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ADP + carbamoyl phosphate
ATP + ?
ADP + carbamoylphosphate
?
ATP + oxamate + HCO3- + H+
ADP + phosphate + ?
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
additional information
?
-
ADP + carbamoyl phosphate
ATP + ?
-
-
-
?
ADP + carbamoyl phosphate
ATP + ?
-
at 0.3% of the rate obtained from pyruvate-carboxylation
-
-
?
ADP + carbamoyl phosphate
ATP + ?
-
-
-
?
ADP + carbamoyl phosphate
ATP + ?
-
-
-
?
ADP + carbamoylphosphate
?
reverse reaction is assessed by using substrate analogue carbamoylphosphate
-
-
r
ADP + carbamoylphosphate
?
reverse reaction is assessed by using substrate analogue carbamoylphosphate
-
-
r
ATP + pyruvate + HCO3-
?
-
anaplerotic CO2 fixation
-
-
?
ATP + pyruvate + HCO3-
?
-
anaplerotic CO2 fixation
-
-
?
ATP + pyruvate + HCO3-
?
-
pyruvate carboxylase deficiency in humans causes severe acidosis
-
-
?
ATP + pyruvate + HCO3-
?
Leptosphaeria michotii
-
one of the enzymes of the asparagine-pyruvate pathway
-
-
?
ATP + pyruvate + HCO3-
?
-
the enzyme occupies a strategic position in the intermediary metabolism of numerous tissues. In the gluconeogenic tissues, e.g. liver, kidney, it catalyzes the first step in the synthesis of glucose from pyruvate. During lipogenesis in liver, adipose tissue and mammary gland it participates in the synthesis of acetyl groups and reducing groups for transport from the mitochondria to the cytosol. In yet other tissues it fulfills an anaplerotic function
-
-
?
ATP + pyruvate + HCO3-
?
-
enzyme is necessary for growth in minimal medium with pyruvate as sole carbon source
-
-
?
ATP + pyruvate + HCO3-
?
-
enzyme synthesis is induced by pyruvate and repressed by tricarboxylic acid cycle intermediates
-
-
?
ATP + pyruvate + HCO3-
?
-
anaplerotic CO2 fixation
-
-
?
ATP + pyruvate + HCO3-
?
-
meets anaplerotic and/or biosynthetic needs in metabolism
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
ATP in form of MgATP2-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
the enzyme catalyzes a pivotal reaction in gluconeogenesis and lipid metabolism in liver, and is a regulatory enzyme in gluconeogenesis that catalyzes the biotin-dependent carboxylation of pyruvate to form oxaloacetate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
anaplerotic enzyme for growth on carbohydrates, reaction is a major bottleneck for amino acid production
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
role of anaplerosis in the central carbon metabolism and amino acid synthesis
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
cells containing the enzyme yield significantly more cell mass while generating less acetate
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
ATP in form of MgATP2-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
intact enzyme and PC-(BC) chain are able to cleave ATP in the presence of free D-biotin and absence of pyruvate
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
ATP in form of MgATP2-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate. In addition to de novo fatty acid synthesis, pyruvate carboxylase is also involved in glyceroneogenesis, a pathway for synthesizing glycerol required for fatty acid re-esterification. Physiological functions and regulation, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
the enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, insulin secretion and other cellular processes
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the enzyme plays a pivotal role in intermediary metabolism. It serves a critical anaplerotic function replenishing the Krebs cycle intermediates by catalyzing the conversion of pyruvate to oxaloacetate. In addition, pyruvate carboxylase controls the first step of hepatic gluconeogenesis, and is involved in lipogenesis
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
the overall catalysis by PC proceeds in two steps. First, the biotin carboxylase domain catalyzes the carboxylation of biotin, which is covalently linked to the biotin carboxylaseCP. Bicarbonate donates the carboxyl group, and ATP is hydrolyzed to ADP in this reaction. The carboxytransferase domain then catalyzes the transfer of the activated carboxyl group to pyruvate to produce the oxaloacetate product
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Leptosphaeria michotii
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
role in gluconeogenesis, lipogenesis, biosynthesis of neurotransmitter substances and in glucose-induced insulin secretion by pancreatic islets
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate. In addition to de novo fatty acid synthesis, pyruvate carboxylase is also involved in glyceroneogenesis, a pathway for synthesizing glycerol required for fatty acid re-esterification. Physiological functions and regulation, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
anaplerotic enzyme
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
ATP in form of MgATP2-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
pyruvate carboxylase, and thereby anaplerosis, is crucial for an appropriate rise in the ATP:ADP ratio in response to fuel metabolism
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate. In addition to de novo fatty acid synthesis, pyruvate carboxylase is also involved in glyceroneogenesis, a pathway for synthesizing glycerol required for fatty acid re-esterification. Physiological functions and regulation, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the enzyme is involved in mitochondrial metabolism
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
ATP in form of MgATP2-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
essential for normal growth
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Pyc1 and Pyc2 display different allosteric properties with respect to acetyl CoA activation and aspartate inhibition, with Pyc1 showing a higher degree of cooperativity than Pyc2, even in the absence of aspartate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Pyc1 and Pyc2 display different allosteric properties with respect to acetyl CoA activation and aspartate inhibition, with Pyc1 showing a higher degree of cooperativity than Pyc2, even in the absence of aspartate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
ATP in form of MgATP2-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
the enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, and other cellular processes
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
-
-
-
-
r
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
-
-
-
-
r
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + oxaloacetate + phosphate
-
-
-
-
r
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate. In addition to de novo fatty acid synthesis, pyruvate carboxylase is also involved in glyceroneogenesis, a pathway for synthesizing glycerol required for fatty acid re-esterification. Physiological functions and regulation, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
involvement of several ionisable residues in both ATP-cleavage and biotin carboxylation
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
Methanococcus sp.
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
Methanococcus sp.
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
additional information
?
-
-
HCO3--dependent ATP cleavage catalyzed in absence of pyruvate
-
-
?
additional information
?
-
-
ATP cleavage by the recombinantly expressed isolated biotin carboxylase domain, overview
-
-
?
additional information
?
-
-
enzyme deficiency is a rare autosomal recessive disease
-
-
?
additional information
?
-
-
in yeast, two metabolic pathways leading to the production of oxaloacetate are the pyruvate carboxylase-catalysed reaction and the glyoxylate cycle.When yeast is grown on acetate, pyruvate carboxylase-catalysed oxaloacetate formation is repressed but the glyoxylate cycle is active, and vice versa if grown on glucose minimal medium
-
-
?
additional information
?
-
-
starvation enhances pyruvate carboxylase activity, whereas diabetes also increases gluconeogenesis through enhanced uptake of substrate and increased flux through liver pyruvate carboxylase mice
-
-
?
additional information
?
-
-
the enzyme in adipocytes interacts with prohibitin, a protein involved in mitochondrial biogenesis
-
-
?
additional information
?
-
-
protein, but not the enzyme is essential for import and assembly of alcohol oxidase into peroxisomes
-
?
additional information
?
-
-
the transcarboxylase domain of pyruvate carboxylase is essential for assembly of the peroxisomal flavoenzyme alcohol oxidase
-
-
?
additional information
?
-
-
in yeast, two metabolic pathways leading to the production of oxaloacetate are the pyruvate carboxylase-catalysed reaction and the glyoxylate cycle.When yeast is grown on acetate, pyruvate carboxylase-catalysed oxaloacetate formation is repressed but the glyoxylate cycle is active, and vice versa if grown on glucose minimal medium
-
-
?
additional information
?
-
-
the enzyme interacts with the biotin protein ligase or holocarboxylase, EC 6.3.4.15, and is associated with the peroxisomal alcohol oxidase
-
-
?
additional information
?
-
-
protein, but not the enzyme is essential for import and assembly of alcohol oxidase into peroxisomes
-
?
additional information
?
-
-
the enzyme is regulated by a pyruvate carboxylase regulator, encoded by gene PA5437 or pycR, PycR inactivation results in 100 000fold attenuation of virulence in the rat lung in vivo, PycR is a regulator with pleiotropic effects on virulence factors, such as lipase and esterase expression and biofilm formation, which are important for maintenance of Pseudomonas aeruginosa in chronic lung infection, overview
-
-
?
additional information
?
-
beta-cells possess compensatory systems that are activated in response to suppression of pyruvate carboxylase nzyme levels. The compensatory events include allosteric activation of pyruvate carboxylase due to increased levels of acetyl-CoA and enhanced conversion of isocitrate to 2-oxoglutarate and downstream metabolites via the cytosolic, NADP-dependent isocitrate dehydrogenase
-
-
?
additional information
?
-
-
starvation enhances pyruvate carboxylase activity, whereas diabetes also increases gluconeogenesis through enhanced uptake of substrate and increased flux through liver pyruvate carboxylase rats
-
-
?
additional information
?
-
-
2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate is no substrate
-
-
?
additional information
?
-
in the absence of the biotin carboxylase domain, oxamate-stimulated decarboxylation of oxaloacetate, reaction of EC 4.1.1.3, proceeds through a simple ping-pong bi bi mechanism
-
-
?
additional information
?
-
-
in the absence of the biotin carboxylase domain, oxamate-stimulated decarboxylation of oxaloacetate, reaction of EC 4.1.1.3, proceeds through a simple ping-pong bi bi mechanism
-
-
?
additional information
?
-
in the absence of the biotin carboxylase domain, oxamate-stimulated decarboxylation of oxaloacetate, reaction of EC 4.1.1.3, proceeds through a simple ping-pong bi bi mechanism
-
-
?
additional information
?
-
-
in yeast, two metabolic pathways leading to the production of oxaloacetate are the pyruvate carboxylase-catalysed reaction and the glyoxylate cycle.When yeast is grown on acetate, pyruvate carboxylase-catalysed oxaloacetate formation is repressed but the glyoxylate cycle is active, and vice versa if grown on glucose minimal medium
-
-
?
additional information
?
-
thermodynamic activation parameters for the pyruvate carboxylase-catalyzed carboxylation of pyruvate are largely independent of acetyl-CoA
-
-
?
additional information
?
-
-
thermodynamic activation parameters for the pyruvate carboxylase-catalyzed carboxylation of pyruvate are largely independent of acetyl-CoA
-
-
?
additional information
?
-
thermodynamic activation parameters for the pyruvate carboxylase-catalyzed carboxylation of pyruvate are largely independent of acetyl-CoA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
additional information
?
-
ATP + pyruvate + HCO3-
?
-
anaplerotic CO2 fixation
-
-
?
ATP + pyruvate + HCO3-
?
-
anaplerotic CO2 fixation
-
-
?
ATP + pyruvate + HCO3-
?
-
pyruvate carboxylase deficiency in humans causes severe acidosis
-
-
?
ATP + pyruvate + HCO3-
?
Leptosphaeria michotii
-
one of the enzymes of the asparagine-pyruvate pathway
-
-
?
ATP + pyruvate + HCO3-
?
-
the enzyme occupies a strategic position in the intermediary metabolism of numerous tissues. In the gluconeogenic tissues, e.g. liver, kidney, it catalyzes the first step in the synthesis of glucose from pyruvate. During lipogenesis in liver, adipose tissue and mammary gland it participates in the synthesis of acetyl groups and reducing groups for transport from the mitochondria to the cytosol. In yet other tissues it fulfills an anaplerotic function
-
-
?
ATP + pyruvate + HCO3-
?
-
enzyme is necessary for growth in minimal medium with pyruvate as sole carbon source
-
-
?
ATP + pyruvate + HCO3-
?
-
enzyme synthesis is induced by pyruvate and repressed by tricarboxylic acid cycle intermediates
-
-
?
ATP + pyruvate + HCO3-
?
-
anaplerotic CO2 fixation
-
-
?
ATP + pyruvate + HCO3-
?
-
meets anaplerotic and/or biosynthetic needs in metabolism
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
the enzyme catalyzes a pivotal reaction in gluconeogenesis and lipid metabolism in liver, and is a regulatory enzyme in gluconeogenesis that catalyzes the biotin-dependent carboxylation of pyruvate to form oxaloacetate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
anaplerotic enzyme for growth on carbohydrates, reaction is a major bottleneck for amino acid production
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
role of anaplerosis in the central carbon metabolism and amino acid synthesis
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
cells containing the enzyme yield significantly more cell mass while generating less acetate
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate. In addition to de novo fatty acid synthesis, pyruvate carboxylase is also involved in glyceroneogenesis, a pathway for synthesizing glycerol required for fatty acid re-esterification. Physiological functions and regulation, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
the enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, insulin secretion and other cellular processes
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the enzyme plays a pivotal role in intermediary metabolism. It serves a critical anaplerotic function replenishing the Krebs cycle intermediates by catalyzing the conversion of pyruvate to oxaloacetate. In addition, pyruvate carboxylase controls the first step of hepatic gluconeogenesis, and is involved in lipogenesis
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
role in gluconeogenesis, lipogenesis, biosynthesis of neurotransmitter substances and in glucose-induced insulin secretion by pancreatic islets
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate. In addition to de novo fatty acid synthesis, pyruvate carboxylase is also involved in glyceroneogenesis, a pathway for synthesizing glycerol required for fatty acid re-esterification. Physiological functions and regulation, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
anaplerotic enzyme
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
pyruvate carboxylase, and thereby anaplerosis, is crucial for an appropriate rise in the ATP:ADP ratio in response to fuel metabolism
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate. In addition to de novo fatty acid synthesis, pyruvate carboxylase is also involved in glyceroneogenesis, a pathway for synthesizing glycerol required for fatty acid re-esterification. Physiological functions and regulation, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the enzyme is involved in mitochondrial metabolism
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
essential for normal growth
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Pyc1 and Pyc2 display different allosteric properties with respect to acetyl CoA activation and aspartate inhibition, with Pyc1 showing a higher degree of cooperativity than Pyc2, even in the absence of aspartate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Pyc1 and Pyc2 display different allosteric properties with respect to acetyl CoA activation and aspartate inhibition, with Pyc1 showing a higher degree of cooperativity than Pyc2, even in the absence of aspartate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
the enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, and other cellular processes
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate. In addition to de novo fatty acid synthesis, pyruvate carboxylase is also involved in glyceroneogenesis, a pathway for synthesizing glycerol required for fatty acid re-esterification. Physiological functions and regulation, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
Methanococcus sp.
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
additional information
?
-
-
enzyme deficiency is a rare autosomal recessive disease
-
-
?
additional information
?
-
-
in yeast, two metabolic pathways leading to the production of oxaloacetate are the pyruvate carboxylase-catalysed reaction and the glyoxylate cycle.When yeast is grown on acetate, pyruvate carboxylase-catalysed oxaloacetate formation is repressed but the glyoxylate cycle is active, and vice versa if grown on glucose minimal medium
-
-
?
additional information
?
-
-
starvation enhances pyruvate carboxylase activity, whereas diabetes also increases gluconeogenesis through enhanced uptake of substrate and increased flux through liver pyruvate carboxylase mice
-
-
?
additional information
?
-
-
protein, but not the enzyme is essential for import and assembly of alcohol oxidase into peroxisomes
-
?
additional information
?
-
-
the transcarboxylase domain of pyruvate carboxylase is essential for assembly of the peroxisomal flavoenzyme alcohol oxidase
-
-
?
additional information
?
-
-
in yeast, two metabolic pathways leading to the production of oxaloacetate are the pyruvate carboxylase-catalysed reaction and the glyoxylate cycle.When yeast is grown on acetate, pyruvate carboxylase-catalysed oxaloacetate formation is repressed but the glyoxylate cycle is active, and vice versa if grown on glucose minimal medium
-
-
?
additional information
?
-
-
protein, but not the enzyme is essential for import and assembly of alcohol oxidase into peroxisomes
-
?
additional information
?
-
-
the enzyme is regulated by a pyruvate carboxylase regulator, encoded by gene PA5437 or pycR, PycR inactivation results in 100 000fold attenuation of virulence in the rat lung in vivo, PycR is a regulator with pleiotropic effects on virulence factors, such as lipase and esterase expression and biofilm formation, which are important for maintenance of Pseudomonas aeruginosa in chronic lung infection, overview
-
-
?
additional information
?
-
beta-cells possess compensatory systems that are activated in response to suppression of pyruvate carboxylase nzyme levels. The compensatory events include allosteric activation of pyruvate carboxylase due to increased levels of acetyl-CoA and enhanced conversion of isocitrate to 2-oxoglutarate and downstream metabolites via the cytosolic, NADP-dependent isocitrate dehydrogenase
-
-
?
additional information
?
-
-
starvation enhances pyruvate carboxylase activity, whereas diabetes also increases gluconeogenesis through enhanced uptake of substrate and increased flux through liver pyruvate carboxylase rats
-
-
?
additional information
?
-
-
in yeast, two metabolic pathways leading to the production of oxaloacetate are the pyruvate carboxylase-catalysed reaction and the glyoxylate cycle.When yeast is grown on acetate, pyruvate carboxylase-catalysed oxaloacetate formation is repressed but the glyoxylate cycle is active, and vice versa if grown on glucose minimal medium
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate
-
allosteric activator of pyruvate carboxylase. The increase in activity between 2 mM and saturating MgATP is approximately 16fold
acetoacetyl-CoA
-
activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
butyryl-CoA
-
can replace acetyl-CoA with little efficiency
L-aspartate
-
allosteric activator
malonyl-CoA
-
activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
n-butanoyl-CoA
-
activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
n-propanoyl-CoA
-
activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
oleoyl-CoA
-
activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
oxamate
-
oxamate acts as a carboxyl acceptor, forming a carbamylated oxamate product and thereby accelerating the enzymatic decarboxylation reaction
palmitoyl-CoA
-
activated by long-chain acyl-CoA derivatives
TNFalpha
-
pyruvate decarboxylase activity decreases in TNFalpha-sensitive cells but increases in bcl-2 transfected cells
-
acetyl CoA
-
activates
acetyl CoA
-
enzyme activator, major effect is to promote the carboxylation of biotin, reduces the Kms for both MgATP2- and biotin, overview
acetyl-CoA
-
activates
acetyl-CoA
-
in absence of acetyl-CoA the maximal rate of oxaloacetate synthesis is 4% of that obtained in presence of saturating concentrations of acetyl-CoA
acetyl-CoA
-
activates in presence of either L-Asp or 2-oxoglutarate but does not activate in absence of these dicarboxylic acids. Trinitrobenzenesulfonate causes selective loss of the capacity for activation by acetyl-CoA
acetyl-CoA
-
best activator
acetyl-CoA
-
in absence of acetyl-CoA the maximal rate of oxaloacetate synthesis is 20% of that obtained in presence of saturating concentrations of acetyl-CoA
acetyl-CoA
-
allosteric activator
acetyl-CoA
-
activates phosphorylation of MgADP2- by carbamoyl phosphate
acetyl-CoA
-
inactive in absence of acetyl-CoA
acetyl-CoA
-
allosteric activator
acetyl-CoA
allosteric activator, 50% of maximal activity at 0.013 mM for the recombinant enzyme and at 0.015 mM for the liver enzyme
acetyl-CoA
-
activates the conversion of pyruvate to oxaloacetate
acetyl-CoA
-
activation by short-chain derivatives of CoA
acetyl-CoA
-
not required
acetyl-CoA
-
allosteric activator
acetyl-CoA
-
dependent, half maximal activation at 0.014 mM
acetyl-CoA
-
allosteric activator
acetyl-CoA
-
in absence of acetyl-CoA the maximal rate of oxaloacetate synthesis is 21% of that observed in the presence of saturating concentrations of the activator
acetyl-CoA
allosteric activator
acetyl-CoA
-
allosteric activator of pyruvate carboxylase, there is a 7fold increase in the turnover number for ATP cleavage induced by acetyl-CoA
acetyl-CoA
nonessential activator. Both acetyl-CoA and Mg2+ assist in coupling the MgATP-dependent carboxylation of biotin in the biotin carboxylase (BC) domain with pyruvate carboxylation in the carboxyl transferase (CT) domain. Absence of acetyl-CoA results in only 9% of fully activated enzyme. Acetyl-CoA also has a noticeable effect on the activity of the oxamate-induced decarboxylation of oxaloacetate but no effect on the rate of MgADP phosphorylation by carbamoyl phosphate
acetyl-CoA
acetyl-CoA acts to decrease the activation free energy of the reaction by both increasing the activation entropy and decreasing the activation enthalpy
acetyl-CoA
interacts directly with residues R469 and D471
acetyl-CoA
-
allosteric activator
acetyl-CoA
-
quite active in absence of acetyl-CoA
acetyl-CoA
-
activates Pyc1 at 0.25 mM
acetyl-CoA
-
activates, half-maximal activity at 0.23 mM
acetyl-CoA
the substrates of the biotin carboxylase and carboxyl transferase domain are energetically coupled in the presence of acetyl-CoA. Both kinetic and energetic coupling between the two domains is lost in the absence of acetyl-CoA
acetyl-CoA
-
best activator
acetyl-CoA
-
activation in decreasing order: acetyl-CoA, n-propanoyl-CoA, n-butanoyl-CoA, malonyl-CoA, CoA, acetoacetyl-CoA, oleoyl-CoA
acetyl-CoA
-
powerful activator
acetyl-CoA
-
highly dependent on
acetyl-CoA
-
allosteric activator. Concentrations eliciting maximal activity are 0.013 mM, 0.042 mM and 0.084 mM at assay temperatures of 45°C, 55°C, and 65°C respectively
acyl-CoA derivatives
-
activate
acyl-CoA derivatives
-
long chain acyl CoA is more effective than acetyl-CoA
acyl-CoA derivatives
-
activation in decreasing order: acetyl-CoA, n-propanyl-CoA, n-butanoyl-CoA, malonyl-CoA/ CoA, acetoacetyl-CoA, oleoyl-CoA
methanesulfonyl-CoA
-
activates
methanesulfonyl-CoA
-
inhibition
methanesulfonyl-CoA
-
inhibition
methanesulfonyl-CoA
-
activates
propionyl-CoA
-
can replace acetyl-CoA with little efficiency
propionyl-CoA
-
activates less efficiently than acetyl-CoA
additional information
-
starvation enhances pyruvate carboxylase activity. Short-term treatment with glucagon increases pyruvate carboxylase mRNA but does not result in an apparent change in protein levels or activity. Pyruvate carboxylase and PEP carboxykinase acts cooperatively
-
additional information
-
starvation enhances pyruvate carboxylase activity. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively
-
additional information
-
starvation enhances pyruvate carboxylase activity. Peroxisome-proliferator-activated receptor gamma increases enzyme expression in adipocytes. Rosiglitazone or other thiazolidinediones induce the enzyme expression. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively
-
additional information
-
activity strongly influenced by the carbon source used for growth
-
additional information
-
starvation enhances pyruvate carboxylase activity. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively
-
additional information
-
acetyl-CoA and K+ have no effect on ADP phosphorylation by carbamoyl phosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.7 - 12.3
Carbamoyl phosphate
4.1
oxamate
-
ATPase reaction, wild-type, pH 7.5, 25°C
additional information
additional information
-
0.0028
ADP
wild-type, MgADP phosphorylation, pH 7.8, 30°C
0.008
ADP
mutant H216N, MgADP phosphorylation, pH 7.8, 30°C
0.1 - 2
ADP
pH 7.5, 25°C, wild-type, reverse reaction
0.009
ATP
wild-type, MgATP cleavage, pH 7.8, 30°C
0.018
ATP
pH 7.5, 25°C, wild-type, 10 mM biotin, pyruvate carboxylation
0.022
ATP
pH 7.5, 25°C, wild-type, no biotin, pyruvate carboxylation
0.027
ATP
-
with 10 mM free Mg2+
0.04
ATP
pH 7.5, 25°C, mutant K119Q, 10 mM biotin, pyruvate carboxylation
0.05
ATP
-
pH 7.8, 30°C, C249A mutant
0.054
ATP
pH 7.5, 25°C, mutant T882A, no biotin, pyruvate carboxylation
0.056
ATP
-
pH 7.8, 30°C, wild-type Pyc1
0.07
ATP
-
pH 7.8, 30°C, wild-type Pyc1
0.08
ATP
-
pyruvate, second values 0.21 mM
0.082
ATP
mutant H216N, MgATP cleavage, pH 7.8, 30°C
0.09
ATP
pH 7.5, 25°C, mutant T882A, 10 mM biotin, pyruvate carboxylation
0.1 - 1
ATP
wild-type, pH 7.8, 30°C
0.145
ATP
pH 7.5, 25°C, wild-type, pyruvate carboxylation
0.16
ATP
mutant R427S, pH 7.8, 30°C
0.2
ATP
-
37°C and 45°C, pH 8, Mg2+ concentration higher than ATP concentration
0.22
ATP
37°C, pH 7.8, liver enzyme
0.25
ATP
37°C, pH 7.8, recombinant enzyme
0.29
ATP
mutant R427K, pH 7.8, 30°C
0.46 - 0.87
ATP
-
pH 8, 30°C
0.54 - 1.03
ATP
-
pH 8, 30°C, ATP-cleavage in absence of pyruvate
0.6
ATP
-
pH 7.8, 30°C, in presence of acetyl-CoA
0.7
ATP
mutant R472K, pH 7.8, 30°C
1
ATP
mutant R472S, pH 7.8, 30°C
1.2
ATP
pH 7.5, 25°C, mutant K119Q, no biotin, pyruvate carboxylation
1.26
ATP
-
37°C, pH 8, Mg2+ concentration equal to that of ATP
1.8
ATP
-
pH 7.8, 30°C, in absence of acetyl-CoA
9.2
ATP
-
45°C, pH 8, Mg2+ concentration equal to that of ATP
3.3
biotin
-
pH 7.8, 30°C, in presence of acetyl-CoA
18
biotin
-
pH 7.8, 30°C, in absence of acetyl-CoA
1.7
Carbamoyl phosphate
-
pH 7.8, 30°C, C249A mutant, with acetyl-CoA and K+
10.7
Carbamoyl phosphate
-
pH 7.8, 30°C, C249A mutant, without acetyl-CoA and K+
11.3
Carbamoyl phosphate
-
pH 7.8, 30°C, wild-type Pyc1, with acetyl-CoA and K+
12.3
Carbamoyl phosphate
-
pH 7.8, 30°C, wild-type Pyc1, without acetyl-CoA and K+
0.22
HCO3-
-
80°C, pH 8.5
0.66
HCO3-
Leptosphaeria michotii
-
-
1.36
HCO3-
-
pH 7.8, 30°C, wild-type Pyc1
1.75
HCO3-
37°C, pH 7.8, recombinant enzyme
2.3
HCO3-
-
pH 7.8, 30°C, C249A mutant
2.6
HCO3-
-
with 10 mM free Mg2+
3.2
HCO3-
37°C, pH 7.8, liver enzyme
3.4
HCO3-
-
with 2 mM free Mg2+
10.8
HCO3-
pH 7.5, 25°C, wild-type, pyruvate carboxylation
16
HCO3-
-
with saturating concentrations of the activator acetyl-CoA
62.2
HCO3-
-
pH 8, 30°C, ATP-cleavage in absence of pyruvate
400
HCO3-
-
without acetyl-CoA
0.039
pyruvate
-
-
0.08
pyruvate
-
wild-type enzyme after retroviral expression
0.12
pyruvate
-
A610T mutant after retroviral expression
0.15
pyruvate
5 mM Mg2+, pH 7.5, 25°C, wild-type, pyruvate carboxylation, Vmax: 3.98 micromol/mg/min
0.15
pyruvate
pH 7.5, 25°C, wild-type, pyruvate carboxylation
0.2
pyruvate
Leptosphaeria michotii
-
-
0.21
pyruvate
-
second value 0.08
0.22
pyruvate
37°C, pH 7.8, liver enzyme
0.23
pyruvate
37°C, pH 7.8, recombinant enzyme
0.25
pyruvate
-
MgATP2-, with 2 mM free Mg2+
0.3
pyruvate
-
37°C, pH 8
0.31
pyruvate
-
pH 8, 30°C
0.45
pyruvate
-
45°C, pH 8
0.45
pyruvate
-
pH 7.8, 30°C, C249A mutant
0.495
pyruvate
-
pH 7.8, 30°C, wild-type Pyc1
0.5
pyruvate
30°C, pH 7.8
0.5
pyruvate
-
pH 7.8, 30°C, wild-type Pyc1
0.53
pyruvate
-
80°C, pH 8.5
0.58
pyruvate
wild-type, pH 7.5, presence of acetyl-CoA
1
pyruvate
-
ATPase reaction, wild-type, pH 7.5, 25°C
1.8
pyruvate
mutant Q870A, pH 7.5
2.3
pyruvate
mutant S911A, pH 7.5
2.65
pyruvate
3 mM Mg2+, pH 7.5, 25°C, wild-type, pyruvate carboxylation, Vmax: 3.18 micromol/mg/min
3
pyruvate
1.5 mM Mg2+, pH 7.5, 25°C, wild-type, pyruvate carboxylation, Vmax: 1.41 micromol/mg/min
3.1
pyruvate
0.7 mM Mg2+, pH 7.5, 25°C, wild-type, pyruvate carboxylation, Vmax: 0.69 micromol/mg/min
4.4
pyruvate
wild-type, pH 7.5
additional information
additional information
-
stopped flow kinetics using fluorescent ATP analogue formycin A-5'-triphosphate, presence of biotin enhanced binding, kinetics of free biotin carboxylation
-
additional information
additional information
0.5 mM Mg2+: Vmax (micromol/mg/min) 1.16, Ka (acetyl-CoA) 0.038 mM/1 mM Mg2+: Vmax (micromol/mg/min) 1.39, Ka (acetyl-CoA) 0.026 mM/1.5 mM Mg2+: Vmax (micromol/mg/min) 2.59, Ka (acetyl-CoA) 0.025 mM/3 mM Mg2+: Vmax (micromol/mg/min) 5.7, Ka (acetyl-CoA) 0.01 mM
-
additional information
additional information
-
0.5 mM Mg2+: Vmax (micromol/mg/min) 1.16, Ka (acetyl-CoA) 0.038 mM/1 mM Mg2+: Vmax (micromol/mg/min) 1.39, Ka (acetyl-CoA) 0.026 mM/1.5 mM Mg2+: Vmax (micromol/mg/min) 2.59, Ka (acetyl-CoA) 0.025 mM/3 mM Mg2+: Vmax (micromol/mg/min) 5.7, Ka (acetyl-CoA) 0.01 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.013
ADP
pH 7.5, 25°C, wild-type, reverse reaction
0.043 - 0.13
Carbamoyl phosphate
0.056 - 0.28
oxaloacetate
0.0013
ATP
pH 7.5, 25°C, mutant K119Q, no biotin, pyruvate carboxylation
0.0018
ATP
-
pH 7.8, 30°C, absence of acetyl CoA, 0.24 mM Mg2+
0.0029
ATP
-
pH 7.8, 30°C, absence of acetyl CoA, 10 mM Mg2+
0.0049
ATP
-
pH 7.8, 30°C, absence of acetyl CoA, 1 mM Mg2+
0.014
ATP
-
pH 7.8, 30°C, ATP cleavage in absence of acetyl-CoA
0.037
ATP
-
pH 7.8, 30°C, ATP cleavage in presence of acetyl-CoA
0.04
ATP
pH 7.5, 25°C, mutant K119Q, 10 mM biotin, pyruvate carboxylation
0.043
ATP
pH 7.5, 25°C, wild-type, no biotin, pyruvate carboxylation
0.05
ATP
pH 7.5, 25°C, wild-type, 10 mM biotin, pyruvate carboxylation
0.054
ATP
-
pH 7.8, 30°C, presence of acetyl CoA, 1 mM Mg2+
0.23
ATP
pH 7.5, 25°C, mutant T882A, no biotin, pyruvate carboxylation
0.28
ATP
-
pH 7.8, 30°C, presence of acetyl CoA, 0.24 mM Mg2+
0.6
ATP
pH 7.5, 25°C, mutant T882A, 10 mM biotin, pyruvate carboxylation
1.9
ATP
mutant R472K, pH 7.8, 30°C
2
ATP
mutant R472S, pH 7.8, 30°C
3.4
ATP
mutant R427K, pH 7.8, 30°C
4.2
ATP
mutant R427S, pH 7.8, 30°C
6.6
ATP
pH 7.5, 25°C, wild-type, pyruvate carboxylation
10.9
ATP
wild-type, pH 7.8, 30°C
0.043
Carbamoyl phosphate
-
pH 7.8, 30°C, C249A mutant, with acetyl-CoA and K+
0.11
Carbamoyl phosphate
-
pH 7.8, 30°C, wild-type Pyc1, with acetyl-CoA and K+
0.11
Carbamoyl phosphate
-
pH 7.8, 30°C, wild-type Pyc1, without acetyl-CoA and K+
0.13
Carbamoyl phosphate
-
pH 7.8, 30°C, C249A mutant, without acetyl-CoA and K+
11.6
HCO3-
pH 7.5, 25°C, wild-type, pyruvate carboxylation
0.056
oxaloacetate
-
pH 7.5, 25°C, 0.25 mM oxamate
0.076
oxaloacetate
-
pH 7.5, 25°C, 0.5 mM oxamate
0.1
oxaloacetate
co-substrate: ADP + phosphate, mutant H216N, oxaloacetate decarboxylation, pH 7.8, 30°C
0.151
oxaloacetate
-
pH 7.5, 25°C, 0.75 mM oxamate
0.2
oxaloacetate
-
pH 7.5, 25°C, 1 mM oxamate
0.28
oxaloacetate
co-substrate: ADP + phosphate, wild-type, oxaloacetate decarboxylation, pH 7.8, 30°C
0.052
pyruvate
co-substrate: HCO3-, mutant H216N, pyruvate carboxylation, pH 7.8, 30°C
0.105
pyruvate
mutant D471A, pH 7.8, 30°C, presence of acetyl-CoA
0.11
pyruvate
mutant D471A, pH 7.8, 30°C
0.18
pyruvate
wild-type, pH 7.8, 30°C, Hill coefficient 2.7
0.26
pyruvate
wild-type, pH 7.8, 30°C
0.28
pyruvate
-
mutant enzyme R548K, in 100 mM Tris-HCl pH 7.8, 30°C
0.37
pyruvate
mutant D420A, pH 7.8, 30°C
0.51
pyruvate
mutant R424S, pH 7.8, 30°C
0.68
pyruvate
mutant R469K, pH 7.8, 30°C, Hill coefficient 0.9
0.72
pyruvate
mutant R429S, pH 7.8, 30°C
0.84
pyruvate
mutant R429K, pH 7.8, 30°C
1.18
pyruvate
mutant E1027R, pH 7.8, 30°C, Hill coefficient 2.3
1.2
pyruvate
mutant Q870A, pH 7.5
1.61
pyruvate
mutant R469S, pH 7.8, 30°C, Hill coefficient 2.3
2.17
pyruvate
mutant D1018A, pH 7.8, 30°C, Hill coefficient 2.1
2.5
pyruvate
mutant S911A, pH 7.5
2.71
pyruvate
mutant E1027R, pH 7.8, 30°C, Hill coefficient 2.3, presence of acetyl-CoA
3.94
pyruvate
mutant E1027A, pH 7.8, 30°C, Hill coefficient 3.0
5.67
pyruvate
mutant R429K, pH 7.8, 30°C, presence of acetyl-CoA
5.73
pyruvate
mutant D420A, pH 7.8, 30°C, presence of acetyl-CoA
6.05
pyruvate
mutant R469K, pH 7.8, 30°C, Hill coefficient 0.9, presence of acetyl-CoA
6.19
pyruvate
mutant R429S, pH 7.8, 30°C, presence of acetyl-CoA
6.5
pyruvate
wild-type, pH 7.5
7.33
pyruvate
pH 7.5, 25°C, wild-type, pyruvate carboxylation
9.8
pyruvate
mutant R424S, pH 7.8, 30°C, presence of acetyl-CoA
11
pyruvate
co-substrate: HCO3-, wild-type, pyruvate carboxylation, pH 7.8, 30°C
11.3
pyruvate
mutant R469S, pH 7.8, 30°C, Hill coefficient 2.3, presence of acetyl-CoA
12.3
pyruvate
mutant D1018A, pH 7.8, 30°C, Hill coefficient 2.1, presence of acetyl-CoA
13.3
pyruvate
wild-type, pH 7.8, 30°C, presence of acetyl-CoA
13.9
pyruvate
-
wild type enzyme, in 100 mM Tris-HCl pH 7.8, 30°C
14.9
pyruvate
mutant E1027A, pH 7.8, 30°C, Hill coefficient 3.0, presence of acetyl-CoA
15.7
pyruvate
wild-type, pH 7.5, presence of acetyl-CoA
17.6
pyruvate
wild-type, pH 7.8, 30°C, Hill coefficient 2.7, presence of acetyl-CoA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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110000
-
4 * 110000, SDS-PAGE
12000
-
4 * 12000, SDS-PAGE
124700
-
4 * 124700, SDS-PAGE
126000
-
4 * 126000, calculation from nucleotide sequence, SDS-PAGE
127370
-
x * 127370, calculation from nucleotide sequence
128200
-
chain PC-(CT+BCCP), gel filtration, dimeric form
129300
calculated from amino acid sequence
13100
-
x * 13100, calculation from nucleotide sequence
133000
-
x * 133000, SDS-PAGE
136750
-
x * 136750, SDS-PAGE
340000
analytical ultracentrifugation
420000 - 440000
Leptosphaeria michotii
-
gel filtration, native PAGE
472000
-
analytical ultracentrifugation
475000
-
meniscus depletion sedimentation equilibrium method
480000
-
gel filtration, Stokes' radius
501300
-
intact enzyme, gel filtration, tetrameric form
51400
-
chain PC-(BC), SDS-PAGE, monomeric form
60000
Leptosphaeria michotii
-
4 * 60000, biotin containing alpha-subunit, + 4 * 50000, biotin-free beta-subunit
66200
-
chain PC-(CT+BCCP), gel filtration, monomeric form
81900
-
chain PC-(BC), gel filtration, dimeric form
additional information
-
at high enzyme concentration the enzyme aggregates to form high molecular weight aggregates
120000
SDS-PAGE
120000
-
x * 120000, SDS-PAGE
120000
-
4 * 120000, SDS-PAGE
125000
-
4 * 125000, SDS-PAGE
125000
-
4 * 125000, SDS-PAGE
125000
-
x * 125000, SDS-PAGE
128000
-
intact enzyme, SDS-PAGE, monomeric form
128000
-
4 * 128000, SDS-PAGE
130000
-
4 * 130000, SDS-PAGE
130000
-
4 * 130000, SDS-PAGE
130000
-
4 * 130000, SDS-PAGE
130000
-
4 * 130000, SDS-PAGE
130000
-
x * 130000, SDS-PAGE
50000
Leptosphaeria michotii
-
4 * 60000, biotin containing alpha-subunit, + 4 * 50000, biotin-free beta-subunit
50000
-
1 * 50000 + 1 * 70000
500000
-
-
500000
-
approach to equilibrium ultracentrifugation
500000
-
approach to equilibrium ultracentrifugation
500000
-
approach to equilibrium ultracentrifugation
54000
-
2 * 65000 + 2 * 54000, SDS-PAGE
54000
-
x * 65000, alpha, + x * 54000, beta, SDS-PAGE. The alpha-polypeptides are on the outside of the molecule and the beta-polypeptides are the internal subunits
55000
-
alpha4,beta4, 4 * 55000 + 4 * 65000, the 65000 Da subunit is biotinylated, the 55000 Da subunit is not, SDS-PAGE
55000
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
55000
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
55000
Methanococcus sp.
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
55000
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
55000
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
65000
-
chain PC-(CT+BCCP), SDS-PAGE, monomeric form
65000
-
2 * 65000 + 2 * 54000, SDS-PAGE
65000
-
x * 65000, alpha, + x * 54000, beta, SDS-PAGE. The alpha-polypeptides are on the outside of the molecule and the beta-polypeptides are the internal subunits
65000
-
alpha4,beta4, 4 * 55000 + 4 * 65000, the 65000 Da subunit is biotinylated, the 55000 Da subunit is not, SDS-PAGE
70000
-
1 * 50000 + 1 * 70000
70000
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
70000
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
70000
Methanococcus sp.
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
70000
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
70000
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
multimer
-
x * 120000, SDS-PAGE
oligomer
-
two pyruvate carboxylase subunits PycA and PycB
polymer
-
about 4% of the total enzyme elutes as a high molecular weight species, gel filtration
?
-
x * 133000, SDS-PAGE
?
-
x * 127370, calculation from nucleotide sequence
?
-
x * 65000, alpha, + x * 54000, beta, SDS-PAGE. The alpha-polypeptides are on the outside of the molecule and the beta-polypeptides are the internal subunits
?
-
x * 125000-130000, SDS-PAGE with dithiothreitol
?
-
x * 13100, calculation from nucleotide sequence
dimer
-
1 * 50000 + 1 * 70000
dimer
-
about 12% of the total enzyme, gel filtration
dimer
-
PC-(BC) exists as a monomer and as a dimer, (CT+BCCP) exists mostly as a dimer, gel filtration
homotetramer
-
-
homotetramer
-
analytical ultracentrifugation
monomer
-
about 10% of the total enzyme, gel filtration
monomer
-
PC-(BC) exists as a monomer and as a dimer, gel filtration
octamer
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
octamer
Leptosphaeria michotii
-
4 * 60000, biotin containing alpha-subunit, + 4 * 50000, biotin-free beta-subunit
octamer
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
octamer
-
alpha4,beta4, 4 * 55000 + 4 * 65000, the 65000 Da subunit is biotinylated, the 55000 Da subunit is not, SDS-PAGE
octamer
Methanococcus sp.
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
octamer
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
octamer
-
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit
tetramer
-
4 * 128000, SDS-PAGE
tetramer
-
4 * 130000, SDS-PAGE
tetramer
-
4 * 140000-155000, SDS-PAGE after denaturation by carboxylation in 7.5 M urea or in 6 M guanidine HCl, or succinylation in 7.5 M urea
tetramer
-
4 * 12000, SDS-PAGE
tetramer
-
4 * 120000-130000, alpha4
tetramer
-
4 * 125000, SDS-PAGE
tetramer
-
about 73% of the total enzyme, gel filtration
tetramer
-
4 * 128500-137000, SDS-PAGE, gel filtration, intact enzyme
tetramer
-
4 * 120000-130000, alpha4
tetramer
-
4 * 130000, SDS-PAGE
tetramer
-
4 * 120000-130000, alpha4
tetramer
tetrameric organization of wild-type and isolated C-terminal region, the PC tetramerization, PT, domain is important for oligomerization, conserved mode of tetramerization, overview
tetramer
-
4 * 120000-130000, alpha4
tetramer
-
four identical subunits
tetramer
-
4 * 110000, SDS-PAGE
tetramer
-
4 * 120000-130000, alpha4
tetramer
-
4 * 120000-130000, alpha4
tetramer
-
2 * 65000 + 2 * 54000, SDS-PAGE
tetramer
-
4 * 130000, SDS-PAGE
tetramer
-
4 * 124700, SDS-PAGE
tetramer
-
4 * 120000-130000, alpha4
tetramer
-
4 * 126000, calculation from nucleotide sequence, SDS-PAGE
tetramer
-
4 * 120000-130000, alpha4
tetramer
-
4 * 125000, SDS-PAGE
tetramer
Glu40 and Glu433 play essential roles in subunit interactions
tetramer
-
4 * 120000-130000, alpha4
tetramer
-
4 * 120000, SDS-PAGE
tetramer
-
4 * 120000, SDS-PAGE
-
tetramer
-
4 * 120000-130000, alpha4
tetramer
tetrameric organization of wild-type and isolated C-terminal region, the PC tetramerization, PT, domain is important for oligomerization, conserved mode of tetramerization
tetramer
-
4 * 130000, SDS-PAGE
additional information
-
structure analysis, the enzyme shows the alpha4beta4 form, each subunit is made up of two polypeptide chains, the 55 kDa non-biotinylated subunit alpha, which possesses the biotin carboxylase activity, and the 70 kDa beta subunit, which carries the biotin and also contains the carboxytransferase activity, overview. Dimerization interface structure, overview
additional information
-
all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
additional information
-
all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
additional information
-
all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
additional information
localization of a BCCP domain is located in the active site of the carboxytransferase domain that participates in the carboxyltransfer reaction
additional information
-
localization of a BCCP domain is located in the active site of the carboxytransferase domain that participates in the carboxyltransfer reaction
additional information
-
all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
additional information
-
structure analysis, the enzyme shows the alpha4beta4 form, each subunit is made up of two polypeptide chains, the 55 kDa non-biotinylated subunit alpha, which possesses the biotin carboxylase activity, and the 70 kDa beta subunit, which carries the biotin and also contains the carboxytransferase activity, overview
additional information
Methanococcus sp.
-
structure analysis, the enzyme shows the alpha4beta4 form, each subunit is made up of two polypeptide chains, the 55 kDa non-biotinylated subunit alpha, which possesses the biotin carboxylase activity, and the 70 kDa beta subunit, which carries the biotin and also contains the carboxytransferase activity, overview
additional information
-
structure analysis, the enzyme shows the alpha4beta4 form, each subunit is made up of two polypeptide chains, the 55 kDa non-biotinylated subunit alpha, which possesses the biotin carboxylase activity, and the 70 kDa beta subunit, which carries the biotin and also contains the carboxytransferase activity, overview
additional information
-
each protomer consists of two polypeptide chains, with alpha and beta subunits arranged in an (alphabeta)4 structure
additional information
-
all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
additional information
-
all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
additional information
-
structure analysis, the enzyme shows the alpha4beta4 form, each subunit is made up of two polypeptide chains, the 55 kDa non-biotinylated subunit alpha, which possesses the biotin carboxylase activity, and the 70 kDa beta subunit, which carries the biotin and also contains the carboxytransferase activity, overview
additional information
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all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
additional information
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the enzyme exists predominantly as a tetramer in solution and, while it can equilibrate between the tetramer, dimer and monomer, only the tetrameric form of the enzyme catalyses the overall reaction, subunit arrangement. All three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview. Quarternary structure, overview
additional information
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all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
additional information
localization of a BCCP domain is located in the active site of the carboxytransferase domain that participates in the carboxyltransfer reaction
additional information
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localization of a BCCP domain is located in the active site of the carboxytransferase domain that participates in the carboxyltransfer reaction
additional information
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the enzyme exists predominantly as a tetramer in solution and, while it can equilibrate between the tetramer, dimer and monomer, only the tetrameric form of the enzyme catalyses the overall reaction, subunit arrangement. All three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
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D543E
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mutant with decreased activity
D649N
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mutant with decreased activity
D713E
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mutant with decreased activity
D713N
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mutant with decreased activity
D762E
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mutant with decreased activity
D762N
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mutant with decreased activity
E576D
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mutant with decreased activity
E576Q
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mutant with decreased activity
E592Q
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mutant with decreased activity
K1112A
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site-directed mutagenesis, the mutant lacks the biotin binding site and boud biotin, it does not catalyse the complete reaction, but catalyses ATP-cleavage and the carboxylation of free biotin. Oxaloacetate decarboxylation is not catalysed, even in the presence of free biotin, suggesting that only the biotin carboxylation domain of the enzyme is accessible to free biotin. The mutant K1112A also catalyses the phosphorylation of ADP from carbamoyl phosphate
K712Q
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mutant with decreased activity
K712R
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mutant with decreased activity
F1077A
mutant cyrstal structure, overview
M743I
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naturally occurring mutation involved in pyruvate carboxylase deficiency type A
R451C
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naturally occurring mutation involved in pyruvate carboxylase deficiency type A, the mutant enzyme shows markedly decreased acetyl-CoA-dependent activation
V145A
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naturally occurring mutation involved in pyruvate carboxylase deficiency type A
G746A
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mutation to corresponding Entercoccus faecalis residue. Mutant shows similar activity as wild-type, mutation reduces inhibition by cyclic di-3',5'-adenosine monophosphate to 40%, compared to 60% for wild-type
Y715T
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mutation to correspoinding human residue. Mutant shows similar activity as wild-type, mutation abolishes inhibition by cyclic di-3',5'-adenosine monophosphate
A465R
mutation in the alpha subunit, abolishes the formation of the holoenzyme, catalytically inactive
D502A/E507A
mutation in the alpha subunit, mutant forms a stable holoenzyme, about 40% of wild-type activity
H476A/E478A
mutation in the alpha subunit, mutant forms a stable holoenzyme and is fully active
H476A/E478A/D502A/E507A
mutation in the alpha subunit, abolishes the formation of the holoenzyme, catalytically inactive
K419A/E421A/E422A
mutations bin the beta subunit designed to reduce the surface entropy. The mutations have no effect on the catalytic activity of the enzyme
Q452stop
mutation in the alpha subunit, abolishes the formation of the holoenzyme
R401E
mutation in the alpha subunit, mutant forms a stable holoenzyme, about 50% of wild-type activity
A465R
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mutation in the alpha subunit, abolishes the formation of the holoenzyme, catalytically inactive
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H476A/E478A
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mutation in the alpha subunit, mutant forms a stable holoenzyme and is fully active
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K419A/E421A/E422A
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mutations bin the beta subunit designed to reduce the surface entropy. The mutations have no effect on the catalytic activity of the enzyme
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Q452stop
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mutation in the alpha subunit, abolishes the formation of the holoenzyme
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R401E
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mutation in the alpha subunit, mutant forms a stable holoenzyme, about 50% of wild-type activity
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Y542V/A557Q/S762D
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the triple mutation fully inactivates the moonlighting function of Pyc1, but not the enzyme activity of pyruvate carboxylase
A55T
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mutation in the beta subunit, reduces activity by 50fold and interferes with biotin binding to the active site,mutant exhibits growth on pyruvate similar to the wild type
K451stop
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mutation in alpha subunit, disrupts holoenzyme formation
K572A
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mutation in the beta subunit, abolishes biotinylation and leads to growth defects in pyruvate that are similar to that of a gene deletion mutant
D1018A
mutant has increased activity in the absence of acetyl-CoA, but not in its presence
D420A
mutation affects acetyl-CoA binding, enhances the activity of the enzyme in the absence of acetyl-CoA
D471A
mutant exhibits no acetyl CoA-activation
E1027A
mutant has increased activity in the absence of acetyl-CoA, but not in its presence
E1027R
mutant has increased activity in the absence of acetyl-CoA, but not in its presence
H216N
no differences to quarterny structures compared to wild-type. Mutation results in a 9fold increase in the Km for MgATP in its steady-state cleavage in the absence of pyruvate and a 3fold increase in the Km for MgADP in its steady-state phosphorylation by carbamoyl phosphate. kcat/Km (MgATP)98% decreased compared to wild-type. For MgADP phosphorylation kcat/Km is 99.5% decreased compared to wild-type. The Kd of the enzyme MgATP complex is essentially the same in the wildtype enzyme and H216N but the first-order rate constant for MgATP cleavage in the single-turnover experiments in H216N is only 0.75% of that for the wild-type enzyme, and thus, the MgATP cleavage step is rate-limiting in the steady state for H216N but not for the wild-type enzyme
K1119Q
mutant that lacks tethered biotin. Addition of 10 mM biotin increases the kcat of MgATP hydrolysis to rates observed for wild-type RePC in the absence of free biotin. This rate increase, coupled with a 35fold decrease in the Km for MgATP, results in a nearly 1000fold increase in the catalytic efficiency of the mutant K1119Q RePC catalyzed reaction when 10 mM free biotin is added
K119Q
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no catalytic acitivy for pyruvate decarboxylation, or oxaloacetate decarboxylation
K718Q
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2.9% of wild-type activity for pyruvate carboxylation, 14% for full reverse reaction, 7.2% for oxaloacetate decarboxylation in presence of oxamate
Q552A
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the mutation results in loss of the ability to catalyse pyruvate carboxylation, biotin-dependent decarboxylation of oxaloacetate and proton exchange between pyruvate and water
Q552N
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the mutation results in loss of the ability to catalyse pyruvate carboxylation, biotin-dependent decarboxylation of oxaloacetate and proton exchange between pyruvate and water
Q844L/S885A
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13% of wild-type activity for pyruvate carboxylation, 53% for full reverse reaction, 4.7% for oxaloacetate decarboxylation in presence of oxamate
R424
mutation affects acetyl-CoA binding, enhances the activity of the enzyme in the absence of acetyl-CoA. Mutation decreases the activation enthalpy of the pyruvate carboxylation reaction by an amount consistent with removal of a single hydrogen bond
R427K
more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 76fold higher compared to wild-type, kcat 32% of wild-type enzyme, Km (MgATP) 2.6fold higher compared to wild-type, kcat/Km value 12% of wild-type. Ka (activation value) for Mg2+ is 8fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.4% of wild-type in the presence of acetyl-CoA/0.8% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 21% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 6% biotin carboxylation rate of wild-type. residual activity at saturating concentrations of L-aspartate is 2fold greater than wild-type
R427S
more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 15fold higher compared to wild-type, kcat 41% of wild-type enzyme, Km (MgATP) 1.5fold higher compared to wild-type, kcat/Km value 26% of wild-type. Ka (activation value) for Mg2+ is 2fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 1.1% of wild-type in the presence of acetyl-CoA/5.8% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 17% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity similar to wild-type. Mutant exhibits 6% biotin carboxylation rate of wild-type
R429K
enhances the activity of the enzyme in the absence of acetyl-CoA
R429S
residue Arg429 is especially important for acetyl CoA binding. Mutation results in a 100fold increase in the Ka of acetyl-CoA activation and a large decrease in the cooperativity of this activation
R469K
mutant shows increased enzymic activity in the presence and absence of acetyl-CoA
R469S
mutant shows increased enzymic activity in the presence and absence of acetyl-CoA
R472K
45% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 252fold higher compared to wild-type, kcat 32% of wild-type enzyme, Km (MgATP) 6.7fold higher compared to wild-type, kcat/Km value 3% of wild-type. Ka (activation value) for Mg2+ is 37fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.6% of wild-tpye in the presence of acetyl-CoA/0.9% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 8% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 3% biotin carboxylation rate of wild-type
R548A
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the mutation results in loss of the ability to catalyse pyruvate carboxylation, biotin-dependent decarboxylation of oxaloacetate and proton exchange between pyruvate and water
R548K
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the mutation results in loss of the ability to catalyse pyruvate carboxylation (2% residual activity), biotin-dependent decarboxylation of oxaloacetate and proton exchange between pyruvate and water
T882C
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7.1% of wild-type activity for pyruvate carboxylation, 20% for full reverse reaction, 11% for oxaloacetate decarboxylation in presence of oxamate
T882S
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21% of wild-type activity for pyruvate carboxylation, 51% for full reverse reaction, 30% for oxaloacetate decarboxylation in presence of oxamate
D420A
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mutation affects acetyl-CoA binding, enhances the activity of the enzyme in the absence of acetyl-CoA
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D471A
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mutant exhibits no acetyl CoA-activation
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E1027A
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mutant has increased activity in the absence of acetyl-CoA, but not in its presence
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E1027R
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mutant has increased activity in the absence of acetyl-CoA, but not in its presence
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R424
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mutation affects acetyl-CoA binding, enhances the activity of the enzyme in the absence of acetyl-CoA. Mutation decreases the activation enthalpy of the pyruvate carboxylation reaction by an amount consistent with removal of a single hydrogen bond
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R429K
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enhances the activity of the enzyme in the absence of acetyl-CoA
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R429S
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residue Arg429 is especially important for acetyl CoA binding. Mutation results in a 100fold increase in the Ka of acetyl-CoA activation and a large decrease in the cooperativity of this activation
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R469K
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mutant shows increased enzymic activity in the presence and absence of acetyl-CoA
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R469S
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mutant shows increased enzymic activity in the presence and absence of acetyl-CoA
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H216N
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no differences to quarterny structures compared to wild-type. Mutation results in a 9fold increase in the Km for MgATP in its steady-state cleavage in the absence of pyruvate and a 3fold increase in the Km for MgADP in its steady-state phosphorylation by carbamoyl phosphate. kcat/Km (MgATP)98% decreased compared to wild-type. For MgADP phosphorylation kcat/Km is 99.5% decreased compared to wild-type. The Kd of the enzyme MgATP complex is essentially the same in the wildtype enzyme and H216N but the first-order rate constant for MgATP cleavage in the single-turnover experiments in H216N is only 0.75% of that for the wild-type enzyme, and thus, the MgATP cleavage step is rate-limiting in the steady state for H216N but not for the wild-type enzyme
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K1119Q
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mutant that lacks tethered biotin. Addition of 10 mM biotin increases the kcat of MgATP hydrolysis to rates observed for wild-type RePC in the absence of free biotin. This rate increase, coupled with a 35fold decrease in the Km for MgATP, results in a nearly 1000fold increase in the catalytic efficiency of the mutant K1119Q RePC catalyzed reaction when 10 mM free biotin is added
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R427K
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more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 76fold higher compared to wild-type, kcat 32% of wild-type enzyme, Km (MgATP) 2.6fold higher compared to wild-type, kcat/Km value 12% of wild-type. Ka (activation value) for Mg2+ is 8fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.4% of wild-type in the presence of acetyl-CoA/0.8% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 21% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 6% biotin carboxylation rate of wild-type. residual activity at saturating concentrations of L-aspartate is 2fold greater than wild-type
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R427S
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more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 15fold higher compared to wild-type, kcat 41% of wild-type enzyme, Km (MgATP) 1.5fold higher compared to wild-type, kcat/Km value 26% of wild-type. Ka (activation value) for Mg2+ is 2fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 1.1% of wild-type in the presence of acetyl-CoA/5.8% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 17% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity similar to wild-type. Mutant exhibits 6% biotin carboxylation rate of wild-type
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R472K
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45% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 252fold higher compared to wild-type, kcat 32% of wild-type enzyme, Km (MgATP) 6.7fold higher compared to wild-type, kcat/Km value 3% of wild-type. Ka (activation value) for Mg2+ is 37fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.6% of wild-tpye in the presence of acetyl-CoA/0.9% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 8% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 3% biotin carboxylation rate of wild-type
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R472S
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more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 203fold higher compared to wild-type, kcat 25% of wild-type enzyme, Km (MgATP) 8.7fold higher compared to wild-type, kcat/Km value 2% of wild-type. Ka (activation value) for Mg2+ is 30fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.6% of wild-type in the presence of acetyl-CoA/1.2% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 5% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 2% biotin carboxylation rate of wild-type
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T882A
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T882 mutant is a tetrameric holoenzyme where positioning of the tethered biotin favors placement in the BC domain. Free biotin increases the kcat for both the wild-type and the T882A mutant RePC-catalyzed reactions without having a major effect on the Km for MgATP. Crystal structures of mutant T882A pyruvate carboxylase are determined cocrystallized with phosphonoacetate and MgADP
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C249A
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only small effects on enzyme activity
E40R
predominant form of mutant E40R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
E433R
predominant form of mutant E433R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
R36E
the R36E is much more susceptible to tetramer dissociation and inactivation than the wild type enzyme. Coexpression of mutant forms with wild type Pyc1 shows that the R36E mutation had no effect on the interaction of these subunits with those of wild type Pyc1
R36E/E433R
predominant form of mutant R36E/E433R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
A610T
more than 30fold loss in catalytic efficiency
K912T
more than 30fold loss in catalytic efficiency
Q870A
2fold loss in catalytic efficiency
R644A
more than 30fold loss in catalytic efficiency
R644K
more than 30fold loss in catalytic efficiency
S911A
1.5fold loss in catalytic efficiency
T908A
more than 30fold loss in catalytic efficiency
Y651A
more than 30fold loss in catalytic efficiency
A610T
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reduced enzyme activity, no import of the enzyme into mitochondria
A610T
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naturally occurring mutation involved in pyruvate carboxylase deficiency type A, the mutant's catalytic activity and steady-state level are markedly decreased
R472S
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the mutation severely decreases the affinity of the enzyme for acetyl-CoA
R472S
more than 70% of mutant exist in the tetrameric form, Ka (activation value) for acetyl-CoA is 203fold higher compared to wild-type, kcat 25% of wild-type enzyme, Km (MgATP) 8.7fold higher compared to wild-type, kcat/Km value 2% of wild-type. Ka (activation value) for Mg2+ is 30fold higher compared to wild-type. Bicarbonate-dependent ATP cleavage activity: 0.6% of wild-type in the presence of acetyl-CoA/1.2% of wild-type in the absence of acetyl-CoA. ADP phosphorylation by carbamoyl phosphate: 5% of wild-type in the presence of acetyl-CoA. In the absence of acetyl-CoA activity slightly increased compared to wild-type. Mutant exhibits 2% biotin carboxylation rate of wild-type
T882A
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no catalytic activity for reactions involving the carboxyl transferase domain. 7- and 3.5fold increases in activity, as compared to that of the wild-type enzyme, for the ADP phosphorylation and bicarbonate-dependent ATPase reactions, respectively. Partial inhibition of the T882A-catalyzed biotin carboxylase domain reactions by oxamate and pyruvate
T882A
T882 mutant is a tetrameric holoenzyme where positioning of the tethered biotin favors placement in the BC domain. Free biotin increases the kcat for both the wild-type and the T882A mutant RePC-catalyzed reactions without having a major effect on the Km for MgATP. Crystal structures of mutant T882A pyruvate carboxylase are determined cocrystallized with phosphonoacetate and MgADP
additional information
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a chimeric enzyme mutant, comprising the biotin carboxylase domain of the enzyme from Aquifex aeolicus and the transcarboxylation and BCCP domain from Bacillus thermodenitrificans, shows an activity that is independent of acetyl-CoA, a characteristic of the Aquifex aeolicus enzyme and not the Bacillus thermodentrificans enzyme
additional information
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polypeptide chain is divided into two chains, between the biotin carboxylase and carboxyltransferase domains, resulting in two proteins PC-(BC) and PC-(CT+BCCP) with retained enzyme activity
additional information
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construction of an enzyme mutant form, in which the lysine residue to which the biotin is normally covalently bound is mutated to an alanine residue, this results in the production of an unbiotinylated apo-enzyme, which can, however, carboxylate free biotin in a reaction that proceeds 8fold faster in the presence of acetyl-CoA than in its absence. A chimeric enzyme mutant, comprising the biotin carboxylase domain of the nezyme from Aquifex aeolicus and the transcarboxylation and BCCP domain from Bacillus thermodenitrificans, shows an activity that is independent of acetyl-CoA, a characteristic of the Aquifex aeolicus enzyme and not the Bacillus thermodentrificans enzyme
additional information
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molecular basis of pyruvate carboxylase deficiency, mosaicism correlates with prolonged survival, three clinical phenotypes: type A is an infantile form, type B is a neonatal form, and type Casa benign form. Analysis of combinations of missense mutations, deletions, a splice site substitution and a nonsense mutation, overview
additional information
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three forms of PC deficiency are classified. Type A or the North American phenotype is caused by several point mutations and characterized by a mild lactic acidaemia but a normal ratio of plasma lactate to pyruvate, psychomotor retardation and in some, but not all cases, death in the first years of life. type B phenotype, a complex genotype in which two deletion mutations in both PC alleles was identified, i.e. one allele possesses two nucleotide deletions in exon 16, creating a frameshift mutation, whereas the other allele possesses four nucleotide deletions in intron 15, resulting in an aberrant transcript. These two mutations generate premature terminations of the protein. The type C or benign phenotype is characterized as a mild lactic acidosis but normal psychomotor development
additional information
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transgenic mice carrying a dominant-negative mutant CREB show a global reduction of gluconeogenic enzymes including PC, PEPCK and glucose 6-phosphatase
additional information
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deletion of the PC gene in this yeast impairs alcohol oxidase activity, causing the accumulation of inactive alcohol oxidase in the cytosol
additional information
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mutant strain STM5437contains an insertion in the PA5437 or pycR gene encoding for a pyruvate carboxylase regulator, PycR inactivation results in 100000fold attenuation of virulence in the rat lung in vivo, phenotype, overview
additional information
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overexpression of v-MAFA in INS1 cells causes a 5fold increase of pyruvate carboxylase mRNA
additional information
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stable overexpression of the enzyme in INS-1 cells leads to significantly upregulated insulin secretion and cell proliferation, while enzyme downregulation by siRNA expression reduces insulin secretion and cell proliferation, phenotypes, overview
additional information
suppression by stable expression of siRNA causes impaired anaplerosis and insulin secretion in insulinoma cells, knockout in INS-1 832/13 cells, cell lines U6 and CHS, and in INS-1 832/13-derived cell lines PCX3, PC1971, PC1973, PC3064, and PC118. Insulin release in response to pyruvate alone, 2-aminobicyclo[2,2,1]heptane-2-carboxylic acid plus glutamine, or methyl succinate plus beta-hydroxybutyrate is also decreased in the PC knockdown cells, phenotype, overview
additional information
construction of deletion mutants lacking the biotin carboxylase domain or both biotin carboxylase and biotin carboxyl carrier domains. The biotin carboxyl carrier domain devoid of biotin does not contribute directly to the enzymatic reaction, a deletion mutant demonstrates biotin-independent oxaloacetate decarboxylation activity
additional information
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construction of deletion mutants lacking the biotin carboxylase domain or both biotin carboxylase and biotin carboxyl carrier domains. The biotin carboxyl carrier domain devoid of biotin does not contribute directly to the enzymatic reaction, a deletion mutant demonstrates biotin-independent oxaloacetate decarboxylation activity
additional information
generation of functional, mixed hybrid tetramers using the E218A (inactive biotin carboxylase domain) and T882S (low pyruvate binding, low activity) mutant forms of pyruvate carboxylase. The apparent Ka pyruvate for the pyruvate-stimulated release of Pi by the hybrid tetramer is comparable to the wild-type enzyme and nearly 10fold lower than that for the T882S homotetramer. The ratio of the rates of oxaloacetate formation to Pi release for the WT:T882S[1:1] complex and 218A:T882S[1:1] hybrid tetramer-catalyzed reactions is 0.5 and 0.6, respectively, while the T882S homotetramer exhibits a near 1:1 coupling of the two domains
additional information
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construction of deletion mutants lacking the biotin carboxylase domain or both biotin carboxylase and biotin carboxyl carrier domains. The biotin carboxyl carrier domain devoid of biotin does not contribute directly to the enzymatic reaction, a deletion mutant demonstrates biotin-independent oxaloacetate decarboxylation activity
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additional information
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generation of functional, mixed hybrid tetramers using the E218A (inactive biotin carboxylase domain) and T882S (low pyruvate binding, low activity) mutant forms of pyruvate carboxylase. The apparent Ka pyruvate for the pyruvate-stimulated release of Pi by the hybrid tetramer is comparable to the wild-type enzyme and nearly 10fold lower than that for the T882S homotetramer. The ratio of the rates of oxaloacetate formation to Pi release for the WT:T882S[1:1] complex and 218A:T882S[1:1] hybrid tetramer-catalyzed reactions is 0.5 and 0.6, respectively, while the T882S homotetramer exhibits a near 1:1 coupling of the two domains
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additional information
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
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construction of chimeric enzymes of Pyc1 and Pyc2
additional information
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50% down-regulation of the enzyme in the RTG1 and the RTG2 mutants
additional information
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construction of chimeric enzymes of Pyc1 and Pyc2
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a Pseudomonas aeruginosa strain carrying the T7 polymerase gene can serve as a host for the overexpression of Mycobacterium smegmatis alpha4 under the control of the T7 promoter from a broad-host-range conjugative plasmid. Overexpression occurrs both in aerobic (LB medium) and nitrate-respiring anaerobic (LB medium plus glucose and nitrate) cultures. The latter system presents a simpler option because it involved room temperature cultures in stationary screw-cap bottles. Developed of a Pseudomonas aeruginosa DELTApyc strain that allows the expression of recombinant PYCs in the absence of the native enzyme
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a Pseudomonas aeruginosa strain carrying the T7 polymerase gene can serve as a host for the overexpression of Pseudomonas aeruginosa alpha4beta4 PYC under the control of the T7 promoter from a broad-host-range conjugative plasmid. Overexpression occurs both in aerobic (LB medium) and nitrate-respiring anaerobic (LB medium plus glucose and nitrate) cultures. The latter system presents a simpler option because it involved room temperature cultures in stationary screw-cap bottles. Development of a Pseudomonas aeruginosa DELTApyc strain that allows the expression of recombinant PYCs in the absence of the native enzyme
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codon-optimized expression in CHO cells
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coexpressed with human erythropoietin in BHK-21 cells
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coexpression of pyruvate carboxylase 1 isozyme (Pyc1) with an N-terminal myc tag, together with constructs encoding either the biotin carboxylase domain or the transcarboxylase-biotin carboxyl carrier domain, each with an N-terminal 9-histidine tag
DNA and amino acid sequence determination and analysis
DNA and amino acid sequence determination and analysis, expression mutant enzymes and of the isolated biotin carboxylase domain
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DNA and amino acid sequence determination and analysis, genetic structure, key cognate transcription factors regulating tissue-specific expression, transcriptional regulation, overview
DNA and amino acid sequence determination and analysis, genetic structure, key cognate transcription factors regulating tissue-specific expression. Five species of enzyme mRNAs have been reported, each having the same coding sequence but differing in their 5'-untranslated regions. These mRNA variants are the product of alternative splicing of two primary transcripts initiated from two alternative promoters, the proximal and the distal promoters. Neither of these promoters contains a TATA box but both possess multiple GC boxes. Production of specific forms of PC mRNA are linked to certain physiological states, i.e. development, gluconeogenesis and lipogenesis. Two pancreatic isletspecific transcription factors, i.e. pancreatic duodenal homeobox-1or PDX1, and v-MAFA, are involved in transcriptional regulation of the enzyme in INS1 cells. Identification of a putative cAMP-responsive element in the proximal promoter of the rat PC gene, transcriptional regulation, overview
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DNA and amino acid sequence determination and analysis, identification of promoter regions of bovine pyruvate carboxylase, putative transcription factor binding sites of promoter P1 and of P2, overview
expressed in Escherichia coli
expressed in Escherichia coli and Streptomyces lividans as a His-tagged fusion protein. In Streptomyces lividans a functional His-EhPYC1 is expressed
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli NZN111 and AFP111
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expressed in L-929 cells
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expression analysis of the enzyme in diverse wild-type and knockout insulinoma cell lines, overview
expression in CHO-K1-hGM-CSF cells
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expression in Escherichia coli GJT001, coexpression with pantothenate kinase
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expression in Escherichia coli JM109
expression in Escherichia coli mutant SBS110MG
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expression in Escherichia coli ptsG mutant
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expression in Escherichia coli wild-type GJT001 and mutants YBS121
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expression in type B pyruvate decarboxylase deficient skin fibroblasts
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expression of His9-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
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expression of the C-terminal region, excluding the mitochondrial targeting sequence, in Escherichia coli strain BL21(DE3)
expression of the subunits biotin carboxylase BC and carboxyl transferase CT (PC-(BC+CT)) and biotin carboxyl carrier protein BCCP (PC-(BCCP)) in Escherichia coli JM109
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FLAG-tagged human pyruvate carboxylase is introduced into a dihydrofolate-deficient CHO cell line DG44. Through the expression of the human pyruvate carboxylase enzyme, lactate formation in CHO cell culture can be efficiently reduced. This effect of expression of the human pyruvate carboxylase is observed not only in adherent batch culture using the serum-containing medium but in the serum-free suspension fed-batch culture as well, demonstrating its potential use to extend the culture longevity of CHO cell culture, which often shows a significant accumulation of lactate
genes pycA and pycB encoding two subunits are divergently transcribed upstream of pycR encoding for a pyruvate carboxylase regulator PycR, genomic organization of the PA5436-5435, pycAB, operon and the PA5437 or pycR gene, overview
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genetic structure, expression analysis, genotyping of genetic variants
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key cognate transcription factors regulating tissue-specific expression. The proximal promoter of the bovine PC gene mediates the mRNA variants that are restricted to gluconeogenic and lipogenic tissues, transcriptional regulation, overview
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Pyc1 isoform and C249A mutant
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stable overexpression in enzyme-deficient INS-1 insulinoma cell line
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the enzyme is expressed in 6 alternatively spliced variants that share a common ORF but differ in the 5'UTRs, resulting in different translational efficiencies, overview. In vitro transcription and translation by rabbit reticulocyte lysate as luciferase-linked protein, functional synthesis of luciferase, overview
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two genes PYC1 and PYC2 located on different chromosomes, expression of PYC1 and PYC2 is influenced by both the growth phase and carbon source, overview
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two polypeptide chain: PC-(BC) and PC-(CT+BCCP)
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wild-type and mutants without enzyme activity
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DNA and amino acid sequence determination and analysis
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DNA and amino acid sequence determination and analysis
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DNA and amino acid sequence determination and analysis, genetic structure, key cognate transcription factors regulating tissue-specific expression, transcriptional regulation, overview
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DNA and amino acid sequence determination and analysis, genetic structure, key cognate transcription factors regulating tissue-specific expression, transcriptional regulation, overview
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expressed in Escherichia coli as a His-tagged fusion protein
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expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli JM109
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expression in Escherichia coli JM109
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