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Information on EC 1.1.1.272 - D-2-hydroxyacid dehydrogenase (NADP+) and Organism(s) Haloferax mediterranei and UniProt Accession Q2VEQ7

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EC Tree
IUBMB Comments
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+).
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Haloferax mediterranei
UNIPROT: Q2VEQ7
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The taxonomic range for the selected organisms is: Haloferax mediterranei
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
d-2-hydroxyacid dehydrogenase, d2-hdh, d-isomer specific 2-hydroxyacid dehydrogenase, 2hadh, l-sulfolactate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-D-hydroxyacid dehydrogenase
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D-2-hydroxyacid dehydrogenase
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D-isomer specific 2-hydroxyacid dehydrogenase
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(R)-2-hydroxyacid dehydrogenase
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-
-
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(R)-sulfolactate dehydrogenase
-
-
-
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(R)-sulfolactate:NAD(P)+ oxidoreductase
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-
-
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L-sulfolactate dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+
show the reaction diagram
the catalytic triad is probably formed by Arg226, Glu255, and His274
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
show the reaction diagram
-
-
-
r
2-oxo-4-methylpentanoate + NAD(P)H
(2R)-2-hydroxy-4-methylpentanoate + NAD(P)+
show the reaction diagram
-
-
-
ir
2-oxobutyrate + NAD(P)H
(2R)-2-hydroxybutyrate + NAD(P)+
show the reaction diagram
-
-
-
ir
2-oxobutyrate + NADH + H+
(2R)-2-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
r
2-oxobutyrate + NADPH + H+
2-D-hydroxybutyrate + NADP+
show the reaction diagram
-
-
-
r
2-oxoisocaproate + NADH + H+
2-D-hydroxyisocaproate + NAD+
show the reaction diagram
-
-
-
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
show the reaction diagram
-
-
-
r
2-oxoisoleucine + NAD(P)H
2-D-hydroxyisoleucine + NAD(P)+
show the reaction diagram
-
-
-
ir
2-oxoisoleucine + NADH + H+
2-D-hydroxyisoleucine + NAD+
show the reaction diagram
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
show the reaction diagram
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
show the reaction diagram
-
-
-
r
pyruvate + NADPH + H+
D-lactate + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
show the reaction diagram
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
the enzyme prefers NADPH over NADH
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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
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview
additional information
sequence-structure-function relationships, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
111000
recombinant enzyme, gel filtration
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 33336, sequence calculation, 4 * 29500, recombinant enzyme, CTAB-PAGE, 4 * 47000, SDS-PAGE
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
three crystal structures of DDH_HALMT are solved in complex with combinations of NAD+, NADP+, NADPH, 2-ketohexanoic acid, and 2-hydroxyhexanoic acid (PDB IDs are 5mha, 5mh5, 5mh6)
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
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Domenech, J.; Ferrer, J.
A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity from Haloferax mediterranei, sequence analysis and heterologous overexpression
Biochim. Biophys. Acta
1760
1667-1674
2006
Haloferax mediterranei (Q2VEQ7), Haloferax mediterranei, Haloferax mediterranei R-4 / ATCC 33500 (Q2VEQ7)
Manually annotated by BRENDA team
Domenech, J.; Baker, P.; Sedelnikova, S.; Rodgers, H.; Rice, D.; Ferrer, J.
Crystallization and preliminary X-ray analysis of D-2-hydroxyacid dehydrogenase from Haloferax mediterranei
Acta Crystallogr. Sect. F
65
415-418
2009
Haloferax mediterranei (Q2VEQ7), Haloferax mediterranei
Manually annotated by BRENDA team
Matelska, D.; Shabalin, I.; Jablonska, J.; Domagalski, M.; Kutner, J.; Ginalski, K.; Minor, W.
Classification, substrate specificity and structural features of D-2-hydroxyacid dehydrogenases 2HADH knowledgebase
BMC Evol. Biol.
18
199
2018
Haloferax mediterranei (Q2VEQ7), Haloferax mediterranei ATCC 33500 (Q2VEQ7), Haloferax mediterranei DSM 1411 (Q2VEQ7), Haloferax mediterranei JCM 8866 (Q2VEQ7), Haloferax mediterranei NBRC 14739 (Q2VEQ7), Haloferax mediterranei NCIMB 2177 (Q2VEQ7), Haloferax mediterranei R-4 (Q2VEQ7)
Manually annotated by BRENDA team