Catalytic synthesis of cyclic guanidines via hydrogen atom transfer and radical-polar crossover

S Ohuchi, H Koyama, H Shigehisa - ACS Catalysis, 2021 - ACS Publications
Cyclic guanidines are found in many biologically active compounds and natural products.
Further, the formation of the atypical seven-membered ring of cyclic guanidine remains …

Pyruvate carboxylase, structure and function

M Valle - Macromolecular Protein Complexes: Structure and …, 2017 - Springer
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 …

Allosteric Site at the Biotin Carboxylase Dimer Interface Mediates Activation and Inhibition in Staphylococcus aureus Pyruvate Carboxylase

AJ Laseke, TJ Boram, NO Schneider, JR Lohman… - Biochemistry, 2023 - ACS Publications
Allosteric regulation of the essential anaplerotic enzyme, pyruvate carboxylase (PC), is vital
for metabolic homeostasis. PC catalyzes the bicarbonate-and ATP-dependent carboxylation …

A substrate-induced biotin binding pocket in the carboxyltransferase domain of pyruvate carboxylase

AD Lietzan, MS Maurice - Journal of Biological Chemistry, 2013 - ASBMB
Biotin-dependent enzymes catalyze carboxyl transfer reactions by efficiently coordinating
multiple reactions between spatially distinct active sites. Pyruvate carboxylase (PC), a …

Kinetic and Thermodynamic Analysis of Acetyl-CoA Activation of Staphylococcus aureus Pyruvate Carboxylase

LE Westerhold, LC Bridges, SR Shaikh… - Biochemistry, 2017 - ACS Publications
Allosteric regulation of pyruvate carboxylase (PC) activity is pivotal to maintaining metabolic
homeostasis. In contrast, dysregulated PC activity contributes to the pathogenesis of …

Pyruvate occupancy in the carboxyl transferase domain of pyruvate carboxylase facilitates product release from the biotin carboxylase domain through an …

LE Westerhold, SL Adams, HL Bergman… - Biochemistry, 2016 - ACS Publications
Protein structure, ligand binding, and catalytic turnover contributes to the governance of
catalytic events occurring at spatially distinct domains in multifunctional enzymes …

Mechanisms of Inhibition of Rhizobium etli Pyruvate Carboxylase by l-Aspartate

C Sirithanakorn, A Adina-Zada, JC Wallace… - Biochemistry, 2014 - ACS Publications
l-Aspartate is a regulatory feedback inhibitor of the biotin-dependent enzyme pyruvate
carboxylase in response to increased levels of tricarboxylic acid cycle intermediates …

Investigation of the Roles of Allosteric Domain Arginine, Aspartate, and Glutamate Residues of Rhizobium etli Pyruvate Carboxylase in Relation to Its Activation by …

C Sirithanakorn, S Jitrapakdee, PV Attwood - Biochemistry, 2016 - ACS Publications
The mechanism of allosteric activation of pyruvate carboxylase by acetyl CoA is not fully
understood. Here we have examined the roles of residues near the acetyl CoA binding site …

The role of the phosphate groups of trinitrophenyl adenosine 5′-triphosphate (TNP-ATP) in allosteric activation of pyruvate carboxylase and the inhibition of acetyl …

K Rattanapornsompong, C Sirithanakorn… - Archives of Biochemistry …, 2021 - Elsevier
A previous study showed that 2′-3′-O-(2, 4, 6-trinitrophenyl) adenosine 5′-triphosphate
(TNP-ATP) was a weak allosteric activator of Rhizobium etli pyruvate carboxylase (RePC) in …

[HTML][HTML] Residues in the acetyl CoA binding site of pyruvate carboxylase involved in allosteric regulation

K Choosangtong, C Sirithanakorn, A Adina-Zada… - FEBS letters, 2015 - Elsevier
We have examined the roles of Asp1018, Glu1027, Arg469 and Asp471 in the allosteric
domain of Rhizobium etli pyruvate carboxylase. Arg469 and Asp471 interact directly with the …