BRENDA - Enzyme Database show
show all sequences of 4.1.1.38

Phosphoenolpyruvate carboxytransphosphorylase. An investigation of the mechanism with 18 O

O'Brien, W.E.; Singleton, R.; Wood, H.G.; Biochemistry 12, 5247-5253 (1973)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Propionibacterium freudenreichii subsp. shermanii
-
-
-
Reaction
Reaction
Commentary
Organism
diphosphate + oxaloacetate = phosphate + phosphoenolpyruvate + CO2
the mechanism involves the formation of pentavalent diphosphoenolpyruvate which then is carboxylated to yield oxaloacetate and diphosphate
Propionibacterium freudenreichii subsp. shermanii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phosphate + phosphoenolpyruvate + CO2
-
33095
Propionibacterium freudenreichii subsp. shermanii
diphosphate + oxaloacetate
-
33095
Propionibacterium freudenreichii subsp. shermanii
-
phosphoenolpyruvate + phosphate
the pentavalent diphosphoenolpyruvate breaks down irreversibly to enolpyruvate and diphosphate
33095
Propionibacterium freudenreichii subsp. shermanii
pyruvate + diphosphate
-
33095
Propionibacterium freudenreichii subsp. shermanii
ir
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phosphate + phosphoenolpyruvate + CO2
-
33095
Propionibacterium freudenreichii subsp. shermanii
diphosphate + oxaloacetate
-
33095
Propionibacterium freudenreichii subsp. shermanii
-
phosphoenolpyruvate + phosphate
the pentavalent diphosphoenolpyruvate breaks down irreversibly to enolpyruvate and diphosphate
33095
Propionibacterium freudenreichii subsp. shermanii
pyruvate + diphosphate
-
33095
Propionibacterium freudenreichii subsp. shermanii
ir
Other publictions for EC 4.1.1.38
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)
748197
Chiba
Discovery of PPi-type phospho ...
Entamoeba histolytica
J. Biol. Chem.
290
23960-23970
2015
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726738
Zhou
Atypical glycolysis in Clostri ...
no activity in Clostridium thermocellum
Appl. Environ. Microbiol.
79
3000-3008
2013
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662039
Liu
Phosphoenolpyruvate carboxykin ...
Agrobacterium tumefaciens
J. Bacteriol.
187
6039-6045
2005
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660748
Kim
Effect of overexpression of Ac ...
Actinobacillus succinogenes
Appl. Environ. Microbiol.
70
1238-1241
2004
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641615
Asanuma
Molecular characterization, en ...
Selenomonas ruminantium
Microbiology
147
681-690
2001
1
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2
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2
1
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1
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1
1
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1
1
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33096
Wood
Phosphorylation enzymes of the ...
Acidipropionibacterium acidipropionici, Propionibacterium freudenreichii, Propionibacterium freudenreichii subsp. shermanii
Proc. Natl. Acad. Sci. USA
82
312-315
1985
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33097
Eden
-
Autotrophic CO2 fixation in Ac ...
Acetobacterium woodii
Arch. Microbiol.
135
68-73
1983
1
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33093
Perl
Phosphoenol-pyruvate-carboxyla ...
Gossypium hirsutum, Sorghum bicolor
Planta
139
239-243
1978
1
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3
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2
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33098
Wood
Properties of carboxytransphos ...
Propionibacterium freudenreichii subsp. shermanii
Adv. Enzymol. Relat. Areas Mol. Biol.
45
85-155
1977
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33094
O'Brien
Carboxytransphosphorylase. 8. ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
249
4917-4925
1974
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33092
Willard
Formation of enolpyruvate in t ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
12
5241-5246
1973
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33095
O'Brien
Phosphoenolpyruvate carboxytra ...
Propionibacterium freudenreichii subsp. shermanii
Biochemistry
12
5247-5253
1973
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33091
Lochmueller
Phosphoenolpyruvate carboxytra ...
Propionibacterium freudenreichii subsp. shermanii
J. Biol. Chem.
241
5678-5691
1966
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12
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12
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