[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/22.13.2576; PubMed=8041620 [NCBI, ExPASy, EBI, Israel, Japan]
Sofia H.J.,
Burland V.,
Daniels D.L.,
Plunkett G. III,
Blattner F.R.;
"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes.";
Nucleic Acids Res. 22:2576-2586(1994).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO C-TERMINUS.
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R.,
Plunkett G. III,
Bloch C.A.,
Perna N.T.,
Burland V.,
Riley M.,
Collado-Vides J.,
Glasner J.D.,
Rode C.K.,
Mayhew G.F.,
Gregor J.,
Davis N.W.,
Kirkpatrick H.A.,
Goeden M.A.,
Rose D.J.,
Mau B.,
Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K.,
Morooka N.,
Yamamoto Y.,
Fujita K.,
Isono K.,
Choi S.,
Ohtsubo E.,
Baba T.,
Wanner B.L.,
Mori H.,
Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
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[4]
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PROTEIN SEQUENCE OF 1-22, SUBUNIT, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9811658 [NCBI, ExPASy, EBI, Israel, Japan]
Yum D.-Y.,
Lee B.-Y.,
Hahm D.-H.,
Pan J.-G.;
"The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase.";
J. Bacteriol. 180:5984-5988(1998).
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[5]
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PARTIAL PROTEIN SEQUENCE OF 1-8.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J.,
Robison K.,
Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
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[6]
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CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
DOI=10.1042/0264-6021:3540707; PubMed=11237876 [NCBI, ExPASy, EBI, Israel, Japan]
Nunez M.F.,
Pellicer M.T.,
Badia J.,
Aguilar J.,
Baldoma L.;
"Biochemical characterization of the 2-ketoacid reductases encoded by ycdW and yiaE genes in Escherichia coli.";
Biochem. J. 354:707-715(2001).
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- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2-keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D-fructose and L-sorbose. Activity with NAD is very low.
- CATALYTIC ACTIVITY: Glycolate + NADP+ = glyoxylate + NADPH.
- CATALYTIC ACTIVITY: D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H.
- CATALYTIC ACTIVITY: D-gluconate + NADP+ = 2-dehydro-D-gluconate + NADPH.
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=0.7 mM for hydroxypyruvate (at pH 7.5); | | KM=1.5 mM for 2-oxo-D-gluconate (at pH 7.5); | | KM=6.6 mM for glyoxylate (at pH 7.5); | | Vmax=345 µmol/min/mg enzyme with glyoxylate as substrate (at pH 7); | | Vmax=123 µmol/min/mg enzyme with hydroxypyruvate as substrate (at pH 7); | | Vmax=69 µmol/min/mg enzyme with 2-oxo-D-gluconate as substrate (at pH 7); | | Note=The catalytic efficiency is better for hydroxypyruvate than glyoxylate with NADPH as electron donor; | | pH dependence: |
Optimum pH is 7.5; | |
- SUBUNIT: Homodimer.
- INTERACTION:
P36938:pgm; NbExp=1; IntAct=EBI-562547, EBI-542427;
- SUBCELLULAR LOCATION: Cytoplasm (Probable).
- INDUCTION: Constitutively expressed.
- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.
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