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Information on EC 1.1.1.272 - D-2-hydroxyacid dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.272
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.272 D-2-hydroxyacid dehydrogenase (NADP+)
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+).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.1.1.272
- dehydrogenases
-
2-hydroxyacids
-
enterococcus
-
nad-dependent
- d-mandelate
-
2-oxobutyric
- d-lactate
- 2-ketoisocaproate
-
knowledgebase
- delbrueckii
-
2-keto
-
4-methylthio
- benzoylformate
-
haloferax
- glyoxylate
- bulgaricus
- faecium
-
d-2-hydroxyisocaproate
- mediterranei
showSynonyms
d-2-hydroxyacid dehydrogenase, d2-hdh, d-isomer specific 2-hydroxyacid dehydrogenase, 2hadh, l-sulfolactate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-2-hydroxyacid dehydrogenase
-
-
-
-
(R)-sulfolactate dehydrogenase
-
-
-
-
(R)-sulfolactate:NAD(P)+ oxidoreductase
-
-
-
-
2-D-hydroxyacid dehydrogenase
2HADH
D-2-hydroxyacid dehydrogenase
D-isomer specific 2-hydroxyacid dehydrogenase
D2-HDH
DDH
HDH
L-2-hydroxyacid dehydrogenase
L-sulfolactate dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+
-
-
-
-
an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+
the catalytic triad is probably formed by Arg226, Glu255, and His274
an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+
the catalytic triad is probably formed by Arg226, Glu255, and His274
Haloferax mediterranei R-4 / ATCC 33500
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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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+).
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CAS REGISTRY NUMBER
COMMENTARY
81210-65-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
(2R)-2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADH + H+
2-D-hydroxyisocaproate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADH + H+
2-D-hydroxyisoleucine + NAD+
Substrates: -
Products: -
Products: -
r
2-dehydro-L-gulonic acid + NADPH + H+
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydro-L-gulonic acid + NADPH + H+
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-oxo-4-methylpentanoate + NAD(P)H
(2R)-2-hydroxy-4-methylpentanoate + NAD(P)+
Substrates: -
Products: -
Products: -
ir
2-oxo-4-methylpentanoate + NAD(P)H
(2R)-2-hydroxy-4-methylpentanoate + NAD(P)+
Haloferax mediterranei R-4 / ATCC 33500
Substrates: -
Products: -
Products: -
ir
2-oxobutyrate + NAD(P)H
(2R)-2-hydroxybutyrate + NAD(P)+
Substrates: -
Products: -
Products: -
ir
2-oxobutyrate + NAD(P)H
(2R)-2-hydroxybutyrate + NAD(P)+
Haloferax mediterranei R-4 / ATCC 33500
Substrates: -
Products: -
Products: -
ir
2-oxobutyrate + NADPH + H+
2-D-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADPH + H+
2-D-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADPH + H+
2-D-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADPH + H+
2-D-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADPH + H+
2-D-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADPH + H+
2-D-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADPH + H+
2-D-hydroxybutyrate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NAD(P)H
2-D-hydroxyisoleucine + NAD(P)+
Substrates: -
Products: -
Products: -
ir
2-oxoisoleucine + NAD(P)H
2-D-hydroxyisoleucine + NAD(P)+
Haloferax mediterranei R-4 / ATCC 33500
Substrates: -
Products: -
Products: -
ir
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
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r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
D-lactate + NADP+
Substrates: -
Products: -
Products: -
ir
pyruvate + NADPH + H+
D-lactate + NADP+
Substrates: -
Products: -
Products: -
r
pyruvate + NADPH + H+
D-lactate + NADP+
Substrates: -
Products: -
Products: -
r
pyruvate + NADPH + H+
D-lactate + NADP+
Substrates: -
Products: -
Products: -
r
pyruvate + NADPH + H+
D-lactate + NADP+
Substrates: -
Products: -
Products: -
r
pyruvate + NADPH + H+
D-lactate + NADP+
Substrates: -
Products: -
Products: -
r
pyruvate + NADPH + H+
D-lactate + NADP+
Substrates: -
Products: -
Products: -
r
pyruvate + NADPH + H+
D-lactate + NADP+
Substrates: -
Products: -
Products: -
r
pyruvate + NADPH + H+
D-lactate + NADP+
Haloferax mediterranei R-4 / ATCC 33500
Substrates: -
Products: -
Products: -
ir
additional information
?
-
Substrates: no activity with 2-D-hydroxyacids and L-2-hydroxyisocaproic acid in oxidation reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-D-hydroxyacids and L-2-hydroxyisocaproic acid in oxidation reaction
Products: -
Products: -
?
additional information
?
-
Substrates: the DDH enzyme is a 2-oxocarboxylic reductase with broad substrate specificity. It shows a marked preference for those having an unbranched chain of 4-5 carbon atoms, such as 2-oxoisoleucine. It exhibits dual cofactor specificity, yet shows better catalytic efficiency with NADPH
Products: -
Products: -
?
additional information
?
-
Haloferax mediterranei R-4 / ATCC 33500
Substrates: no activity with 2-D-hydroxyacids and L-2-hydroxyisocaproic acid in oxidation reaction
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-dehydro-L-gulonic acid + NADPH + H+
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydro-L-gulonic acid + NADPH + H+
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
IMAGE
21.96
pyruvate
pH 5.0, 40°C, recombinant enzyme, cofactor NADPH
13.45
2-oxobutyrate
pH 8.5, 40°C, recombinant enzyme, cofactor NADPH
106
2-oxobutyrate
pH 8.5, 40°C, recombinant enzyme, cofactor NADH
3.77
2-oxoisocaproate
pH 8.5, 40°C, recombinant enzyme, cofactor NADPH
13.9
2-oxoisocaproate
pH 8.5, 40°C, recombinant enzyme, cofactor NADH
1.31
2-oxoisoleucine
pH 8.5, 40°C, recombinant enzyme, cofactor NADPH
11.9
2-oxoisoleucine
pH 8.5, 40°C, recombinant enzyme, cofactor NADH
0.233
NADH
pH 8.5, 40°C, recombinant enzyme, substrate 2-oxoisocaproate
0.33
NADH
pH 8.5, 40°C, recombinant enzyme, substrate 2-oxoisoleucine
0.5
NADH
pH 8.5, 40°C, recombinant enzyme, substrate 2-oxobutyrate
0.031
NADPH
pH 8.5, 40°C, recombinant enzyme, substrate 2-oxoisocaproate
0.046
NADPH
pH 8.5, 40°C, recombinant enzyme, substrate 2-oxoisoleucine
0.054
NADPH
pH 8.5, 40°C, recombinant enzyme, substrate 2-oxobutyrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
substrate and cofactor specificity, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
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
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
-
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
-
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
-
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
-
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
-
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
-
physiological function
-
the enzyme catalyzes the bioconversion of 2-dehydro-L-gulonic acid to L-idonate, which plays a negative role in the manufacture of vitamin C, cf. EC 1.1.1.215. The primary biochemical function of HDH from Ketogulonicigenium vulgare is C=O bond oxidation-reduction
physiological function
-
the enzyme catalyzes the bioconversion of 2-dehydro-L-gulonic acid to L-idonate, which plays a negative role in the manufacture of vitamin C, cf. EC 1.1.1.215. The primary biochemical function of HDH from Ketogulonicigenium vulgare is C=O bond oxidation-reduction
-
additional information
-
the amino acid residues Arg234, Glu263 and His 279 form the active site of enzyme HDH. Residues Arg234, Ala210, Thr211, and Arg212, which are located on top of the catalytic triad, act as a size filter to jointly determine the substrate specificity
additional information
sequence-structure-function relationships, overview
additional information
-
sequence-structure-function relationships, overview
-
additional information
-
sequence-structure-function relationships, overview
-
additional information
-
the amino acid residues Arg234, Glu263 and His 279 form the active site of enzyme HDH. Residues Arg234, Ala210, Thr211, and Arg212, which are located on top of the catalytic triad, act as a size filter to jointly determine the substrate specificity
-
additional information
-
sequence-structure-function relationships, overview
-
additional information
-
sequence-structure-function relationships, overview
-
additional information
-
sequence-structure-function relationships, overview
-
additional information
-
sequence-structure-function relationships, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HADHA_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
347
0
37997
Swiss-Prot
-
MORA_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
329
0
35853
Swiss-Prot
-
DDH_HALMT
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
308
0
33336
Swiss-Prot
-
COMC_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
344
0
37358
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
tetramer
4 * 33336, sequence calculation, 4 * 29500, recombinant enzyme, CTAB-PAGE, 4 * 47000, SDS-PAGE
tetramer
Haloferax mediterranei R-4 / ATCC 33500
-
4 * 33336, sequence calculation, 4 * 29500, recombinant enzyme, CTAB-PAGE, 4 * 47000, SDS-PAGE
-
additional information
-
the enzyme shows a structure consisting of two-compact domains separated by a deep active cleft. This typical topology is conserved in other 2-HDH. The smaller domain is the substrate binding domain or catalytic domain, which is formed from N-terminal residues 2-102 and C-terminal residues 288-317. It is folded into a five-stranded parallel beta-sheet flanked by five alpha-helices, forming a modified Rossmann topology. The larger 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. A two-stranded hinge connects the two domains showing flexibilty during catalysis
additional information
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the enzyme shows a structure consisting of two-compact domains separated by a deep active cleft. This typical topology is conserved in other 2-HDH. The smaller domain is the substrate binding domain or catalytic domain, which is formed from N-terminal residues 2-102 and C-terminal residues 288-317. It is folded into a five-stranded parallel beta-sheet flanked by five alpha-helices, forming a modified Rossmann topology. The larger 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. A two-stranded hinge connects the two domains showing flexibilty during catalysis
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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)
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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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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)
brenda
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
brenda
Han, X.; Xiong, X.; Hu, X.; Li, M.; Zhang, W.; Liu, X.
Crystallization and structural analysis of 2-hydroxyacid dehydrogenase from Ketogulonicigenium vulgare
Biotechnol. Lett.
36
295-300
2014
Ketogulonicigenium vulgare, Ketogulonicigenium vulgare Y25
brenda
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 DSM 1411 (Q2VEQ7), Haloferax mediterranei ATCC 33500 (Q2VEQ7), Haloferax mediterranei R-4 (Q2VEQ7), Haloferax mediterranei JCM 8866 (Q2VEQ7), Haloferax mediterranei NBRC 14739 (Q2VEQ7), Haloferax mediterranei NCIMB 2177 (Q2VEQ7)
brenda
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