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 …

Enzymatic strategies and biocatalysts for amide bond formation: tricks of the trade outside of the ribosome

A Goswami, SG Van Lanen - Molecular BioSystems, 2015 - pubs.rsc.org
Amide bond-containing (ABC) biomolecules are some of the most intriguing and functionally
significant natural products with unmatched utility in medicine, agriculture and …

CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase

JP López-Alonso, M Lázaro, D Gil-Cartón… - Nature …, 2022 - nature.com
Pyruvate carboxylase (PC) is a tetrameric enzyme that contains two active sites per subunit
that catalyze two consecutive reactions. A mobile domain with an attached prosthetic biotin …

The overlooked role of a biotin precursor for marine bacteria-desthiobiotin as an escape route for biotin auxotrophy

G Wienhausen, S Bruns, S Sultana… - The ISME …, 2022 - academic.oup.com
Biotin (vitamin B7) is involved in a wide range of essential biochemical reactions and a
crucial micronutrient that is vital for many pro-and eukaryotic organisms. The few biotin …

The enzymes of biotin dependent CO2 metabolism: What structures reveal about their reaction mechanisms

GL Waldrop, HM Holden, MS Maurice - Protein Science, 2012 - Wiley Online Library
Biotin is the major cofactor involved in carbon dioxide metabolism. Indeed, biotin‐dependent
enzymes are ubiquitous in nature and are involved in a myriad of metabolic processes …

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 …

Nickel‐Catalyzed CO2 Rearrangement of Enol Metal Carbonates for the Efficient Synthesis of β‐Ketocarboxylic Acids

R Ninokata, T Yamahira, G Onodera… - Angewandte …, 2017 - Wiley Online Library
Methylene‐1, 3‐dioxolan‐2‐ones underwent oxidative addition of a Ni0 catalyst in the
presence of Me2Al (OMe), followed by a coupling reaction with alkynes, to form δ, ϵ …

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 …

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 …

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 …