The Rat Pyruvate Carboxylase Gene Structure
نویسندگان
چکیده
منابع مشابه
Structure, function and regulation of pyruvate carboxylase.
Pyruvate carboxylase (PC; EC 6.4.1.1), a member of the biotin-dependent enzyme family, catalyses the ATP-dependent carboxylation of pyruvate to oxaloacetate. PC has been found in a wide variety of prokaryotes and eukaryotes. In mammals, PC plays a crucial role in gluconeogenesis and lipogenesis, in the biosynthesis of neurotransmitter substances, and in glucose-induced insulin secretion by panc...
متن کاملStructure, mechanism and regulation of pyruvate carboxylase.
PC (pyruvate carboxylase) is a biotin-containing enzyme that catalyses the HCO(3)(-)- and MgATP-dependent carboxylation of pyruvate to form oxaloacetate. This is a very important anaplerotic reaction, replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways. PC is therefore considered as an enzyme that is crucial for intermediary metabolism,...
متن کاملInhibitors of Pyruvate Carboxylase.
This review aims to discuss the varied types of inhibitors of biotin-dependent carboxylases, with an emphasis on the inhibitors of pyruvate carboxylase. Some of these inhibitors are physiologically relevant, in that they provide ways of regulating the cellular activities of the enzymes e.g. aspartate and prohibitin inhibition of pyruvate carboxylase. Most of the inhibitors that will be discusse...
متن کاملPurification and properties of rat brain pyruvate carboxylase.
Rat brain pyruvate carboxylase was purified 2000-fold and some of its properties and kinetic parameters were investigated. The use of (NH4)2SO4 gradient solubilization on a Celite column and precipitation with polyethylene glycol permitted purification to an estimated 20% purity. Except for a few subtle kinetic differences this enzyme is indistinguishable from rat liver pyruvate carboxylase.
متن کاملPyruvate Carboxylase from Chicken Liver
On the basis of initial velocity and product inhibition studies a nonclassical Ping Pong Bi Bi Uni Uni mechanism has been proposed for pyruvate carboxylase from chicken liver. The nonclassical feature of this mechanism is the proposal that each active site on the enzyme is composed of two separate and functionally distinct catalytic sites, i.e., a separate catalytic site exists for the reactant...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1997
ISSN: 0021-9258
DOI: 10.1074/jbc.272.33.20522