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Information on EC 1.1.1.337 - L-2-hydroxycarboxylate dehydrogenase (NAD+)
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1.1.1.337 L-2-hydroxycarboxylate dehydrogenase (NAD+)IUBMB Comments
The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate . Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
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Word Map
- 1.1.1.337
- dehydrogenases
- lactobacillus
- confusus
- l-lactate
- jannaschii
-
nadh-dependent
-
methanogen
- sulfite
-
dogfish
- 2-oxoisocaproate
-
desulfonation
- methanocaldococcus
- cysteate
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
l-hicdh, l-2-hydroxyisocaproate dehydrogenase, sulfolactate dehydrogenase, mj1425, mdh i, l-hydroxyisocaproate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-2-hydroxyisocaproate dehydrogenase
-
MDH I
MJ1425
sulfolactate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (2S)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(2S)-2-hydroxycarboxylate:NAD+ oxidoreductase
The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate [3]. Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
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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
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
-
-
r
1-hydroxy-1,3,4,6-hexanetetracarboxylate + NAD+
1-oxo-1,3,4,6-hexanetetracarboxylate + NADH + H+
-
-
r
2-hydroxyisocaproate + NAD+
2-oxoisocaproate + NADH + H+
the initial rate of the reduction of 2-oxoisocaproate is about seven times faster than the reverse reaction, the dehydrogenation of L-2-hydroxyisocaproate, measured in buffers at the respective pH optima
-
r
2-oxoglutarate + NADH + H+
(S)-2-hydroxyglutarate + NAD+
-
-
?
2-oxopentanedioic acid + NADH + H+
2-hydroxypentandioic acid + NAD+
-
-
?
4-methyl-2-oxopentanoate + NADH + H+
(S)-2-hydroxy-4-methylpentanoate + NAD+
-
-
r
glyoxylate + NADH + H+
2-hydroxypropanoate + NAD+
-
-
?
oxopropandioic acid + NADH + H+
2-hydroxypropanedioic acid + NAD+
-
-
?
(2R)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
-
-
r
(2R)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
-
-
r
2-oxocaproate + NADH + H+
2-hydroxycaproate + NAD+
2-oxocaproate is the best substrate for the wild-type enzyme
-
r
2-oxoisocaproate + NADH + H+
2-hydroxyisocaproate + NAD+
2-oxoisocaproate is the best substrate with the lowest KM-valus of 0.065 mM. Tthe initial rate of the reduction of 2-oxoisocaproate is about seven times faster than the reverse reaction, the dehydrogenation of L-2-hydroxyisocaproate, measured in buffers at the respective pH optima
-
r
3-sulfopyruvate + NADH + H+
(S)-3-sulfolactate + NAD+
-
-
r
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
-
-
?
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
Paracoccus pantotrophus NKNCYSA / DSM 12449
-
-
-
?
a 2-oxocarboxylate + NADH + H+
(2S)-2-hydroxycarboxylate + NAD+
-
-
r
a 2-oxocarboxylate + NADH + H+
(2S)-2-hydroxycarboxylate + NAD+
various 2-oxocarboxylic acids are stereospecifically reduced to the corresponding (S)-2-hydroxycarboxylic acids. In the reverse reaction the NAD+-dependent dehydrogenation of L-2-hydroxycarboxylic acids is observed
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
transfer of pro-4S hydrogen from the reduced coenzyme to the 2-oxoacid substrate
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
transfer of pro-4S hydrogen from the reduced coenzyme to the 2-oxoacid substrate
-
?
additional information
?
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: pyruvate
-
?
additional information
?
-
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: pyruvate
-
?
additional information
?
-
enzyme catalyzes the NADH-dependent reduction of oxaloacetate, 2-oxoglutarate, and pyruvate to the corresponding (S)-2-hydroxyacids with pro-S NADH-stereospecifity
-
?
additional information
?
-
no substrates: pyruvate, 2-oxobutanoate, 2-oxovalerate, ketoisovalerate, 2-oxohexanedioate, 2-ketohexanedioate, 3-methyl 2-oxovalerate and 4-methyl-2-oxovalerate
-
?
additional information
?
-
-
no substrates: pyruvate, 2-oxobutanoate, 2-oxovalerate, ketoisovalerate, 2-oxohexanedioate, 2-ketohexanedioate, 3-methyl 2-oxovalerate and 4-methyl-2-oxovalerate
-
?
additional information
?
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: 2-oxoglutarate, pyruvate, 1-oxo-1,3,4,6-hexanetetracarboxylate
-
?
additional information
?
-
-
enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: 2-oxoglutarate, pyruvate, 1-oxo-1,3,4,6-hexanetetracarboxylate
-
?
additional information
?
-
broad substrate specificity, utilizes a wide range of 2-oxo acids branched at the C4 atom
-
?
additional information
?
-
-
broad substrate specificity, utilizes a wide range of 2-oxo acids branched at the C4 atom
-
?
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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
a 2-oxocarboxylate + NADH + H+
(2S)-2-hydroxycarboxylate + NAD+
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
the enzyme requires NAD+ as a cofactor, no reaction with NADP+ in concentrations up to 3 mM
NADH
ratio vmax/Km for NADH is about 20fold greater than for NADPH
NADH
the enzyme requires NADH as a cofactor, no reaction with NADPH up to 0.24 mM
NADPH
ratio vmax/Km for NADH is about 20fold greater than for NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
at 1 mM no influence is observed with Mg2+, Ca2+, Co2+, Ni2+, and Cd2+ and very weak effects with Mn2+, Cu2+, and Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
reduced glutathione (20 mM) has no effect. EDTA, 2,2'-bipyridyl in 1 mM and 10 mM final concentrations have no effect on enzymatic activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
1-oxo-1,3,4,6-hexanetetracarboxylate
cosubstrate NADH, pH 8.0, 70°C
19
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
1 - 4
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82
2.8
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87/delP88
43
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
2.8
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
30
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
25
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82
39
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
520000
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87/delP88
12000
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
0.004
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.68
2-oxocaproate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
0.91
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
1.8
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme del I81/delK82
190000
4-methyl-2-oxopentanoate
pH 7.0, 30°C, mutant enzyme delN87/delP88
4300
phenylpyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
0.00013
pyruvate
pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
the maximal temperature is around 50°C. At this temperature the reaction proceeded at about 3fold increase of the rate compared to 30°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
maximum specific and volume activities are found at the end of the exponential growth phase, during further fermentation enzyme activity declines rapidly and is no longer detectable after 15 h
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin
physiological function
enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin
physiological function
-
enzyme is part of the degradative pathway from (R)-cysteate to pyruvate and sulfate
physiological function
Microorganisms
-
overview on the pathways for synthesis of methanofuran, 5,6,7,8-tetrahydromethanopterin, coenzyme F420, coenzyme M (2-mercaptoethanesulfonic acid) and coenzyme B
physiological function
Paracoccus pantotrophus NKNCYSA / DSM 12449
-
enzyme is part of the degradative pathway from (R)-cysteate to pyruvate and sulfate
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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). COMC_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
344
0
37358
Swiss-Prot
-
COMC_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
341
0
36631
Swiss-Prot
-
A0A1Q9P4Q2_HEILC
Heimdallarchaeota archaeon (strain LC_2)
391
0
42955
TrEMBL
-
MDH_METFV
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
339
0
36762
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with NADH, to 2.5 A resolution. The asymmetric unit contains a tetramer of tight dimers. Structure does not contain a cofactor-binding domain with Rossmann-fold topology. The NADH is bound in an extended conformation in each active site, in a manner that explains the pro-S specificity. Cofactor binding involves residues belonging to both subunits within the tight dimers. The results indicate the existence of a substrate discrimination mechanism, which involves electrostatic interactions
recombinant enzyme is crystallized with ammonium sulfate as precipitant in the presence of NAD+. The crystals belong to the trigonal space group P3(2)21, with a = 135.9 A and c = 205.9 A, and diffract X-rays to 2.2 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
del I81/delK82
phenylpyruvate is the only substrate which is converted at a significant catalytic rate by the mutant enzyme. In the publication this mutant is referred to as Ile100ADELTA/Lys100BDELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
del I81/delK82/delN87/delP88
specific modifications in catalytic rates and substrate recognition
del L 83
deletion mutant shows an altered substrate specificity. In the publication this mutant is referred to as Leu101DELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delI81
drastic reductions in the catalytic activity for all tested substrates. In the publication this mutant is referred to as Ile100ADELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delK82
drastic reductions in the catalytic activity for all tested substrates. In the publication this mutant is referred to as Lys100BDELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delN87
deletion mutant shows an altered substrate specificity. In the publication this mutant is referred to as Asn105ADELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delN87/delP88
for the deletion mutant enzyme 2-oxo carboxylic acids branched at C4 are better substrates than 2-oxocaproate, the substrate with the best kcat,/KM ratio known for the wild-type enzyme.The mutation results in a 5.2fold increased catalytic efficiency towards 4-methyl-2-oxopentanoate compared to the wild-type enzyme. In the publication this mutant is referred to as Asn105ADELTA/Pro105BDELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
delP88
deletion mutant shows an altered substrate specificity. In the publication this mutant is referred to as Pro105BDELTA, according to the numbering system of the dogfish L-lactate dehydrogenase coenzyme loop region
F236S
phenylpyruvate displays the largest kcat of the tested substrates. All kcat values, with the exception of phenylpyruvate, are reduced, but the relative acceptance of phenylglyoxylate is greatly increased
F236V
decrease in the second-order rate constants for all tested substrates. The kcat values for the smaller substrates decrease drastically. Phenylpyruvate is the favourite substrate (2-oxocaproate is the favourite substrate of the wild-type enzyme)
G234V/G235D
the second-order rate constant decreased for most substrates with the exception of pyruvate, which reacts 2.5times faster in the mutant enzyme than in the wild-type enzyme. The catalysis of 2-oxoisocaproate is unaffected
L239A
shift of enzyme specificity towards the substrates branched at C3 corresponding to an increase in the turnover numbers for 2-oxoisocaproate
L239F
slight decrease in the KM values for phenylglyoxylate combined with a dramatic decrease in the kcat values
L239M
KM values of all substrates of the enzyme variant are very similar to those of the wild-type enzyme, large improvement in the kcat values of the C4-branched substrates 2-oxoisocaproate and phenylpyruvate, decrease in the turnover number of 2-oxocaproate (the substrate favoured by the wild-type enzyme). Whereas in the wild-type enzyme the second-order rate constant for 2-oxoisocaproate is only 1% of that for the unbranched substrate, in the mutant enzyme the rate constant of 2-oxocaproate is only 18% of that for 2-oxoisocaproate
L239M/T245A
the catalytic rates are reduced by several orders of magnitude and the KM values shows at least a 100fold increase for most substrates (with the exception of phenylglyoxylate). With respect to L239M the substrate specificity shifts towards keto-tert-leucine and with respect to T245A 2-oxoisocaproate and phenylpyruvate are more favoured
L239W
slight decrease in the KM values for phenylglyoxylate combined with a dramatic decrease in the kcat values
T245A
the catalytic rates are reduced by several orders of magnitude, relative shift of substrate specificity for keto-tert-leucine of more than 17 000 compared with the 2-oxocaproate (kcat/KM)
additional information
additional information
the coenzyme loop, a functional element which is essential for catalysis and substrate specificity, is modified in order to identify the residues involved in the catalytic reaction and substrate specificity
additional information
-
the coenzyme loop, a functional element which is essential for catalysis and substrate specificity, is modified in order to identify the residues involved in the catalytic reaction and substrate specificity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
4°C, 6 months, concentrated enzyme solutions, 10% loss of activity
726750
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52
heat capacity function of the enzyme shows a single peak with the T(m) values between 52.14° C and 55.89°C at pH 7.0 at different scan rates
additional information
additional information
the thermal denaturation of the enzyme is studied by Differential Scanning Calorimetry and Circular Dichroism spectroscopy. The thermal denaturation is pH dependent. The thermal denaturation is irreversible and the T(m) is dependent on the scan-rate. Stabilizing effect of NADH binding. The denaturation process of L-HicDH is kinetically determined
additional information
-
the thermal denaturation of the enzyme is studied by Differential Scanning Calorimetry and Circular Dichroism spectroscopy. The thermal denaturation is pH dependent. The thermal denaturation is irreversible and the T(m) is dependent on the scan-rate. Stabilizing effect of NADH binding. The denaturation process of L-HicDH is kinetically determined
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 6.5, concentrated enzyme solution, 10% loss of activity after 6 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
single-step purification of hexahistidine-tagged enzyme. The tag removal is accomplished by a derivative of recombinant tobacco etch virus protease
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
the L-HicDH gene is expressed under control of phage lambda Leftward and rightward promoters in Escherichia coli up to 35% of total cell protein. The enzyme produced under these conditions exhibits full specific activity and is found exclusively in soluble form
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the enzyme can be applied in an industrial process for the production of L-amino acids
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Graupner, M.; Xu, H.; White, R.H.
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea
J. Bacteriol.
182
3688-3692
2000
Methanothermus fervidus (P16142), Methanothermus fervidus, Methanocaldococcus jannaschii (Q58820), Methanocaldococcus jannaschii
brenda
Rein, U.; Gueta, R.; Denger, K.; Ruff, J.; Hollemeyer, K.; Cook, A.M.
Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA
Microbiology
151
737-747
2005
Paracoccus pantotrophus, Paracoccus pantotrophus NKNCYSA / DSM 12449
brenda
Graupner, M.; White, R.H.
The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea
Biochim. Biophys. Acta
158
169-173
2001
Methanothermus fervidus (P16142), Methanocaldococcus jannaschii (Q58820)
brenda
Irimia, A.; Madern, D.; Zaccai, G.; Vellieux, F.M.
Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes
EMBO J.
23
1234-1244
2004
Methanocaldococcus jannaschii (Q58820), Methanocaldococcus jannaschii
brenda
Schütte, W.; Hummel, W.; Kula, M.R.
L-2-Hydroxyisocaproate dehydrogenase - A new enzyme from Lactobacillus confusus for the stereospecific reduction of 2-ketocarboxylic acids
Appl. Microbiol. Biotechnol.
19
167-176
1984
Weissella confusa (P14295)
-
brenda
Feil, I.K.; Lerch, H.P.; Schomburg, D.
Deletion variants of L-hydroxyisocaproate dehydrogenase. Probing substrate specificity
Eur. J. Biochem.
223
857-863
1994
Weissella confusa (P14295), Weissella confusa
brenda
Lerch, H.P.; Frank, R.; Collins, J.
Cloning, sequencing and expression of the L-2-hydroxyisocaproate dehydrogenase-encoding gene of Lactobacillus confusus in Escherichia coli
Gene
83
263-270
1989
Weissella confusa (P14295), Weissella confusa
brenda
Niefind, K.; Hecht, H.J.; Schomburg, D.
Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 A resolution. An example of strong asymmetry between subunits
J. Mol. Biol.
251
256-281
1995
Weissella confusa (P14295), Weissella confusa
brenda
Feil, I.K.; Hendle, J.; Schomburg, D.
Modified substrate specificity of L-hydroxyisocaproate dehydrogenase derived from structure-based protein engineering
Protein Eng.
10
255-262
1997
Weissella confusa (P14295), Weissella confusa
brenda
Chatterjee, S.; Schoepe, J.; Lohmer, S.; Schomburg, D.
High level expression and single-step purification of hexahistidine-tagged L-2-hydroxyisocaproate dehydrogenase making use of a versatile expression vector set
Protein Expr. Purif.
39
137-143
2005
Weissella confusa (P14295)
brenda
Bao, L.; Chatterjee, S.; Lohmer, S.; Schomburg, D.
An irreversible and kinetically controlled process: thermal induced denaturation of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus
Protein J.
26
143-151
2007
Weissella confusa (P14295), Weissella confusa
brenda
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