Title |
Early evolution of the biotin-dependent carboxylase family
|
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Published in |
BMC Ecology and Evolution, August 2011
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DOI | 10.1186/1471-2148-11-232 |
Pubmed ID | |
Authors |
Jonathan Lombard, David Moreira |
Abstract |
Biotin-dependent carboxylases are a diverse family of carboxylating enzymes widespread in the three domains of life, and thus thought to be very ancient. This family includes enzymes that carboxylate acetyl-CoA, propionyl-CoA, methylcrotonyl-CoA, geranyl-CoA, acyl-CoA, pyruvate and urea. They share a common catalytic mechanism involving a biotin carboxylase domain, which fixes a CO₂ molecule on a biotin carboxyl carrier peptide, and a carboxyl transferase domain, which transfers the CO₂ moiety to the specific substrate of each enzyme. Despite this overall similarity, biotin-dependent carboxylases from the three domains of life carrying their reaction on different substrates adopt very diverse protein domain arrangements. This has made difficult the resolution of their evolutionary history up to now. |
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Demographic breakdown
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Mendeley readers
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