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Information on EC 1.1.1.272 - D-2-hydroxyacid dehydrogenase (NADP+)
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EC Tree
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+).
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Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
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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-
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxobutyrate + NADH + H+
(2R)-2-hydroxybutyrate + NAD+
-
-
-
r
2-oxoisocaproate + NADH + H+
2-D-hydroxyisocaproate + NAD+
-
-
-
r
2-oxoisocaproate + NADPH + H+
2-hydroxyisocaproate + NADP+
-
-
-
r
2-oxoisoleucine + NADH + H+
2-D-hydroxyisoleucine + NAD+
-
-
-
r
2-dehydro-L-gulonic acid + NADPH + H+
L-idonate + NADP+
-
-
-
-
?
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
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-
-
r
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
-
-
-
r
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
-
-
-
r
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
-
-
-
r
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
-
-
-
r
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
-
-
-
r
2-oxo-3-methylvalerate + NADPH + H+
2-D-hydroxy-3-methylvalerate + NADP+
-
-
-
r
2-oxo-4-methylpentanoate + NAD(P)H
(2R)-2-hydroxy-4-methylpentanoate + NAD(P)+
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-
-
ir
2-oxo-4-methylpentanoate + NAD(P)H
(2R)-2-hydroxy-4-methylpentanoate + NAD(P)+
Haloferax mediterranei R-4 / ATCC 33500
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-
-
ir
2-oxobutyrate + NAD(P)H
(2R)-2-hydroxybutyrate + NAD(P)+
-
-
-
ir
2-oxobutyrate + NAD(P)H
(2R)-2-hydroxybutyrate + NAD(P)+
Haloferax mediterranei R-4 / ATCC 33500
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-
-
ir
2-oxoisoleucine + NAD(P)H
2-D-hydroxyisoleucine + NAD(P)+
-
-
-
ir
2-oxoisoleucine + NAD(P)H
2-D-hydroxyisoleucine + NAD(P)+
Haloferax mediterranei R-4 / ATCC 33500
-
-
-
ir
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
-
?
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
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-
-
-
?
additional information
?
-
no activity with 2-D-hydroxyacids and L-2-hydroxyisocaproic acid in oxidation reaction
-
-
?
additional information
?
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-
no activity with 2-D-hydroxyacids and L-2-hydroxyisocaproic acid in oxidation reaction
-
-
?
additional information
?
-
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
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-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
Haloferax mediterranei R-4 / ATCC 33500
no activity with 2-D-hydroxyacids and L-2-hydroxyisocaproic acid in oxidation reaction
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-dehydro-L-gulonic acid + NADPH + H+
L-idonate + NADP+
-
-
-
-
?
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
2-oxoisoleucine + NADPH + H+
2-D-hydroxyisoleucine + NADP+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
r
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
-
?
an (R)-2-hydroxycarboxylate + NADP+
a 2-oxocarboxylate + NADPH + H+
-
-
-
-
?
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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
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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
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (507 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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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
-
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