Biotin carboxylation domain

Definition

Biotin-dependent carboxylase enzymes perform a two step reaction. Enzyme-bound biotin is first carboxylated by bicarbonated and ATP and the carboxyl group temporarily bound to biotin is subsequently transferred to an acceptor substrate such as pyruvate or acetyl-CoA. The first step is mediated by the BC domain common to all biotin-dependent carboxylases PMID:12769720. The BC domain can be divided in three subdomains (N-terminal, central and C-terminal). The N-terminal region provides part of the active site; the central region corresponds to the ATP-grasp domain, which is common to many ATP-dependent enzymes involved in macromolecular synthesis PMID:8564538. The ATP-grasp module directly binds the ATP molecule. The C-terminal subdomain is involved in dimer formation. Several structure of the BC domain have been solved [[cite:PMID:14993673], [cite:PMID:10821865]]. The central module is splayed significantly away from the main body of the domain and is able to rotate of approximately 45 degree upon nucleotide binding thereby closing off the active site pocket PMID:10821865.

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (5 proteins: gene, accession, name)

• ACACA
• ACACB
• MCCC1
• PC
• PCCA