BRENDA - Enzyme Database show
show all sequences of 1.1.1.93

Tartrate dehydrogenase, an enzyme with multiple catalytic activities

Tipton, P.A.; Protein Pept. Lett. 7, 323-332 (2000)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
NH4+
required
Pseudomonas putida
Inhibitors
Inhibitors
Commentary
Organism
Structure
D-malate
competitive versus L-tartrate and meso-tartate
Pseudomonas putida
L-Tartrate
competitive versus meso-tartrate and D-malate
Pseudomonas putida
meso-tartrate
competitive versus L-tartrate and D-malate
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
isopropylmalate
-
Pseudomonas putida
0.05
-
D-malate
-
Pseudomonas putida
0.06
-
meso-tartrate
-
Pseudomonas putida
1
-
L-Tartrate
-
Pseudomonas putida
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
monovalent cation required, maximal activity with K+ and Rb+
Pseudomonas putida
Mg2+
supports catalytic activity
Pseudomonas putida
Mn2+
required; supports catalytic activity
Pseudomonas putida
Rb+
monovalent cation required, maximal activity with K+ and Rb+
Pseudomonas putida
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-(+)-tartrate + NAD+
Pseudomonas putida
enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
oxaloglycolate + NADH
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Reaction
Reaction
Commentary
Organism
tartrate + NAD+ = oxaloglycolate + NADH + H+
A-side dehydrogenase, i.e. the hydride is transferred from the substrate to the pro-R position of C4 of NADH
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-malate + NAD+
-
389612
Pseudomonas putida
pyruvate + CO2 + NADH
D-malate is oxidized to oxaloacetate, which remains bound to the enzyme and undergoes decarboxylation to yield pyruvate
389612
Pseudomonas putida
?
isopropylmalate + NAD+
-
389612
Pseudomonas putida
?
-
-
-
?
L-(+)-tartrate + NAD+
enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
389612
Pseudomonas putida
oxaloglycolate + NADH
-
-
-
-
L-tartrate + NAD+
oxidation occurs at 2R position
389612
Pseudomonas putida
oxaloglycolate + NADH + H+
3R-oxaloglycolate
389612
Pseudomonas putida
?
meso-tartrate + NAD+
oxidation occurs at 2R oposition
389612
Pseudomonas putida
oxaloglycolate + NADH + H+
meso-tartrate is oxidized to 3S-oxaloglycolate, followed by decarboxylation to hydroxypyruvate
389612
Pseudomonas putida
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.2
-
isopropylmalate
-
Pseudomonas putida
0.483
-
L-Tartrate
-
Pseudomonas putida
0.617
-
meso-tartrate
-
Pseudomonas putida
19.7
-
D-malate
-
Pseudomonas putida
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
cofactor
Pseudomonas putida
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
NH4+
required
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
cofactor
Pseudomonas putida
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-malate
competitive versus L-tartrate and meso-tartate
Pseudomonas putida
L-Tartrate
competitive versus meso-tartrate and D-malate
Pseudomonas putida
meso-tartrate
competitive versus L-tartrate and D-malate
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
isopropylmalate
-
Pseudomonas putida
0.05
-
D-malate
-
Pseudomonas putida
0.06
-
meso-tartrate
-
Pseudomonas putida
1
-
L-Tartrate
-
Pseudomonas putida
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
monovalent cation required, maximal activity with K+ and Rb+
Pseudomonas putida
Mg2+
supports catalytic activity
Pseudomonas putida
Mn2+
required; supports catalytic activity
Pseudomonas putida
Rb+
monovalent cation required, maximal activity with K+ and Rb+
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-(+)-tartrate + NAD+
Pseudomonas putida
enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
oxaloglycolate + NADH
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-malate + NAD+
-
389612
Pseudomonas putida
pyruvate + CO2 + NADH
D-malate is oxidized to oxaloacetate, which remains bound to the enzyme and undergoes decarboxylation to yield pyruvate
389612
Pseudomonas putida
?
isopropylmalate + NAD+
-
389612
Pseudomonas putida
?
-
-
-
?
L-(+)-tartrate + NAD+
enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
389612
Pseudomonas putida
oxaloglycolate + NADH
-
-
-
-
L-tartrate + NAD+
oxidation occurs at 2R position
389612
Pseudomonas putida
oxaloglycolate + NADH + H+
3R-oxaloglycolate
389612
Pseudomonas putida
?
meso-tartrate + NAD+
oxidation occurs at 2R oposition
389612
Pseudomonas putida
oxaloglycolate + NADH + H+
meso-tartrate is oxidized to 3S-oxaloglycolate, followed by decarboxylation to hydroxypyruvate
389612
Pseudomonas putida
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.2
-
isopropylmalate
-
Pseudomonas putida
0.483
-
L-Tartrate
-
Pseudomonas putida
0.617
-
meso-tartrate
-
Pseudomonas putida
19.7
-
D-malate
-
Pseudomonas putida
Other publictions for EC 1.1.1.93
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)
710720
Malik
Structural characterization of ...
Pseudomonas putida
Acta Crystallogr. Sect. D
66
673-684
2010
-
-
1
1
6
-
-
8
-
-
-
-
-
2
-
-
1
1
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
1
-
1
6
-
-
-
-
8
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
8
8
667741
Karsten
An isothermal titration calori ...
Pseudomonas putida
Biochemistry
45
9000-9006
2006
-
-
-
-
-
-
-
1
-
2
-
-
-
2
-
-
-
1
-
-
-
-
2
1
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
654622
Karsten
Tartrate dehydrogenase catalyz ...
Escherichia coli
Biochemistry
41
12193-12199
2002
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
389612
Tipton
-
Tartrate dehydrogenase, an enz ...
Pseudomonas putida
Protein Pept. Lett.
7
323-332
2000
1
-
-
-
-
-
3
4
-
4
-
1
-
1
-
-
-
1
-
-
-
-
5
-
-
-
-
4
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
3
-
4
-
4
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
389619
Tsukatani
-
Quantification of L-tartrate i ...
Escherichia coli
Anal. Sci.
16
265-268
2000
-
1
-
-
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
389613
Harve
Production and purification of ...
Pseudomonas putida
Appl. Biochem. Biotechnol.
70-72
677-686
1998
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389614
Tipton
Transient-state kinetic analys ...
Pseudomonas putida
Biochemistry
35
3108-3114
1996
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
349359
Serfozo
Substrate determinants of the ...
Pseudomonas putida
Biochemistry
34
7517-7524
1995
-
-
-
-
-
-
-
14
-
-
-
-
-
1
-
-
-
-
-
-
-
-
14
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
14
-
-
-
-
-
-
-
-
-
-
-
-
14
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
349358
Beecher
Tartrate dehydrogenase-oxalate ...
Pseudomonas putida
Arch. Biochem. Biophys.
315
255-261
1994
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389617
Tipton
Tartrate dehydrogenase, a new ...
Pseudomonas putida
Arch. Biochem. Biophys.
313
15-21
1994
-
-
1
-
-
-
-
3
-
-
1
-
-
3
-
-
-
-
-
-
-
-
2
1
-
-
-
3
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
2
1
-
-
-
3
-
-
-
-
-
-
-
-
-
-
389618
Tipton
Characterization of the multip ...
Pseudomonas putida
Biochemistry
29
1749-1756
1990
-
-
-
-
-
-
1
-
-
2
2
-
-
2
-
-
1
1
-
-
1
1
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
2
2
-
-
-
-
1
-
-
1
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389611
Gifforn
-
L-(+)-Tartrate ...
Rhodobacter sphaeroides
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
7
78-85
1985
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287429
Ebbighausen
-
A novel mechanism involved in ...
Rhodobacter sphaeroides
Arch. Microbiol.
138
338-344
1984
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389609
Giffhorn
Purification and characterizat ...
Rhodobacter sphaeroides
J. Bacteriol.
155
281-290
1983
1
-
-
-
-
1
4
4
-
6
3
-
-
2
-
-
1
-
-
-
1
1
2
1
1
-
1
-
1
1
-
1
-
-
-
1
-
-
1
-
-
1
-
4
-
4
-
6
3
-
-
-
-
1
-
-
1
1
2
1
1
-
1
-
1
1
-
-
-
-
-
-
-
-
389610
Kohn
Tartaric acid metabolism. V. C ...
Pseudomonas putida
J. Biol. Chem.
243
2479-2485
1968
-
-
-
1
-
-
-
5
-
1
2
-
-
1
-
-
1
-
-
-
1
-
3
1
-
-
-
-
2
2
-
2
-
-
-
-
-
-
2
1
-
-
-
-
-
5
-
1
2
-
-
-
-
1
-
-
1
-
3
1
-
-
-
-
2
2
-
-
-
-
-
-
-
-