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Literature summary extracted from

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

General Stability

EC Number General Stability Organism
2.1.3.1 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.
2.1.3.1 glycerol, 20% retards dissociation of 12S and 6S-biotinyl subunit Propionibacterium sp.
2.1.3.1 polyvalent anions stabilize Propionibacterium sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.1 (S)-methylmalonyl-CoA
-
 Propionibacterium sp.
2.1.3.1 2-oxobutyrate
-
 Propionibacterium sp.
2.1.3.1 3-methyloxaloacetate strong Propionibacterium sp.
2.1.3.1 Avidin strong Propionibacterium sp.
2.1.3.1 coenzyme A
-
 Propionibacterium sp.
2.1.3.1 additional information no inhibition by metal chelating agents, such as EDTA Propionibacterium sp.
2.1.3.1 oxalate
-
 Propionibacterium sp.
2.1.3.1 oxaloacetate
-
 Propionibacterium sp.
2.1.3.1 propionyl pantetheine
-
 Propionibacterium sp.
2.1.3.1 propionyl-CoA
-
 Propionibacterium sp.
2.1.3.1 pyruvate
-
 Propionibacterium sp.
2.1.3.1 SH-reagents weak Propionibacterium sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.1 additional information
-
 additional information kinetics and mechanism Propionibacterium sp.
2.1.3.1 0.0077
-
 (2S)-methylmalonyl-coenzyme A
-
 Propionibacterium sp.
2.1.3.1 0.034
-
 propionyl-CoA
-
 Propionibacterium sp.
2.1.3.1 0.035
-
 malonyl-CoA
-
 Propionibacterium sp.
2.1.3.1 0.063
-
 oxaloacetate
-
 Propionibacterium sp.
2.1.3.1 0.25
-
 butyryl-CoA
-
 Propionibacterium sp.
2.1.3.1 0.5
-
 acetyl-CoA
-
 Propionibacterium sp.
2.1.3.1 0.77
-
 pyruvate
-
 Propionibacterium sp.

Localization

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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.3.1 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)

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

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.1 Propionibacterium sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.1
-
 Propionibacterium sp.

Reaction

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.3.1 40
-
-
 Propionibacterium sp.

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.1.3.1 More structure Propionibacterium sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.3.1 5.5 7.8 broad Propionibacterium sp.

Cofactor

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.3.1 0.000018
-
 oxalate
-
 Propionibacterium sp.
2.1.3.1 0.00004
-
 (S)-methylmalonyl-CoA
-
 Propionibacterium sp.
2.1.3.1 0.00049
-
 propionyl-CoA
-
 Propionibacterium sp.
2.1.3.1 0.0007
-
 oxaloacetate
-
 Propionibacterium sp.
2.1.3.1 0.003
-
 3-methyloxaloacetate
-
 Propionibacterium sp.
2.1.3.1 0.003 0.007 propionyl pantetheine
-
 Propionibacterium sp.
2.1.3.1 0.0063
-
 coenzyme A
-
 Propionibacterium sp.
2.1.3.1 0.0089
-
 pyruvate
-
 Propionibacterium sp.
2.1.3.1 0.025
-
 2-oxobutyrate
-
 Propionibacterium sp.