BRENDA - Enzyme Database show
show all sequences of 1.1.1.375

Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases

Lee, B.I.; Chang, C.; Cho, S.J.; Eom, S.H.; Kim, K.K.; Yu, Y.G.; Suh, S.W.; J. Mol. Biol. 307, 1351-1362 (2001)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
D-fructose 1,6-bisphosphate
activates
Methanocaldococcus jannaschii
Crystallization (Commentary)
Crystallization
Organism
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
Methanocaldococcus jannaschii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.2
-
NADPH
pH 6.0-7.0, 45°C
Methanocaldococcus jannaschii
0.84
-
pyruvate
pH 6.0-7.0, 45°C
Methanocaldococcus jannaschii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
Q60176
-
-
Methanocaldococcus jannaschii DSM 2661
Q60176
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-sulfopyruvate + NADH
preference of NADPH over NADH
728123
-
(2R)-3-sulfolactate + NAD+
-
-
-
?
3-sulfopyruvate + NADPH
the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH
728123
-
(2R)-3-sulfolactate + NADP+
-
-
-
?
oxaloacetate + NADH
preference of NADPH over NADH
728123
-
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADPH
the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH
728123
-
(S)-malate + NADP+
-
-
-
r
pyruvate + NADH
preference of NADPH over NADH. Activity is detected only when the allosteric activator fructose-1,6-bisphosphate is added to the assay mixture
728123
-
(S)-lactate + NAD+
-
-
-
?
pyruvate + NADH + H+
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
728123
Methanocaldococcus jannaschii
(S)-lactate + NAD+
-
-
-
ir
pyruvate + NADH + H+
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
728123
Methanocaldococcus jannaschii DSM 2661
(S)-lactate + NAD+
-
-
-
ir
pyruvate + NADPH
preference of NADPH over NADH. Activity is detected only when the allosteric activator fructose-1,6-bisphosphate is added to the assay mixture
728123
-
(S)-lactate + NADP+
-
-
-
?
pyruvate + NADPH + H+
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
728123
Methanocaldococcus jannaschii
(S)-lactate + NADP+
-
-
-
ir
pyruvate + NADPH + H+
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
728123
Methanocaldococcus jannaschii DSM 2661
(S)-lactate + NADP+
-
-
-
ir
Subunits
Subunits
Commentary
Organism
tetramer
exists in solution predominantly as a tetramer
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
assay at
Methanocaldococcus jannaschii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
7
assay at
Methanocaldococcus jannaschii
Cofactor
Cofactor
Commentary
Organism
Structure
NAD(P)H
the cofactor is bound at the active site
Methanocaldococcus jannaschii
NADH
preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site
Methanocaldococcus jannaschii
NADPH
preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site
Methanocaldococcus jannaschii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
D-fructose 1,6-bisphosphate
activates
Methanocaldococcus jannaschii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD(P)H
the cofactor is bound at the active site
Methanocaldococcus jannaschii
NADH
preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site
Methanocaldococcus jannaschii
NADPH
preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site
Methanocaldococcus jannaschii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Methanocaldococcus jannaschii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.2
-
NADPH
pH 6.0-7.0, 45°C
Methanocaldococcus jannaschii
0.84
-
pyruvate
pH 6.0-7.0, 45°C
Methanocaldococcus jannaschii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-sulfopyruvate + NADH
preference of NADPH over NADH
728123
-
(2R)-3-sulfolactate + NAD+
-
-
-
?
3-sulfopyruvate + NADPH
the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH
728123
-
(2R)-3-sulfolactate + NADP+
-
-
-
?
oxaloacetate + NADH
preference of NADPH over NADH
728123
-
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADPH
the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH
728123
-
(S)-malate + NADP+
-
-
-
r
pyruvate + NADH
preference of NADPH over NADH. Activity is detected only when the allosteric activator fructose-1,6-bisphosphate is added to the assay mixture
728123
-
(S)-lactate + NAD+
-
-
-
?
pyruvate + NADH + H+
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
728123
Methanocaldococcus jannaschii
(S)-lactate + NAD+
-
-
-
ir
pyruvate + NADH + H+
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
728123
Methanocaldococcus jannaschii DSM 2661
(S)-lactate + NAD+
-
-
-
ir
pyruvate + NADPH
preference of NADPH over NADH. Activity is detected only when the allosteric activator fructose-1,6-bisphosphate is added to the assay mixture
728123
-
(S)-lactate + NADP+
-
-
-
?
pyruvate + NADPH + H+
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
728123
Methanocaldococcus jannaschii
(S)-lactate + NADP+
-
-
-
ir
pyruvate + NADPH + H+
ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions
728123
Methanocaldococcus jannaschii DSM 2661
(S)-lactate + NADP+
-
-
-
ir
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
exists in solution predominantly as a tetramer
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
assay at
Methanocaldococcus jannaschii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
7
assay at
Methanocaldococcus jannaschii
Other publictions for EC 1.1.1.375
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
726931
Madern
Differences in the oligomeric ...
Archaeoglobus fulgidus, Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Biochemistry
40
10310-10306
2001
-
-
1
-
-
-
-
-
-
-
2
3
-
10
-
-
2
-
-
-
-
-
3
2
2
-
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
3
-
-
-
2
-
-
-
-
3
2
2
-
-
-
2
1
-
-
-
-
-
-
-
-
728123
Lee
Crystal structure of the MJ049 ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
J. Mol. Biol.
307
1351-1362
2001
1
-
-
1
-
-
-
2
-
-
-
-
-
8
-
-
-
-
-
-
-
-
10
1
1
-
-
-
1
-
-
3
-
-
-
1
-
-
3
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
10
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
389520
Graupner
Identification of an archaeal ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
J. Bacteriol.
182
3688-3692
2000
-
-
1
-
-
-
-
7
-
-
-
1
-
8
-
-
-
-
-
-
-
-
14
-
1
-
-
-
-
-
-
4
-
-
-
-
-
1
4
-
-
-
-
-
-
7
-
-
-
1
-
-
-
-
-
-
-
-
14
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
728317
Madern
The putative L-lactate dehydro ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Mol. Microbiol.
37
1515-1520
2000
-
-
-
-
-
-
1
3
-
5
-
-
1
5
1
-
1
-
-
-
-
-
4
-
1
-
1
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
3
-
5
-
-
1
1
-
1
-
-
-
-
4
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-