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Literature summary for 5.4.99.2 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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
placenta
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 9
-
Homo sapiens

Cofactor

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