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show all sequences of 1.1.1.93

Tartrate dehydrogenase-oxalate complexes: formation of a stable analog of a reaction intermediate complex

Beecher, B.S.; Koder, R.L.; Tipton, P.A.; Arch. Biochem. Biophys. 315, 255-261 (1994)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
oxalate
forms a stable complex with Mn-tartrate dehydrogenase-NADH complexes
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
expression by Escherichia coli
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tartrate + NAD+
-
349358
Pseudomonas putida
oxaloglycolate + NADH + H+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
cofactor
Pseudomonas putida
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
cofactor
Pseudomonas putida
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
oxalate
forms a stable complex with Mn-tartrate dehydrogenase-NADH complexes
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tartrate + NAD+
-
349358
Pseudomonas putida
oxaloglycolate + NADH + H+
-
-
-
?
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
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8
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-
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2
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1
1
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1
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6
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1
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6
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8
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1
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1
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6
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8
8
667741
Karsten
An isothermal titration calori ...
Pseudomonas putida
Biochemistry
45
9000-9006
2006
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1
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2
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2
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1
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654622
Karsten
Tartrate dehydrogenase catalyz ...
Escherichia coli
Biochemistry
41
12193-12199
2002
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1
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1
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389612
Tipton
-
Tartrate dehydrogenase, an enz ...
Pseudomonas putida
Protein Pept. Lett.
7
323-332
2000
1
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3
4
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4
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5
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4
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389619
Tsukatani
-
Quantification of L-tartrate i ...
Escherichia coli
Anal. Sci.
16
265-268
2000
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1
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389613
Harve
Production and purification of ...
Pseudomonas putida
Appl. Biochem. Biotechnol.
70-72
677-686
1998
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389614
Tipton
Transient-state kinetic analys ...
Pseudomonas putida
Biochemistry
35
3108-3114
1996
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1
1
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3
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1
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349359
Serfozo
Substrate determinants of the ...
Pseudomonas putida
Biochemistry
34
7517-7524
1995
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14
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1
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14
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14
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14
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349358
Beecher
Tartrate dehydrogenase-oxalate ...
Pseudomonas putida
Arch. Biochem. Biophys.
315
255-261
1994
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389617
Tipton
Tartrate dehydrogenase, a new ...
Pseudomonas putida
Arch. Biochem. Biophys.
313
15-21
1994
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1
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3
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1
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3
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1
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389618
Tipton
Characterization of the multip ...
Pseudomonas putida
Biochemistry
29
1749-1756
1990
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2
2
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389611
Gifforn
-
L-(+)-Tartrate ...
Rhodobacter sphaeroides
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
7
78-85
1985
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287429
Ebbighausen
-
A novel mechanism involved in ...
Rhodobacter sphaeroides
Arch. Microbiol.
138
338-344
1984
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389609
Giffhorn
Purification and characterizat ...
Rhodobacter sphaeroides
J. Bacteriol.
155
281-290
1983
1
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3
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3
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389610
Kohn
Tartaric acid metabolism. V. C ...
Pseudomonas putida
J. Biol. Chem.
243
2479-2485
1968
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1
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