Publication: The biotin enzyme family: Conserved structural motifs and domain rearrangements
Issued Date
2003-06-01
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13892037
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2-s2.0-0038811689
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Mahidol University
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SCOPUS
Bibliographic Citation
Current Protein and Peptide Science. Vol.4, No.3 (2003), 217-229
Suggested Citation
Sarawut Jitrapakdee, John C. Wallace The biotin enzyme family: Conserved structural motifs and domain rearrangements. Current Protein and Peptide Science. Vol.4, No.3 (2003), 217-229. doi:10.2174/1389203033487199 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/20721
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Title
The biotin enzyme family: Conserved structural motifs and domain rearrangements
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Abstract
The biotin carboxylase family is comprised of a group of enzymes that utilize a covalently bound prosthetic group, biotin, as a cofactor. These enzymes, which include acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranoyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase transcarboxylase and urea amidolyase, are found in diverse biosynthetic pathways in both prokaryotes and eukaryotes. The reactions catalyzed by most members of this group of enzymes share two common features: (1) carboxylation of biotin, apparently via the formation of a carboxyphosphate intermediate, followed by (2) transcarboxylation of CO2 from biotin to specific acceptor molecules to yield different products. Structural determinations by NMR and X-ray crystallography, complemented by mutagenesis studies, have identified some motifs that are structurally or catalytically important. Analysis of the amino acid sequences of a number of biotin carboxylases not only shows remarkable similarities within certain domains but also that there appears to have been domain rearrangements between groups of carboxylases. Acyl-coenzyme A derivatives, which bind either as substrates or as allosteric regulators of the biotin carboxylases, do not appear to share any of the CoA binding motifs that have been identified in other CoA-SH/acyl-CoA binding proteins. Further comparisons of biotin-dependent carboxylases with other groups of enzymes in the protein data bank reveal that this family of biotin enzymes has strong similarities in specific domains to a number of ATP-utilizing enzymes and to the lipoyl-containing enzymes. These structural homologies are so extensive as to be highly suggestive of evolutionary relationships between biotin carboxylases and these other enzymes.