Information on EC 1.1.1.375 - L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.375
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RECOMMENDED NAME
GeneOntology No.
L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (2S)-2-hydroxycarboxylate + NAD(P)+ = a 2-oxocarboxylate + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme M biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(2S)-2-hydroxycarboxylate:NAD(P)+ oxidoreductase
The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates) [1]. The enzyme can use both NADH and NADPH, although activity is higher with NADPH [1-3]. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+ [1]. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S)-3-sulfolactate + NADP+
3-sulfopyruvate + NADPH + H+
show the reaction diagram
weak activity, Vmax/KM: 1/min*mg. The enzyme does not catalyse the oxidation of (2S)-3-sulfolactate with NAD+ as cofactor
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r
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
(S)-malate + NADP+
oxaloacetate + NADPH + H+
show the reaction diagram
3-sulfopyruvate + NADH
(2R)-3-sulfolactate + NAD+
show the reaction diagram
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preference of NADPH over NADH
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?
3-sulfopyruvate + NADH + H+
(2S)-3-sulfolactate + NAD+
show the reaction diagram
Vmax/KM: 34/min*mg. The enzyme prefers oxaloacetate over 3-sulfopyruvate using NADH as cofactor
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ir
3-sulfopyruvate + NADPH
(2R)-3-sulfolactate + NADP+
show the reaction diagram
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the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH
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?
3-sulfopyruvate + NADPH + H+
(2S)-3-sulfolactate + NADP+
show the reaction diagram
oxaloacetate + NADH
(S)-malate + NAD+
show the reaction diagram
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preference of NADPH over NADH
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r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
oxaloacetate + NADPH
(S)-malate + NADP+
show the reaction diagram
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the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH
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r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
show the reaction diagram
pyruvate + NADH
(S)-lactate + NAD+
show the reaction diagram
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preference of NADPH over NADH. Activity is detected only when the allosteric activator fructose-1,6-bisphosphate is added to the assay mixture
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?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
pyruvate + NADPH
(S)-lactate + NADP+
show the reaction diagram
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preference of NADPH over NADH. Activity is detected only when the allosteric activator fructose-1,6-bisphosphate is added to the assay mixture
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?
pyruvate + NADPH + H+
(S)-lactate + NADP+
show the reaction diagram
additional information
?
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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
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
3-sulfopyruvate + NADPH + H+
(2S)-3-sulfolactate + NADP+
show the reaction diagram
Q60176
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
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the cofactor is bound at the active site
NAD+
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the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate
NADP+
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the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
K+
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in the presence of NADPH, full enzymatic activity requires a minimum salt concentration of 0.1 M NaCl or KCl. At lower salt concentrations, the activity decreases by a factor of three. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
Mg2+
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in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
Mn2+
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in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
Na+
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in the presence of NADPH, full enzymatic activity requires a minimum salt concentration of 0.1 M NaCl or KCl. At lower salt concentrations, the activity decreases by a factor of three. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxaloacetate
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above 0.3 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-fructose 1,6-bisphosphate
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activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6
(2S)-3-sulfolactate
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70C, pH 9.5, cofactor: NADP+
0.025 - 0.15
(S)-malate
0.19 - 1.3
3-sulfopyruvate
0.14
NADH
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70C, pH 8.0
0.02 - 0.2
NADPH
0.06 - 0.3
oxaloacetate
0.84
pyruvate
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pH 6.0-7.0, 45C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
enzymatic activity of the dimeric enzyme is controlled by a pH-dependent transition between an active and inactive dimeric state at pH 7 without dissociation of the subunits
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
sedimentation analysis
113000
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sedimentation analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the three-dimensional structure is determined in two crystal forms: a dimeric structure in the orthorhombic crystal at 1.9 A resolution and a structure in the tetragonal crystal at 2.8 A; the three-dimensional structure of its gene product has been determined in two crystal forms: a dimeric structure in the orthorhombic crystal at 1.9 A resolution and a tetrameric structure in the tetragonal crystal at 2.8 A
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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thermal transition between active and inactive enzyme starts at about 80C and follows first-order kinetics
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is not sensitive to oxygen
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728317
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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overexpressed in Escherichia coli
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