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Literature summary for 6.4.1.6 extracted from

  • Boyd, J.M.; Ellsworth, H.; Ensign, S.A.
    Bacterial acetone carboxylase is a manganese-dependent metalloenzyme (2004), J. Biol. Chem., 279, 46644-46651.
    View publication on PubMed
Search for more literature for 6.4.1.6

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ enzyme contains 1.9 Mn2+ per alpha2beta2gamma2 multimer, tightly bound and not removed upon dialysis against various metal ion chelators. Presence of a mononuclear Mn2+ center with possible spin coupling of two mononuclear sites. Manganese is essential for acetone carboxylation Rhodobacter capsulatus
Mn2+ tightly bound to the enzyme and not removed upon dialysis against various metal chelators. Presence of a mononuclear Mn2+ center, with possible spin coupling of two mononuclear sites. Mn2+ is essential for acetone carboxylation Rhodobacter capsulatus

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
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Rhodobacter capsulatus B10
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rhodobacter capsulatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetone + CO2 + ATP + H2O
-
 Rhodobacter capsulatus acetoacetate + AMP + phosphate
-
 ?
acetone + CO2 + ATP + H2O
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 Rhodobacter capsulatus B10 acetoacetate + AMP + phosphate
-
 ?