Biotin-dependent carboxylases include acetyl-CoA carboxylase (ACC), propionyl-CoA
carboxylase (PCC), 3-methylcrotonyl-CoA carboxylase (MCC), geranyl-CoA carboxylase …

In this review we examine the effects of the allosteric activator, acetyl CoA on both the
structure and catalytic activities of pyruvate carboxylase. We describe how the binding of …

LytS/LytTR-type histidine kinase/response regulator systems regulate crucial host-specific
mechanisms during infection of human or plant hosts. Escherichia coli has two of them, and …

Pyruvate carboxylase is a metabolic enzyme that fuels the tricarboxylic acid cycle with one of
its intermediates and also participates in the first step of gluconeogenesis. This large …

Biotin-dependent enzymes catalyze carboxyl transfer reactions by efficiently coordinating
multiple reactions between spatially distinct active sites. Pyruvate carboxylase (PC), a …

The catalytic mechanism of the MgATP-dependent carboxylation of biotin in the biotin
carboxylase domain of pyruvate carboxylase from R. etli (Re PC) is common to the biotin …

Biotin-dependent enzymes catalyze carboxylation, decarboxylation and transcarboxylation
reactions that participate in the primary metabolism of a wide range of organisms. In all …

Pyruvate carboxylase (PC) is a biotin-dependent enzyme that catalyzes the MgATP-and
bicarbonate-dependent carboxylation of pyruvate to oxaloacetate, an important anaplerotic …

The characterization of functionally diverse enzyme superfamilies provides the opportunity
to identify evolutionarily conserved catalytic strategies, as well as amino acid substitutions …

Numerous steady‐state kinetic studies have examined the complex catalytic reaction
mechanism of the multifunctional enzyme, pyruvate carboxylase (PC). Through initial …