Information on EC 1.1.1.272 - D-2-hydroxyacid dehydrogenase (NADP+)

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.272
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RECOMMENDED NAME
GeneOntology No.
D-2-hydroxyacid dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
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redox reaction
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-
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reduction
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-
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxycarboxylate:NADP+ oxidoreductase
This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyses a stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency. cf. EC 1.1.1.345, (D)-2-hydroxyacid dehydrogenase (NAD+).
CAS REGISTRY NUMBER
COMMENTARY hide
81210-65-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Haloferax mediterranei R-4 / ATCC 33500
gene ddh; strain R4, gene ddh
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-dehydro-L-gulonic acid + NADPH + H+
L-idonate + NADP+
show the reaction diagram
2-oxo-4-methylpentanoate + NAD(P)H
(2R)-2-hydroxy-4-methylpentanoate + NAD(P)+
show the reaction diagram
2-oxobutyrate + NAD(P)H
(2R)-2-hydroxybutyrate + NAD(P)+
show the reaction diagram
2-oxoisoleucine + NAD(P)H
2-D-hydroxyisoleucine + NAD(P)+
show the reaction diagram
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
show the reaction diagram
pyruvate + NADPH + H+
D-lactate + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-dehydro-L-gulonic acid + NADPH + H+
L-idonate + NADP+
show the reaction diagram
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
the larger enzyme domain is responsible for binding the cofactor and contains a conserved [GXGXXG (X17) D] motif that is characteristic of the NAD(P)H/NAD(P)+-binding region. It consists of residues 103-287, forming a seven-stranded parallel beta-sheet flanked by seven alpha-helices
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.45 - 106
2-oxobutyrate
3.77 - 13.9
2-oxoisocaproate
1.31 - 11.9
2-oxoisoleucine
0.233 - 0.5
NADH
0.031 - 0.054
NADPH
21.96
pyruvate
pH 5.0, 40°C, recombinant enzyme, cofactor NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
substrate and cofactor specificity, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
assay at, with substrate pyruvate
8.5
assay at, all substrates, except for pyruvate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
assay at, recombinant refolded enzyme
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29500
4 * 33336, sequence calculation, 4 * 29500, recombinant enzyme, CTAB-PAGE, 4 * 47000, SDS-PAGE
33336
4 * 33336, sequence calculation, 4 * 29500, recombinant enzyme, CTAB-PAGE, 4 * 47000, SDS-PAGE
47000
4 * 33336, sequence calculation, 4 * 29500, recombinant enzyme, CTAB-PAGE, 4 * 47000, SDS-PAGE
111000
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
free enzyme, to 3.0 A resolution, and the nonproductive ternary complex with alpha-ketohexanoic acid and NAD+ to 2.0 A resolution, by hanging-drop vapour-diffusion method
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 30 mg/ml protein in 25 mM Tris/HCl, pH 8.0, 0.3 M NaCl, and 1 mM dithiothreitol, with 0.001 ml of reservoir solution containing 23% w/v PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.0, and equilibration against 0.1 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.64 A resolution, molecular replacement and modeling
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinant enzyme partially from Escherichia coli strain BL21(DE3) inclusion bodies by solubilization with 8 M urea in DTT-containing buffer and refolding by rapid 10fold dilution
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity and anion exchange chromatography, followed by gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene ddh, DNA and amino acid sequence determination and analysis, sequence comparison, subcloning and expression in Escherichia coli strains XL1 Blue and BL21(DE3) in inclusion bodies
recombinant overexpression of C-terminally His6-tagged enzyme in Escherichia coli
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding of recombinant enzyme from Escherichia coli strain BL21(DE3) inclusion bodies, solubilized by 8 M urea in DTT-containing buffer, by rapid 10fold dilution, optimally in presence of 4 M NaCl at pH 8.0 and 37°C
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