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Literature summary extracted from

  • Kolhouse, J.F.; Stabler, S.P.; Allen, R.H.
    L-Methylmalonyl-CoA mutase from human placenta (1988), Methods Enzymol., 166, 407-414.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.99.2 0.2
-
(R/S)-2-methyl-3-oxopropanoyl-CoA
-
Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.4.99.2 72000
-
2 * 72000, SDS-PAGE in presence of 2-mercaptoethanol Homo sapiens
5.4.99.2 144000
-
gel filtration Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.2 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.2
-
Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.4.99.2 placenta
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.4.99.2 1.33
-
-
Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.2 (R)-2-methylmalonyl-CoA
-
Homo sapiens succinyl-CoA
-
?
5.4.99.2 (R/S)-2-methyl-3-oxopropanoyl-CoA
-
Homo sapiens succinyl-CoA
-
?

Subunits

EC Number Subunits Comment Organism
5.4.99.2 dimer 2 * 72000, SDS-PAGE in presence of 2-mercaptoethanol Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.99.2 7 9
-
Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.2 cobamide required, Km: 0.00005 mM Homo sapiens