Publication:
The biotin enzyme family: Conserved structural motifs and domain rearrangements

dc.contributor.authorSarawut Jitrapakdeeen_US
dc.contributor.authorJohn C. Wallaceen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherUniversity of Adelaideen_US
dc.date.accessioned2018-07-24T03:19:42Z
dc.date.available2018-07-24T03:19:42Z
dc.date.issued2003-06-01en_US
dc.description.abstractThe 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.en_US
dc.identifier.citationCurrent Protein and Peptide Science. Vol.4, No.3 (2003), 217-229en_US
dc.identifier.doi10.2174/1389203033487199en_US
dc.identifier.issn13892037en_US
dc.identifier.other2-s2.0-0038811689en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/20721
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0038811689&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleThe biotin enzyme family: Conserved structural motifs and domain rearrangementsen_US
dc.typeReviewen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0038811689&origin=inwarden_US

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