BRENDA - Enzyme Database show
show all sequences of 6.2.1.9

Malate thiokinase. The reaction mechanism as determined by initial rate studies

Hersh, L.B.; J. Biol. Chem. 249, 6264-6271 (1974)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Chromium-ATP
dead-end inhibitor
Pseudomonas sp.
phosphate
product inhibitor
Pseudomonas sp.
succinyl-CoA
product inhibitor
Pseudomonas sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Pseudomonas sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas sp.
-
-
-
Pseudomonas sp. MA
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + malate + CoA
-
855
Pseudomonas sp.
ADP + phosphate + malyl-CoA
-
-
-
-
ATP + malate + CoA
-
855
Pseudomonas sp. MA
ADP + phosphate + malyl-CoA
-
-
-
-
ATP + succinate + CoA
random addition of substrates
855
Pseudomonas sp.
ADP + phosphate + succinyl-CoA
-
-
-
-
ATP + succinate + CoA
random addition of substrates
855
Pseudomonas sp. MA
ADP + phosphate + succinyl-CoA
-
-
-
-
additional information
arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate
855
Pseudomonas sp.
?
-
-
-
-
additional information
enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate
855
Pseudomonas sp.
?
-
-
-
-
additional information
arsenolysis reaction
855
Pseudomonas sp.
?
-
-
-
-
additional information
arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate
855
Pseudomonas sp. MA
?
-
-
-
-
additional information
enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate
855
Pseudomonas sp. MA
?
-
-
-
-
additional information
arsenolysis reaction
855
Pseudomonas sp. MA
?
-
-
-
-
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Chromium-ATP
dead-end inhibitor
Pseudomonas sp.
phosphate
product inhibitor
Pseudomonas sp.
succinyl-CoA
product inhibitor
Pseudomonas sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Pseudomonas sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + malate + CoA
-
855
Pseudomonas sp.
ADP + phosphate + malyl-CoA
-
-
-
-
ATP + malate + CoA
-
855
Pseudomonas sp. MA
ADP + phosphate + malyl-CoA
-
-
-
-
ATP + succinate + CoA
random addition of substrates
855
Pseudomonas sp.
ADP + phosphate + succinyl-CoA
-
-
-
-
ATP + succinate + CoA
random addition of substrates
855
Pseudomonas sp. MA
ADP + phosphate + succinyl-CoA
-
-
-
-
additional information
arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate
855
Pseudomonas sp.
?
-
-
-
-
additional information
enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate
855
Pseudomonas sp.
?
-
-
-
-
additional information
arsenolysis reaction
855
Pseudomonas sp.
?
-
-
-
-
additional information
arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate
855
Pseudomonas sp. MA
?
-
-
-
-
additional information
enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate
855
Pseudomonas sp. MA
?
-
-
-
-
additional information
arsenolysis reaction
855
Pseudomonas sp. MA
?
-
-
-
-
Other publictions for EC 6.2.1.9
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)
743968
Wu
Gene cloning, expression and ...
Aureobasidium pullulans, Aureobasidium pullulans CCTCC M2012223
Acta Microbiol. Sin.
54
919-925
2014
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1
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1
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10
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1
1
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1
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1
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10
-
1
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1
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850
Willibald
Preparative synthesis of beta- ...
Pseudomonas sp., Pseudomonas sp. AM1(2006)
Anal. Biochem.
227
363-367
1995
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1
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5
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848
Friedrich
-
Fermentative degradation of gl ...
Methanogenic bacterium
Arch. Microbiol.
156
398-404
1991
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849
Friedrich
-
Fermentative degradation of gl ...
Bacteria, Bacteria PerGlx1
Arch. Microbiol.
156
392-397
1991
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2
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2
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4
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851
Surendranathan
Malate thiokinase. Evidence fo ...
Pseudomonas sp., Pseudomonas sp. AM1(2006)
J. Biol. Chem.
258
3794-3798
1983
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5
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1
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2
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852
Hersh
Reaction of malate thiokinase ...
Pseudomonas sp.
J. Biol. Chem.
257
11633-11638
1982
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1
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1
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1
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853
Hersh
Half-of-the-sites reactivity i ...
Pseudomonas sp., Pseudomonas sp. MA
J. Biol. Chem.
256
1732-1737
1981
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8
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6
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6
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854
Elwell
Substrate-dependent dissociati ...
Pseudomonas sp., Pseudomonas sp. MA
J. Biol. Chem.
254
2434-2438
1979
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4
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1
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1
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855
Hersh
Malate thiokinase. The reactio ...
Pseudomonas sp., Pseudomonas sp. MA
J. Biol. Chem.
249
6264-6271
1974
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3
1
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8
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10
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3
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10
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856
Hersh
Malate adenosine triphosphate ...
Pseudomonas sp., Pseudomonas sp. MA
J. Biol. Chem.
248
7295-7303
1973
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1
3
1
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8
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8
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8
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