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Literature summary for 2.1.3.1 extracted from

  • Wood, H.G.
    Transcarboxylase (1972), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 6, 83-115.
No PubMed abstract available

General Stability

General Stability Organism
alkaline pH, low ionic strength, monovalent ions, low protein concentration and elevated temperatures favor dissociation to inactive 5S, 6S and 1.3S subunits Propionibacterium sp.
glycerol, 20% retards dissociation of 12S and 6S-biotinyl subunit Propionibacterium sp.
polyvalent anions stabilize Propionibacterium sp.

Inhibitors

Inhibitors Comment Organism Structure
(S)-methylmalonyl-CoA
-
Propionibacterium sp.
2-oxobutyrate
-
Propionibacterium sp.
3-methyloxaloacetate strong Propionibacterium sp.
Avidin strong Propionibacterium sp.
coenzyme A
-
Propionibacterium sp.
additional information no inhibition by metal chelating agents, such as EDTA Propionibacterium sp.
oxalate
-
Propionibacterium sp.
oxaloacetate
-
Propionibacterium sp.
propionyl pantetheine
-
Propionibacterium sp.
propionyl-CoA
-
Propionibacterium sp.
pyruvate
-
Propionibacterium sp.
SH-reagents weak Propionibacterium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics and mechanism Propionibacterium sp.
0.0077
-
(2S)-methylmalonyl-coenzyme A
-
Propionibacterium sp.
0.034
-
propionyl-CoA
-
Propionibacterium sp.
0.035
-
malonyl-CoA
-
Propionibacterium sp.
0.063
-
oxaloacetate
-
Propionibacterium sp.
0.25
-
butyryl-CoA
-
Propionibacterium sp.
0.5
-
acetyl-CoA
-
Propionibacterium sp.
0.77
-
pyruvate
-
Propionibacterium sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Propionibacterium sp. 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ requirement Propionibacterium sp.
additional information no additional metal requirement Propionibacterium sp.
Zn2+ requirement, can replace Co2+ Propionibacterium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
two active forms of enzyme: 18S and 16S, the 16S species arises from 18S species by loss of a 6S biotin, Co, Zn subunit Propionibacterium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
propionyl-CoA + oxaloacetate Propionibacterium sp.
-
(S)-methylmalonyl-CoA + pyruvate
-
r

Organism

Organism UniProt Comment Textmining
Propionibacterium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Propionibacterium sp.

Reaction

Reaction Comment Organism Reaction ID
(S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate mechanism Propionibacterium sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
40
-
-
Propionibacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetoacetyl-CoA + oxaloacetate carboxylation at about 2.5% the rate of propionyl-CoA Propionibacterium sp. 3-oxoglutaryl-CoA + pyruvate
-
?
acetyl-CoA + oxaloacetate carboxylation at about 50% the rate of propionyl-CoA Propionibacterium sp. malonyl-CoA + pyruvate
-
r
butyryl-CoA + oxaloacetate carboxylation at about 10% the rate of propionyl-CoA Propionibacterium sp. ethylmalonyl-CoA + pyruvate
-
?
additional information 2-oxobutyrate, 2-oxovalerate, 2-oxoglutarate, 3-oxoglutarate cannot replace pyruvate and is no C1-donor Propionibacterium sp. ?
-
?
propionyl-CoA + oxaloacetate
-
Propionibacterium sp. (S)-methylmalonyl-CoA + pyruvate
-
r
propionyl-CoA + oxaloacetate
-
Propionibacterium sp. (S)-methylmalonyl-CoA + pyruvate enzyme specific for the S isomer r

Subunits

Subunits Comment Organism
More structure Propionibacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 7.8 broad Propionibacterium sp.

Cofactor

Cofactor Comment Organism Structure
biotin requirement Propionibacterium sp.
biotin biotinyl-enzyme, 6 mol per 18S and 4 mol per 16S enzyme species Propionibacterium sp.
additional information no ATP requirement Propionibacterium sp.

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000018
-
oxalate
-
Propionibacterium sp.
0.00004
-
(S)-methylmalonyl-CoA
-
Propionibacterium sp.
0.00049
-
propionyl-CoA
-
Propionibacterium sp.
0.0007
-
oxaloacetate
-
Propionibacterium sp.
0.003
-
3-methyloxaloacetate
-
Propionibacterium sp.
0.003 0.007 propionyl pantetheine
-
Propionibacterium sp.
0.0063
-
coenzyme A
-
Propionibacterium sp.
0.0089
-
pyruvate
-
Propionibacterium sp.
0.025
-
2-oxobutyrate
-
Propionibacterium sp.