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Literature summary for 6.4.1.4 extracted from

  • Schiele, U.; Niedermeier, R.; Sturzer, M.; Lynen, F.
    Investigations of the structure of 3-methylcrotonyl-CoA carboxylase from Achromobacter (1975), Eur. J. Biochem., 60, 259-266.
    View publication on PubMed
Search for more literature for 6.4.1.4

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
78000
-
 x * 78000, biotin-free subunit A, + x * 96000, biotin-containing subunit, SDS-PAGE Achromobacter sp.
96000
-
 x * 78000, biotin-free subunit A, + x * 96000, biotin-containing subunit, SDS-PAGE Achromobacter sp.
760000
-
 analytical ultracentrifugation Achromobacter sp.

Organism

Organism UniProt Comment Textmining
Achromobacter sp.
-
 IVS
-
Achromobacter sp. IVS
-
 IVS
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-methylcrotonoyl-CoA + HCO3-
-
 Achromobacter sp. ADP + phosphate + 3-methylglutaconyl-CoA
-
 ?
ATP + 3-methylcrotonoyl-CoA + HCO3-
-
 Achromobacter sp. IVS ADP + phosphate + 3-methylglutaconyl-CoA
-
 ?

Subunits

Subunits Comment Organism
? x * 78000, biotin-free subunit A, + x * 96000, biotin-containing subunit, SDS-PAGE Achromobacter sp.

Cofactor

Cofactor Comment Organism Structure
biotin enzyme contains biotin Achromobacter sp.
biotin biotin is bound to the heavier subunit Achromobacter sp.