant triosephosphate isomerase frombacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions." Protein Science 4, no. 12 (December 1995): 2594–604. http://dx.doi.org/10.1002/pro.5560041217.

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18

Jimenez-Sandoval, Pedro, Eduardo Castro-Torres, Rogelio González-González, Corina Díaz-Quezada, Misraim Gurrola, Laura D. Camacho-Manriquez, Lucia Leyva-Navarro, and Luis G. Brieba. "Crystal structures of Triosephosphate Isomerases from Taenia solium and Schistosoma mansoni provide insights for vaccine rationale and drug design against helminth parasites." PLOS Neglected Tropical Diseases 14, no. 1 (January 10, 2020): e0007815. http://dx.doi.org/10.1371/journal.pntd.0007815.

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19

Díaz-Mazariegos, Selma, Nallely Cabrera, and Ruy Perez-Montfort. "Three unrelated and unexpected amino acids determine the susceptibility of the interface cysteine to a sulfhydryl reagent in the triosephosphate isomerases of two trypanosomes." PLOS ONE 13, no. 1 (January 17, 2018): e0189525. http://dx.doi.org/10.1371/journal.pone.0189525.

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20

Chen, Bing, and Jian-Fan Wen. "The adaptive evolution divergence of triosephosphate isomerases between parasitic and free-living flatworms and the discovery of a potential universal target against flatworm parasites." Parasitology Research 109, no. 2 (January 19, 2011): 283–89. http://dx.doi.org/10.1007/s00436-010-2249-4.

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21

Reyes-Vivas, Horacio, Ignacio de la Mora-de la Mora, Adriana Castillo-Villanueva, Lilian Yépez-Mulia, Gloria Hernández-Alcántara, Rosalia Figueroa-Salazar, Itzhel García-Torres, et al. "Giardial Triosephosphate Isomerase as Possible Target of the Cytotoxic Effect of Omeprazole in Giardia lamblia." Antimicrobial Agents and Chemotherapy 58, no. 12 (September 15, 2014): 7072–82. http://dx.doi.org/10.1128/aac.02900-14.

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ABSTRACTGiardiasis is highly prevalent in the developing world, and treatment failures with the standard drugs are common. This work deals with the proposal of omeprazole as a novel antigiardial drug, focusing on a giardial glycolytic enzyme used to follow the cytotoxic effect at the molecular level. We used recombinant technology and enzyme inactivation to demonstrate the capacity of omeprazole to inactivate giardial triosephosphate isomerase, with no adverse effects on its human counterpart. To establish the specific target in the enzyme, we used single mutants of every cysteine residue in triosephosphate isomerase. The effect on cellular triosephosphate isomerase was evaluated by following the remnant enzyme activity on trophozoites treated with omeprazole. The interaction of omeprazole with giardial proteins was analyzed by fluorescence spectroscopy. The susceptibility to omeprazole of drug-susceptible and drug-resistant strains ofGiardia lambliawas evaluated to demonstrate its potential as a novel antigiardial drug. Our results demonstrate that omeprazole inhibits giardial triosephosphate isomerase in a species-specific manner through interaction with cysteine at position 222. Omeprazole enters the cytoplasmic compartment of the trophozoites and inhibits cellular triosephosphate isomerase activity in a dose-dependent manner. Such inhibition takes place concomitantly with the cytotoxic effect caused by omeprazole on trophozoites.G. lambliatriosephosphate isomerase (GlTIM) is a cytoplasmic protein which can help analyses of how omeprazole works against the proteins of this parasite and in the effort to understand its mechanism of cytotoxicity. Our results demonstrate the mechanism of giardial triosephosphate isomerase inhibition by omeprazole and show that this drug is effectivein vitroagainst drug-resistant and drug-susceptible strains ofG. lamblia.

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22

Rodríguez-Bolaños, Mónica, and Ruy Perez-Montfort. "Medical and Veterinary Importance of the Moonlighting Functions of Triosephosphate Isomerase." Current Protein & Peptide Science 20, no. 4 (February 15, 2019): 304–15. http://dx.doi.org/10.2174/1389203719666181026170751.

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Triosephosphate isomerase is the fifth enzyme in glycolysis and its canonical function is the reversible isomerization of glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. Within the last decade multiple other functions, that may not necessarily always involve catalysis, have been described. These include variations in the degree of its expression in many types of cancer and participation in the regulation of the cell cycle. Triosephosphate isomerase may function as an auto-antigen and in the evasion of the immune response, as a factor of virulence of some organisms, and also as an important allergen, mainly in a variety of seafoods. It is an important factor to consider in the cryopreservation of semen and seems to play a major role in some aspects of the development of Alzheimer's disease. It also seems to be responsible for neurodegenerative alterations in a few cases of human triosephosphate isomerase deficiency. Thus, triosephosphate isomerase is an excellent example of a moonlighting protein.

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23

Brown, J. R., I. O. Daar, J. R. Krug, and L. E. Maquat. "Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family." Molecular and Cellular Biology 5, no. 7 (July 1985): 1694–706. http://dx.doi.org/10.1128/mcb.5.7.1694.

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The functional gene and three intronless pseudogenes for human triosephosphate isomerase were isolated from a recombinant DNA library and characterized in detail. The functional gene spans 3.5 kilobase pairs and is split into seven exons. Its promoter contains putative TATA and CCAAT boxes and is extremely rich in G and C residues (76%). The pseudogenes share a high degree of homology with the functional gene but contain mutations that preclude the synthesis of an active triosephosphate isomerase enzyme. Sequence divergence calculations indicate that these pseudogenes arose approximately 18 million years ago. We present evidence that there is a single functional gene in the human triosephosphate isomerase gene family.

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24

Brown, J. R., I. O. Daar, J. R. Krug, and L. E. Maquat. "Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family." Molecular and Cellular Biology 5, no. 7 (July 1985): 1694–706. http://dx.doi.org/10.1128/mcb.5.7.1694-1706.1985.

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The functional gene and three intronless pseudogenes for human triosephosphate isomerase were isolated from a recombinant DNA library and characterized in detail. The functional gene spans 3.5 kilobase pairs and is split into seven exons. Its promoter contains putative TATA and CCAAT boxes and is extremely rich in G and C residues (76%). The pseudogenes share a high degree of homology with the functional gene but contain mutations that preclude the synthesis of an active triosephosphate isomerase enzyme. Sequence divergence calculations indicate that these pseudogenes arose approximately 18 million years ago. We present evidence that there is a single functional gene in the human triosephosphate isomerase gene family.

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25

Oláh, Judit, Ferenc Orosz, László G. Puskás, László Hackler, Margit Horányi, László Polgár, Susan Hollán, and Judit Ovádi. "Triosephosphate isomerase deficiency: consequences of an inherited mutation at mRNA, protein and metabolic levels." Biochemical Journal 392, no. 3 (December 6, 2005): 675–83. http://dx.doi.org/10.1042/bj20050993.

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Triosephosphate isomerase (TPI) deficiency is a unique glycolytic enzymopathy coupled with neurodegeneration. Two Hungarian compound heterozygote brothers inherited the same TPI mutations (F240L and E145Stop), but only the younger one suffers from neurodegeneration. In the present study, we determined the kinetic parameters of key glycolytic enzymes including the mutant TPI for rational modelling of erythrocyte glycolysis. We found that a low TPI activity in the mutant cells (lower than predicted from the protein level and specific activity of the purified recombinant enzyme) is coupled with an increase in the activities of glycolytic kinases. The modelling rendered it possible to establish the steady-state flux of the glycolysis and metabolite concentrations, which was not possible experimentally due to the inactivation of the mutant TPI and other enzymes during the pre-steady state. Our results showed that the flux was 2.5-fold higher and the concentration of DHAP (dihydroxyacetone phosphate) and fructose 1,6-bisphosphate increased 40- and 5-fold respectively in the erythrocytes of the patient compared with the control. Although the rapid equilibration of triosephosphates is not achieved, the energy state of the cells is not ‘sick’ due to the activation of key regulatory enzymes. In lymphocytes of the two brothers, the TPI activity was also lower (20%) than that of controls; however, the remaining activity was high enough to maintain the rapid equilibration of triosephosphates; consequently, no accumulation of DHAP occurs, as judged by our experimental and computational data. Interestingly, we found significant differences in the mRNA levels of the brothers for TPI and some other, apparently unrelated, proteins. One of them is the prolyl oligopeptidase, the activity decrease of which has been reported in well-characterized neurodegenerative diseases. We found that the peptidase activity of the affected brother was reduced by 30% compared with that of his neurologically intact brother.

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26

Åqvist, Johan. "Cold Adaptation of Triosephosphate Isomerase." Biochemistry 56, no. 32 (August 2, 2017): 4169–76. http://dx.doi.org/10.1021/acs.biochem.7b00523.

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27

Harris, Corrie, Bailey Nelson, Darren Farber, Scott Bickel, Heather Huxol, Alexander Asamoah, and Ronald Morton. "Child Neurology: Triosephosphate isomerase deficiency." Neurology 95, no. 24 (September 1, 2020): e3448-e3451. http://dx.doi.org/10.1212/wnl.0000000000010745.

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28

Schneider, Arthur, and Michel Cohen-Solal. "Hematologically Important Mutations: Triosephosphate Isomerase." Blood Cells, Molecules, and Diseases 22, no. 1 (April 1996): 82–84. http://dx.doi.org/10.1006/bcmd.1996.0011.

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29

Orosz, Ferenc, Judit Oláh, and Judit Ovádi. "Reappraisal of triosephosphate isomerase deficiency." European Journal of Haematology 86, no. 3 (June 10, 2010): 265–67. http://dx.doi.org/10.1111/j.1600-0609.2010.01484.x.

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30

Maquat, L. E., R. Chilcote, and P. M. Ryan. "Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man." Journal of Biological Chemistry 260, no. 6 (March 1985): 3748–53. http://dx.doi.org/10.1016/s0021-9258(19)83687-6.

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31

Kim, Nam-Kuk, Seung-Hwan Lee, Da-Jeong Lim, Du-Hak Yoon, Chang-Soo Lee, Oun-Hyun Kim, Hyeong-Cheol Kim, Sung-Jong Oh, and Seong-Koo Hong. "Association of Succinate Dehydrogenase and Triose Phosphate Isomerase Gene Expression with Intramuscular Fat Content in Loin Muscle of Korean (Hanwoo) Cattle." Journal of Life Science 22, no. 1 (January 30, 2012): 31–35. http://dx.doi.org/10.5352/jls.2012.22.1.31.

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32

Li, Xiaohong, Hai-Wei Yang, Hao Chen, Jing Wu, Yehai Liu, and Ji-Fu Wei. "In SilicoPrediction of T and B Cell Epitopes of Der f 25 inDermatophagoides farinae." International Journal of Genomics 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/483905.

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The house dust mites are major sources of indoor allergens for humans, which induce asthma, rhinitis, dermatitis, and other allergic diseases. Der f 25 is a triosephosphate isomerase, representing the major allergen identified inDermatophagoides farinae. The objective of this study was to predict the B and T cell epitopes of Der f 25. In the present study, we analyzed the physiochemical properties, function motifs and domains, and structural-based detailed features of Der f 25 and predicted the B cell linear epitopes of Der f 25 by DNAStar protean system, BPAP, and BepiPred 1.0 server and the T cell epitopes by NetMHCIIpan-3.0 and NetMHCII-2.2. As a result, the sequence and structure analysis identified that Der f 25 belongs to the triosephosphate isomerase family and exhibited a triosephosphate isomerase pattern (PS001371). Eight B cell epitopes (11–18, 30–35, 71–77, 99–107, 132–138, 173–187, 193–197, and 211–224) and five T cell epitopes including 26–34, 38–54, 66–74, 142–151, and 239–247 were predicted in this study. These results can be used to benefit allergen immunotherapies and reduce the frequency of mite allergic reactions.

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33

HELFERT, Sandra, Antonio M. ESTÉVEZ, Barbara BAKKER, Paul MICHELS, and Christine CLAYTON. "Roles of triosephosphate isomerase and aerobic metabolism in Trypanosoma brucei." Biochemical Journal 357, no. 1 (June 25, 2001): 117–25. http://dx.doi.org/10.1042/bj3570117.

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Kinetoplastid protozoa compartmentalize the first seven enzymes of glycolysis and two enzymes of glycerol metabolism in a microbody, the glycosome. While in its mammalian host, Trypanosoma brucei depends entirely on glucose for ATP generation. Under aerobic conditions, most of the glucose is metabolized to pyruvate. Aerobic metabolism depends on the activities of glycosomal triosephosphate isomerase and a mitochondrial glycerophosphate oxidase, and on glycerophosphate ↔ dihydroxyacetone phosphate exchange across the glycosomal membrane. Using a combination of genetics and computer modelling, we show that triosephosphate isomerase is probably essential for bloodstream trypanosome survival, but not for the insect-dwelling procyclics, which preferentially use amino acids as an energy source. When the enzyme level decreased to about 15% of that of the wild-type, the growth rate was halved. Below this level, a lethal rise in dihydroxyacetone phosphate was predicted. Expression of cytosolic triosephosphate isomerase inhibited cell growth. Attempts to knockout the trypanosome alternative oxidase genes (which are needed for glycerophosphate oxidase activity) were unsuccessful, but when we lowered the level of the corresponding mRNA by expressing a homologous double-stranded RNA, oxygen consumption was reduced fourfold and the rate of trypanosome growth was halved.

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34

Kowallik, Wolfgang, Meinolf Thiemann, Yi Huang, Gerard Mutumba, Lisa Beermann, Dagmar Broer, and Norbert Grotjohann. "Complete Sequence of Glycolytic Enzymes in the Mycorrhizal Basidiomycete, Suillus bovinus." Zeitschrift für Naturforschung C 53, no. 9-10 (October 1, 1998): 818–27. http://dx.doi.org/10.1515/znc-1998-9-1007.

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Axenic cultures of Suillus bovinus were cultivated in inorganic liquid medium with glucose as a carbon source at 25 °C and continuous supply of oxygen by aeration with compressed air in the dark. Exogenous fructose as sole carbon source yielded about 50% less increase in dry weight than glucose. This resulted from different uptake velocities. Sucrose as sole exogenous carbon source yielded no measurable increase in dry weight. In glucose cultures, activities of all glycolytic enzymes were found. Maximum specific activities varied largely (from about 60 [fructose 6-phosphate kinase] to about 20 000 [triosephosphate isomerase] nmoles · mg protein-1 · min-1). Apparent Km-values also varied over more than two orders of magnitude (0.035 mᴍ [pyruvate kinase] to 6.16 mᴍ [triosephosphate isomerase]). Fructose 6-phosphate kinase proved to be the fructose 2,6-bisphosphate-regulated type, aldolase the divalent cation-dependent (class II) type and glyceratephosphate mutase the glycerate 2,3-phosphate-independent type of the respective enzymes. Eight of the 10 enzymes exhibited pʜ-optima′ between 7.5-8.0. Triosephosphate isomerase and pyruvate kinase showed highest activities at pʜ 6.5. Regulatory sites within the glycolytic pathway of Suillus bovinus are discussed; fructose 6-phosphate kinase appears to be its main bottle neck.

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35

Blacklow, Stephen C., Ronald T. Raines, Wendell A. Lim, Philip D. Zamore, and Jeremy R. Knowles. "Triosephosphate isomerase catalysis is diffusion controlled." Biochemistry 27, no. 4 (February 23, 1988): 1158–65. http://dx.doi.org/10.1021/bi00404a013.

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36

Bao, Shijun, Danqing Chen, Shengqing Yu, Hongjun Chen, Lei Tan, Meirong Hu, Xusheng Qiu, Cuiping Song, and Chan Ding. "Characterization of triosephosphate isomerase fromMycoplasma gallisepticum." FEMS Microbiology Letters 362, no. 17 (August 27, 2015): fnv140. http://dx.doi.org/10.1093/femsle/fnv140.

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37

Orosz, Ferenc, Judit Oláh, and Judit Ovádi. "Triosephosphate isomerase deficiency: Facts and doubts." IUBMB Life 58, no. 12 (December 2006): 703–15. http://dx.doi.org/10.1080/15216540601115960.

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38

Nguyen, Trang N., Jan Abendroth, David J. Leibly, Kristen P. Le, Wenjin Guo, Angela Kelley, Lance Stewart, Peter J. Myler, and Wesley C. Van Voorhis. "Structure of triosephosphate isomerase fromCryptosporidium parvum." Acta Crystallographica Section F Structural Biology and Crystallization Communications 67, no. 9 (August 16, 2011): 1095–99. http://dx.doi.org/10.1107/s1744309111019178.

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39

Orosz, Ferenc, Beata G. Vértessy, Susan Hollán, Margit Horányi, and Judit Ovádi. "Triosephosphate Isomerase Deficiency: Predictions and Facts." Journal of Theoretical Biology 182, no. 3 (October 1996): 437–47. http://dx.doi.org/10.1006/jtbi.1996.0184.

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40

Poll-The, Bwee Tien, Jean Aicardi, Robert Girot, and R. Rosa. "Nuerological finding in triosephosphate isomerase deficiency." Annals of Neurology 17, no. 5 (May 1985): 439–43. http://dx.doi.org/10.1002/ana.410170504.

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41

Harris, Thomas K. "The mechanistic ventures of triosephosphate isomerase." IUBMB Life 60, no. 3 (2008): 195–98. http://dx.doi.org/10.1002/iub.43.

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42

Arya, R., MR Lalloz, KH Nicolaides, AJ Bellingham, and DM Layton. "Prenatal diagnosis of triosephosphate isomerase deficiency." Blood 87, no. 11 (June 1, 1996): 4507–9. http://dx.doi.org/10.1182/blood.v87.11.4507.bloodjournal87114507.

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First-trimester prenatal diagnosis was undertaken by chorionic villus DNA analysis in two unrelated families with the inherited glycolytic disorder triosephosphate isomerase (TPI) deficiency. The propositus in each family was shown to be homozygous for a missense mutation (GAG --> GAC) at codon 104 of the TPI gene. In the first case the fetus was heterozygous for the codon 104 mutation and therefore clinically unaffected. Prenatal diagnosis in the second case showed the fetus to be homozygous for the codon 104 mutation and thus affected by TPI deficiency. This represents the first molecular diagnosis during early pregnancy of a human glycolytic enzyme disorder.

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43

Zanella, A., M. Mariani, M. B. Colombo, C. Borgna-Pignatti, P. Stefano, G. Morgese, and G. Sirchia. "Triosephosphate isomerase deficiency: 2 new cases." Scandinavian Journal of Haematology 34, no. 5 (April 24, 2009): 417–24. http://dx.doi.org/10.1111/j.1600-0609.1985.tb00771.x.

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44

Kohlhoff, Michael, Anke Dahm, and Reinhard Hensel. "Tetrameric triosephosphate isomerase from hyperthermophilic Archaea." FEBS Letters 383, no. 3 (April 1, 1996): 245–50. http://dx.doi.org/10.1016/0014-5793(96)00249-9.

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45

Wierenga, R. K., E. G. Kapetaniou, and R. Venkatesan. "Triosephosphate isomerase: a highly evolved biocatalyst." Cellular and Molecular Life Sciences 67, no. 23 (August 7, 2010): 3961–82. http://dx.doi.org/10.1007/s00018-010-0473-9.

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46

Degani, Chemda, Ruth El-Batsri, and Shmuel Gazit. "Enzyme Polymorphism in Mango." Journal of the American Society for Horticultural Science 115, no. 5 (September 1990): 844–47. http://dx.doi.org/10.21273/jashs.115.5.844.

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Forty-one (Mangifera indica L.) cultivars were characterized electrophoretically using the isozyme systems aconitase, isocitrate dehydrogenase, leucine aminopeptidase, phosphoglucose isomerase, phosphoglucomutase, and triosephosphate isomerase. The outcross origin of some of the mango cultivars was supported by the isozymic banding patterns. Reported parentage of some other cultivars was not consistent with their isozymic banding patterns.

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47

Romero, Jorge Miguel, María Elena Carrizo, and Juan Agustín Curtino. "Characterization of human triosephosphate isomerase S-nitrosylation." Nitric Oxide 77 (July 2018): 26–34. http://dx.doi.org/10.1016/j.niox.2018.04.004.

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48

Cansu, Sertan, and Pemra Doruker. "Dimerization Affects Collective Dynamics of Triosephosphate Isomerase†." Biochemistry 47, no. 5 (February 2008): 1358–68. http://dx.doi.org/10.1021/bi701916b.

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49

Gayathri, P., Mousumi Banerjee, A. Vijayalakshmi, Shamina Azeez, Hemalatha Balaram, P. Balaram, and M. R. N. Murthy. "Structure of triosephosphate isomerase (TIM) fromMethanocaldococcus jannaschii." Acta Crystallographica Section D Biological Crystallography 63, no. 2 (January 16, 2007): 206–20. http://dx.doi.org/10.1107/s0907444906046488.

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Wilmshurst, Jo M., Grahame A. Wise, John D. Pollard, and Robert A. Ouvrier. "Chronic axonal neuropathy with triosephosphate isomerase deficiency." Pediatric Neurology 30, no. 2 (February 2004): 146–48. http://dx.doi.org/10.1016/s0887-8994(03)00423-5.

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