Structure and function of biotin-dependent carboxylases
L Tong - Cellular and Molecular Life Sciences, 2013 - Springer
Biotin-dependent carboxylases include acetyl-CoA carboxylase (ACC), propionyl-CoA
carboxylase (PCC), 3-methylcrotonyl-CoA carboxylase (MCC), geranyl-CoA carboxylase …
carboxylase (PCC), 3-methylcrotonyl-CoA carboxylase (MCC), geranyl-CoA carboxylase …
Allosteric regulation of the biotin-dependent enzyme pyruvate carboxylase by acetyl-CoA
A Adina-Zada, TN Zeczycki… - Biochemical Society …, 2012 - portlandpress.com
The activity of the biotin-dependent enzyme pyruvate carboxylase from many organisms is
highly regulated by the allosteric activator acetyl-CoA. A number of X-ray crystallographic …
highly regulated by the allosteric activator acetyl-CoA. A number of X-ray crystallographic …
Mechanistic insight into allosteric activation of human pyruvate carboxylase by acetyl-CoA
P Chai, P Lan, S Li, D Yao, C Chang, M Cao, Y Shen… - Molecular Cell, 2022 - cell.com
Pyruvate carboxylase (PC) catalyzes the two-step carboxylation of pyruvate to produce
oxaloacetate, playing a key role in the maintenance of metabolic homeostasis in cells. Given …
oxaloacetate, playing a key role in the maintenance of metabolic homeostasis in cells. Given …
Ceramide-tamoxifen regimen targets bioenergetic elements in acute myelogenous leukemia1
The objective of our study was to determine the mechanism of action of the short-chain
ceramide analog, C6-ceramide, and the breast cancer drug, tamoxifen, which we show …
ceramide analog, C6-ceramide, and the breast cancer drug, tamoxifen, which we show …
Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli
AD Lietzan, AL Menefee, TN Zeczycki, S Kumar… - Biochemistry, 2011 - ACS Publications
Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to
oxaloacetate, an important anaplerotic reaction in mammalian tissues. To effect catalysis …
oxaloacetate, an important anaplerotic reaction in mammalian tissues. To effect catalysis …
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 …
its intermediates and also participates in the first step of gluconeogenesis. This large …
Design and construction of artificial biological systems for one-carbon utilization
W Zhong, H Li, Y Wang - BioDesign Research, 2023 - spj.science.org
The third-generation (3G) biorefinery aims to use microbial cell factories or enzymatic
systems to synthesize value-added chemicals from one-carbon (C1) sources, such as CO2 …
systems to synthesize value-added chemicals from one-carbon (C1) sources, such as CO2 …
Allosteric regulation alters carrier domain translocation in pyruvate carboxylase
Y Liu, MM Budelier, K Stine, M St. Maurice - Nature communications, 2018 - nature.com
Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to
oxaloacetate. The reaction occurs in two separate catalytic domains, coupled by the long …
oxaloacetate. The reaction occurs in two separate catalytic domains, coupled by the long …
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 …
multiple reactions between spatially distinct active sites. Pyruvate carboxylase (PC), a …
Novel Insights into the Biotin Carboxylase Domain Reactions of Pyruvate Carboxylase from Rhizobium etli
TN Zeczycki, AL Menefee, A Adina-Zada… - Biochemistry, 2011 - ACS Publications
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 …
carboxylase domain of pyruvate carboxylase from R. etli (Re PC) is common to the biotin …