<p>Pyruvate carboxylase (<db_xref db="EC" dbkey="6.4.1.1"/>) (PC), a member of the biotin-dependentenzyme family, is involved in the gluconeogenesis by mediating thecarboxylation of pyruvate to oxaloacetate. Biotin-dependent carboxylaseenzymes perform a two step reaction. Enzyme-bound biotin is first carboxylatedby bicarbonate and ATP and the carboxyl group temporarily bound to biotin issubsequently transferred to an acceptor substrate such as pyruvate [<cite idref="PUB00015343"/>]. PC hasthree functional domains: a biotin carboxylase (BC) domain,a carboxyltransferase (CT) domain which perform the second part of thereaction and a biotinyl domain [<cite idref="PUB00015403"/>, <cite idref="PUB00015404"/>]. The mechanism by whichthe carboxyl group is transferred from the carboxybiotin to the pyruvate is notwell understood.</p><p>The pyruvate carboxyltransferase domain is also found in other pyruvatebinding enzymes and acetyl-CoA dependent enzymes suggesting that this domaincan be associated with different enzymatic activities.</p><p>This domain is found towards the N-terminal region of various aldolase enzymes. This N-terminal TIM barrel domain [<cite idref="PUB00016385"/>] interacts with the C-terminal domain. The C-terminal DmpG_comm domain (<db_xref db="INTERPRO" dbkey="IPR012425"/>) is thought to promote heterodimerisation with members of <db_xref db="INTERPRO" dbkey="IPR003361"/> to form a bifunctional aldolase-dehydrogenase [<cite idref="PUB00016385"/>]. </p> Pyruvate carboxyltransferase