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Pyruvate carboxylase

International Journal of Biochemistry and Cell Biology, 1998
Pyruvate carboxylase [EC 6.4.1.1] is a member of the family of biotin-dependent carboxylases and is found widely among eukaryotic tissues and in many prokaryotic species. It catalyses the ATP-dependent carboxylation of pyruvate to form oxaloacetate which may be utilised in the synthesis of glucose, fat, some amino acids or their derivatives and several
Sarawut Jitrapakdee   +2 more
exaly   +4 more sources

“Pyruvate Carboxylase, Structure and Function”

Sub-cellular biochemistry, 2017
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 enzyme is multifunctional, and each subunit contains two active sites that catalyze two consecutive reactions that lead to the carboxylation of pyruvate into oxaloacetate,
M. Valle
openaire   +3 more sources

Pyruvate carboxylase

Enzyme Active Sites and their Reaction Mechanisms, 2021
H. Morrison
openaire   +2 more sources

Erianin suppresses proliferation and migration of cancer cells in a pyruvate carboxylase-dependent manner.

Fitoterapia, 2022
Erianin is a natural small molecule dibenzyl compound extracted from Dendrobium officinale or Dendrobium chrysotoxum. Studies show erianin has many pharmacological functions such as antioxidant, antibacterial, antiviral, improving diabetic nephropathy ...
Jing Hong   +7 more
semanticscholar   +1 more source

Identification of Pyruvate Carboxylase as the Cellular Target of Natural Bibenzyls with Potent Anticancer Activity against Hepatocellular Carcinoma via Metabolic Reprogramming.

Journal of Medicinal Chemistry, 2021
Cancer cell proliferation in some organs often depends on conversion of pyruvate to oxaloacetate via pyruvate carboxylase (PC) for replenishing the tricarboxylic acid cycle to support biomass production.
Yuwen Sheng   +19 more
semanticscholar   +1 more source

Pyruvate carboxylase deficiency

Journal of Inherited Metabolic Disease, 1984
AbstractThe causes of congenital lactic acidaemia are outlined. Isolated pyruvate carboxylase deficiency is reviewed in detail with a report of a recent case and a discussion of the biochemical consequences. Other causes of defective pyruvate carboxylation are described, particularly the combined carboxylase defects.
K, Bartlett   +4 more
openaire   +2 more sources

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