Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline L-allo-threonine Identifier CHEBI:58585 Charge 0 Formula C4H9NO3 InChIKeyhelp_outline AYFVYJQAPQTCCC-HRFVKAFMSA-N SMILEShelp_outline C[C@H](O)[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADP+ Identifier CHEBI:58349 Charge -3 Formula C21H25N7O17P3 InChIKeyhelp_outline XJLXINKUBYWONI-NNYOXOHSSA-K SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,326 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2S)-2-amino-3-oxobutanoate Identifier CHEBI:78948 Charge 0 Formula C4H7NO3 InChIKeyhelp_outline SAUCHDKDCUROAO-VKHMYHEASA-N SMILEShelp_outline CC(=O)[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADPH Identifier CHEBI:57783 (Beilstein: 10411862) help_outline Charge -4 Formula C21H26N7O17P3 InChIKeyhelp_outline ACFIXJIJDZMPPO-NNYOXOHSSA-J SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,320 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,836 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:30055 | RHEA:30056 | RHEA:30057 | RHEA:30058 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C).
Fujisawa H., Nagata S., Misono H.
Short-chain dehydrogenase/reductase homologues from Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C) show high sequence similarity to serine dehydrogenase from Agrobacterium tumefaciens. We cloned each gene encoding YdfG and YMR226C into E. coli JM109 and purified them to homogeneity ... >> More
Short-chain dehydrogenase/reductase homologues from Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C) show high sequence similarity to serine dehydrogenase from Agrobacterium tumefaciens. We cloned each gene encoding YdfG and YMR226C into E. coli JM109 and purified them to homogeneity from the E. coli clones. YdfG and YMR226C consist of four identical subunits with a molecular mass of 27 and 29 kDa, respectively. Both enzymes require NADP(+) as a coenzyme and use L-serine as a substrate. Both enzymes show maximum activity at about pH 8.5 for the oxidation of L-serine. They also catalyze the oxidation of D-serine, L-allo-threonine, D-threonine, 3-hydroxyisobutyrate, and 3-hydroxybutyrate. The k(cat)/K(m) values of YdfG for L-serine, D-serine, L-allo-threonine, D-threonine, L-3-hydroxyisobutyrate, and D-3-hydroxyisobutyrate are 105, 29, 199, 109, 67, and 62 M(-1) s(-1), and those of YMR226C are 116, 110, 14600, 7540, 558, and 151 M(-1) s(-1), respectively. Thus, YdfG and YMR226C are NADP(+)-dependent dehydrogenases acting on 3-hydroxy acids with a three- or four-carbon chain, and L-allo-threonine is the best substrate for both enzymes. << Less
Biochim. Biophys. Acta 1645:89-94(2003) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
RHEA:30055 part of RHEA:43524