Chemical Compound Review:
3-phosphoglyceraldehyde (2-hydroxy-3-oxo- propoxy)phosphonic acid
Synonyms:
AG-D-83523, AG-G-10444, CHEBI:17138, G5251_SIGMA, HMDB01112, ...
- Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus. Biesecker, G., Harris, J.I., Thierry, J.C., Walker, J.E., Wonacott, A.J. Nature (1977)
- Nucleotide polymorphism and evolution in the glyceraldehyde-3-phosphate dehydrogenase gene (gapA) in natural populations of Salmonella and Escherichia coli. Nelson, K., Whittam, T.S., Selander, R.K. Proc. Natl. Acad. Sci. U.S.A. (1991)
- Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme. Daar, I.O., Artymiuk, P.J., Phillips, D.C., Maquat, L.E. Proc. Natl. Acad. Sci. U.S.A. (1986)
- Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers. Tokunaga, K., Nakamura, Y., Sakata, K., Fujimori, K., Ohkubo, M., Sawada, K., Sakiyama, S. Cancer Res. (1987)
- Partial revertants of tryptophan synthetase alpha chain active site mutant Asp60-->Asn. Yanofsky, C., Yee, M.C., Horn, V. J. Biol. Chem. (1993)
- The cooperative behavior of yeast D-glyceraldehyde-3-phosphate. Dehydrogenase as studied by the formation of the fluorescent NAD derivative. Xu, G.Q., Zou, C.L., Tsou, C.L. Sci. Sin., Ser. B, Chem. Biol. Agric. Med. Earth Sci. (1984)
- Specific pattern of gene expression during induction of mouse erythroleukemia cells. Fraser, P.J., Curtis, P.J. Genes Dev. (1987)
- 14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells. Cotelle, V., Meek, S.E., Provan, F., Milne, F.C., Morrice, N., MacKintosh, C. EMBO J. (2000)
- Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells. Giegé, P., Heazlewood, J.L., Roessner-Tunali, U., Millar, A.H., Fernie, A.R., Leaver, C.J., Sweetlove, L.J. Plant Cell (2003)
- Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility. Miki, K., Qu, W., Goulding, E.H., Willis, W.D., Bunch, D.O., Strader, L.F., Perreault, S.D., Eddy, E.M., O'Brien, D.A. Proc. Natl. Acad. Sci. U.S.A. (2004)
- Simulation of enzyme-substrate encounter with gated active sites. Wade, R.C., Luty, B.A., Demchuk, E., Madura, J.D., Davis, M.E., Briggs, J.M., McCammon, J.A. Nat. Struct. Biol. (1994)
- Tyrosine quenching of tryptophan phosphorescence in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Strambini, G.B., Gabellieri, E., Gonnelli, M., Rahuel-Clermont, S., Branlant, G. Biophys. J. (1998)
- Folding domains and intramolecular ionic interactions of lysine residues in glyceraldehyde 3-phosphate dehydrogenase. Lambert, J.M., Perham, R.N. Biochem. J. (1977)
- Glyceraldehyde-phosphate dehydrogenase (total and isoenzyme activity) in the early diagnosis of myocardial infarction. Griffiths, J., Shaw, S. Clin. Chem. (1977)
- Arginine residues as stabilizing elements in proteins. Mrabet, N.T., Van den Broeck, A., Van den brande, I., Stanssens, P., Laroche, Y., Lambeir, A.M., Matthijssens, G., Jenkins, J., Chiadmi, M., van Tilbeurgh, H. Biochemistry (1992)
- Escherichia coli open reading frame 696 is idi, a nonessential gene encoding isopentenyl diphosphate isomerase. Hahn, F.M., Hurlburt, A.P., Poulter, C.D. J. Bacteriol. (1999)
- An insulin response element in the glyceraldehyde-3-phosphate dehydrogenase gene binds a nuclear protein induced by insulin in cultured cells and by nutritional manipulations in vivo. Nasrin, N., Ercolani, L., Denaro, M., Kong, X.F., Kang, I., Alexander, M. Proc. Natl. Acad. Sci. U.S.A. (1990)
- cDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase. Shoemaker, C., Gross, A., Gebremichael, A., Harn, D. Proc. Natl. Acad. Sci. U.S.A. (1992)
- Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme. Hermes, J.D., Blacklow, S.C., Knowles, J.R. Proc. Natl. Acad. Sci. U.S.A. (1990)
- Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle. Caswell, A.H., Corbett, A.M. J. Biol. Chem. (1985)
- Association of glyceraldehyde-3-phosphate dehydrogenase with the human red cell membrane. A kinetic analysis. Kliman, H.J., Steck, T.L. J. Biol. Chem. (1980)
- Erythrocyte glycolysis and its marked alterations by muscular exercise in type VII glycogenosis. Shimizu, T., Kono, N., Kiyokawa, H., Yamada, Y., Hara, N., Mineo, I., Kawachi, M., Nakajima, H., Wang, Y.L., Tarui, S. Blood (1988)
- Binding of glycolytic enzymes to cardiac sarcolemmal and sarcoplasmic reticular membranes. Pierce, G.N., Philipson, K.D. J. Biol. Chem. (1985)
- Ketone bodies stimulate chaperone-mediated autophagy. Finn, P.F., Dice, J.F. J. Biol. Chem. (2005)
- Tungsten in biological systems. Kletzin, A., Adams, M.W. FEMS Microbiol. Rev. (1996)
- Role of adenine ring and adenine ribose of nicotinamide adenine dinucleotide in binding and catalysis with alcohol, lactate, and glyceraldehyde-3-phosphate dehydrogenases. Suhadolnik, R.J., Lennon, M.B., Uematsu, T., Monahan, J.E., Baur, R. J. Biol. Chem. (1977)
- Thermodynamic analysis of the emergence of new regulatory properties in a phosphoribulokinase-glyceraldehyde 3-phosphate dehydrogenase complex. Graciet, E., Lebreton, S., Camadro, J.M., Gontero, B. J. Biol. Chem. (2002)
- A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role. Hettwer, S., Sterner, R. J. Biol. Chem. (2002)
- Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides. Chen, J.H., Gibson, J.L., McCue, L.A., Tabita, F.R. J. Biol. Chem. (1991)
- The chromatin structure at the promoter of a glyceraldehyde phosphate dehydrogenase gene from Saccharomyces cerevisiae reflects its functional state. Pavlović, B., Hörz, W. Mol. Cell. Biol. (1988)
- Kinetics of connective tissue growth factor expression during experimental proliferative glomerulonephritis. Ito, Y., Goldschmeding, R., Bende, R., Claessen, N., Chand, M., Kleij, L., Rabelink, T., Weening, J., Aten, J. J. Am. Soc. Nephrol. (2001)
- Effects of light and chloroplast functional state on expression of nuclear genes encoding chloroplast glyceraldehyde-3-phosphate dehydrogenase in long hypocotyl (hy) mutants and wild-type Arabidopsis thaliana. Conley, T.R., Shih, M.C. Plant Physiol. (1995)
- Mutations affecting light regulation of nuclear genes encoding chloroplast glyceraldehyde-3-phosphate dehydrogenase in Arabidopsis. Chan, C.S., Peng, H.P., Shih, M.C. Plant Physiol. (2002)
- Acute changes in liver gene expression in the N-nitrosodiethylamine-treated rat. Suzuki, T., Imagawa, M., Yamada, R., Yokoyama, K., Kondo, S., Itakura, K., Muramatsu, M. Carcinogenesis (1994)
- Kinetic studies of crystalline enzymes by single crystal microspectrophotometry. Analysis of a single catalytic turnover in a D-glyceraldehyde-3-phosphate dehydrogenase crystal. Vas, M., Berni, R., Mozzarelli, A., Tegoni, M., Rossi, G.L. J. Biol. Chem. (1979)
- Glyceraldehyde-3-phosphate dehydrogenase-catalyzed chain oxidation of reduced nicotinamide adenine dinucleotide by perhydroxyl radicals. Chan, P.C., Bielski, B.H. J. Biol. Chem. (1980)
- Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis. Corbier, C., Clermont, S., Billard, P., Skarzynski, T., Branlant, C., Wonacott, A., Branlant, G. Biochemistry (1990)
- Identification of the arylazido-beta-alanyl-NAD+-modified site in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase by microsequencing and fast atom bombardment mass spectrometry. Chen, S., Lee, T.D., Legesse, K., Shively, J.E. Biochemistry (1986)