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Literature summary extracted from

  • Kolhouse, J.F.; Allen, R.H.
    Recognition of two intracellular cobalamin binding proteins and their identification as methylmalonyl-CoA mutase and methionine synthetase (1977), Proc. Natl. Acad. Sci. USA, 74, 921-925.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.4.99.2 150000
-
 gel filtration Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.2 additional information Oryctolagus cuniculus acts as a cobalamin binding protein ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.13 Oryctolagus cuniculus
-
-
-
5.4.99.2 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.13 liver
-
 Oryctolagus cuniculus
-
5.4.99.2 liver
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.2 (R)-2-methylmalonyl-CoA
-
 Oryctolagus cuniculus succinyl-CoA
-
 ?
5.4.99.2 additional information acts as a cobalamin binding protein Oryctolagus cuniculus ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.13 vitamin B12 enzyme contains a derivative of vitamin B12 as prosthetic group Oryctolagus cuniculus