Activating Compound | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | allosteric activator | Mus musculus | |
acetyl-CoA | allosteric activator | Homo sapiens | |
acetyl-CoA | allosteric activator | Rattus norvegicus | |
acetyl-CoA | allosteric activator | Saccharomyces cerevisiae | |
acetyl-CoA | allosteric activator | Bos taurus | |
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 | Mus musculus | |
additional information | starvation enhances pyruvate carboxylase activity. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively | Homo sapiens | |
additional information | starvation enhances pyruvate carboxylase activity. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively | Rattus norvegicus | |
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 | Bos taurus |
Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis | Staphylococcus aureus |
DNA and amino acid sequence determination and analysis | Rhizobium etli |
DNA and amino acid sequence determination and analysis, expression mutant enzymes and of the isolated biotin carboxylase domain | Geobacillus thermodenitrificans |
DNA and amino acid sequence determination and analysis, genetic structure, key cognate transcription factors regulating tissue-specific expression, transcriptional regulation, overview | Mus musculus |
DNA and amino acid sequence determination and analysis, genetic structure, key cognate transcription factors regulating tissue-specific expression, transcriptional regulation, overview | Homo sapiens |
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 | Rattus norvegicus |
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 | Bos taurus |
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 | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
---|---|
crystal structure analysis | Staphylococcus aureus |
crystal structure analysis | Rhizobium etli |
Protein Variants | Comment | Organism |
---|---|---|
A610T | naturally occurring mutation involved in pyruvate carboxylase deficiency type A, the mutant's catalytic activity and steady-state level are markedly decreased | Homo sapiens |
M743I | naturally occurring mutation involved in pyruvate carboxylase deficiency type A | Homo sapiens |
additional information | 50% down-regulation of the enzyme in the RTG1 and the RTG2 mutants | Saccharomyces cerevisiae |
additional information | 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 | Aquifex aeolicus |
additional information | 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 | Geobacillus thermodenitrificans |
additional information | deletion of the PC gene in this yeast impairs alcohol oxidase activity, causing the accumulation of inactive alcohol oxidase in the cytosol | Ogataea angusta |
additional information | overexpression of v-MAFA in INS1 cells causes a 5fold increase of pyruvate carboxylase mRNA | Rattus norvegicus |
additional information | 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 | Homo sapiens |
additional information | transgenic mice carrying a dominant-negative mutant CREB show a global reduction of gluconeogenic enzymes including PC, PEPCK and glucose 6-phosphatase | Mus musculus |
R451C | naturally occurring mutation involved in pyruvate carboxylase deficiency type A, the mutant enzyme shows markedly decreased acetyl-CoA-dependent activation | Homo sapiens |
V145A | naturally occurring mutation involved in pyruvate carboxylase deficiency type A | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-aspartate | allosteric inhibitor | Bos taurus | |
L-aspartate | allosteric inhibitor | Homo sapiens | |
L-aspartate | allosteric inhibitor | Mus musculus | |
L-aspartate | allosteric inhibitor | Rattus norvegicus | |
L-aspartate | allosteric inhibitor | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | isozymes PYC1 and PYC2 | Saccharomyces cerevisiae | 5829 | - |
mitochondrial matrix | - |
Mus musculus | 5759 | - |
mitochondrial matrix | - |
Homo sapiens | 5759 | - |
mitochondrial matrix | - |
Rattus norvegicus | 5759 | - |
mitochondrial matrix | - |
Bos taurus | 5759 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | as MgATP2- | Staphylococcus aureus | |
Mg2+ | as MgATP2- | Mus musculus | |
Mg2+ | as MgATP2- | Homo sapiens | |
Mg2+ | as MgATP2- | Rattus norvegicus | |
Mg2+ | as MgATP2- | Saccharomyces cerevisiae | |
Mg2+ | as MgATP2- | Bos taurus | |
Mg2+ | as MgATP2- | Pseudomonas sp. | |
Mg2+ | as MgATP2- | Komagataella pastoris | |
Mg2+ | as MgATP2- | Ogataea angusta | |
Mg2+ | as MgATP2- | Rhizobium etli | |
Mg2+ | as MgATP2- | Methanobacterium sp. | |
Mg2+ | as MgATP2- | Methanococcus sp. | |
Mg2+ | as MgATP2- | Aquifex aeolicus | |
Mg2+ | as MgATP2- | Geobacillus thermodenitrificans | |
Mg2+ | as MgATP2- | Methanosarcina sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
55000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Pseudomonas sp. |
55000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanobacterium sp. |
55000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanococcus sp. |
55000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Aquifex aeolicus |
55000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanosarcina sp. |
70000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Pseudomonas sp. |
70000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanobacterium sp. |
70000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanococcus sp. |
70000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Aquifex aeolicus |
70000 | - |
4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanosarcina sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + pyruvate + HCO3- | Staphylococcus aureus | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Pseudomonas sp. | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Ogataea angusta | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Rhizobium etli | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Aquifex aeolicus | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Geobacillus thermodenitrificans | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Saccharomyces cerevisiae | 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 | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Mus musculus | 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 | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Homo sapiens | 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 | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | Rattus norvegicus | 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 | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | Komagataella pastoris | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | Methanobacterium sp. | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | Methanococcus sp. | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | Methanosarcina sp. | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | Bos taurus | 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 | ADP + phosphate + oxaloacetate | - |
? | |
additional information | Saccharomyces cerevisiae | 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 | Komagataella pastoris | 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 | Ogataea angusta | 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 | Mus musculus | 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 | Rattus norvegicus | starvation enhances pyruvate carboxylase activity, whereas diabetes also increases gluconeogenesis through enhanced uptake of substrate and increased flux through liver pyruvate carboxylase rats | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | - |
- |
- |
Bos taurus | - |
- |
- |
Geobacillus thermodenitrificans | - |
- |
- |
Homo sapiens | - |
- |
- |
Komagataella pastoris | - |
- |
- |
Methanobacterium sp. | - |
- |
- |
Methanococcus sp. | - |
- |
- |
Methanosarcina sp. | - |
- |
- |
Mus musculus | - |
- |
- |
Ogataea angusta | - |
- |
- |
Pseudomonas sp. | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Rhizobium etli | - |
- |
- |
Saccharomyces cerevisiae | - |
two isozymes PYC1 and PYC2 | - |
Staphylococcus aureus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Staphylococcus aureus | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Mus musculus | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Homo sapiens | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Rattus norvegicus | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Saccharomyces cerevisiae | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Bos taurus | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Pseudomonas sp. | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Komagataella pastoris | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Ogataea angusta | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Rhizobium etli | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Methanobacterium sp. | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Methanococcus sp. | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Aquifex aeolicus | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Geobacillus thermodenitrificans | |
ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate | reaction mechanism, overview | Methanosarcina sp. |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
3T3-L1 cell | - |
Mus musculus | - |
adipocyte | tight regulation of enzyme expression with differentiation | Mus musculus | - |
adipose tissue | - |
Mus musculus | - |
adipose tissue | - |
Homo sapiens | - |
adipose tissue | - |
Rattus norvegicus | - |
adipose tissue | - |
Bos taurus | - |
astrocyte | - |
Mus musculus | - |
astrocyte | - |
Homo sapiens | - |
astrocyte | - |
Rattus norvegicus | - |
astrocyte | - |
Bos taurus | - |
brain | - |
Mus musculus | - |
brain | - |
Homo sapiens | - |
brain | - |
Rattus norvegicus | - |
brain | - |
Bos taurus | - |
erythrocyte | - |
Mus musculus | - |
erythrocyte | - |
Homo sapiens | - |
erythrocyte | - |
Rattus norvegicus | - |
erythrocyte | - |
Bos taurus | - |
kidney | cortex | Mus musculus | - |
kidney | cortex | Homo sapiens | - |
kidney | cortex | Rattus norvegicus | - |
kidney | cortex | Bos taurus | - |
liver | - |
Mus musculus | - |
liver | - |
Homo sapiens | - |
liver | - |
Rattus norvegicus | - |
liver | - |
Bos taurus | - |
additional information | tissue-specific expression | Homo sapiens | - |
additional information | expression of the two isoenzymes is differentially regulated and expressed during different growth conditions, expression of PYC1 and PYC2 is influenced by both the growth phase and carbon source, overview | Saccharomyces cerevisiae | - |
additional information | tissue-specific expression, production of specific forms of PC mRNA are linked to certain physiological states, i.e. development, gluconeogenesis and lipogenesis | Rattus norvegicus | - |
additional information | tissue-specific expression. In dairy cows, the expression of the enzyme is markedly elevated during the transition from calving to lactation | Bos taurus | - |
additional information | tissue-specific expression. In murine 3T3-L1 adipocytes, pyruvate carboxylase protein, its activity and mRNA are elevated in parallel with other key lipogenic enzymes, which increase concomitantly with the accumulation of lipid droplets during terminal differentiation of adipocytes | Mus musculus | - |
neuron | - |
Mus musculus | - |
neuron | - |
Homo sapiens | - |
neuron | - |
Rattus norvegicus | - |
neuron | - |
Bos taurus | - |
pancreatic islet | - |
Mus musculus | - |
pancreatic islet | - |
Homo sapiens | - |
pancreatic islet | - |
Rattus norvegicus | - |
pancreatic islet | - |
Bos taurus | - |
small intestine | - |
Mus musculus | - |
small intestine | - |
Homo sapiens | - |
small intestine | - |
Rattus norvegicus | - |
small intestine | - |
Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + pyruvate + HCO3- | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Staphylococcus aureus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Pseudomonas sp. | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Ogataea angusta | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Rhizobium etli | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Aquifex aeolicus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Geobacillus thermodenitrificans | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | 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 | Saccharomyces cerevisiae | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | 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 | Mus musculus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | 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 | Homo sapiens | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- | 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 | Rattus norvegicus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Staphylococcus aureus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Mus musculus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Homo sapiens | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Rattus norvegicus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Saccharomyces cerevisiae | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Bos taurus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Pseudomonas sp. | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Komagataella pastoris | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Ogataea angusta | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Rhizobium etli | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Methanobacterium sp. | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Methanococcus sp. | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Aquifex aeolicus | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Geobacillus thermodenitrificans | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | - |
Methanosarcina sp. | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Komagataella pastoris | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Methanobacterium sp. | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Methanococcus sp. | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview | Methanosarcina sp. | ADP + phosphate + oxaloacetate | - |
? | |
ATP + pyruvate + HCO3- + H+ | 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 | Bos taurus | ADP + phosphate + oxaloacetate | - |
? | |
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 | Saccharomyces cerevisiae | ? | - |
? | |
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 | Komagataella pastoris | ? | - |
? | |
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 | Ogataea angusta | ? | - |
? | |
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 | Mus musculus | ? | - |
? | |
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 | Rattus norvegicus | ? | - |
? | |
additional information | ATP cleavage by the recombinantly expressed isolated biotin carboxylase domain, overview | Geobacillus thermodenitrificans | ? | - |
? | |
additional information | the enzyme in adipocytes interacts with prohibitin, a protein involved in mitochondrial biogenesis | Mus musculus | ? | - |
? | |
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 | Ogataea angusta | ? | - |
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Subunits | Comment | Organism |
---|---|---|
More | all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview | Mus musculus |
More | all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview | Homo sapiens |
More | all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview | Rattus norvegicus |
More | all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview | Saccharomyces cerevisiae |
More | all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview | Bos taurus |
More | all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview | Komagataella pastoris |
More | all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview | Ogataea angusta |
More | all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview | Geobacillus thermodenitrificans |
More | 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 | Pseudomonas sp. |
More | 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 | Methanobacterium sp. |
More | 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 | Methanococcus sp. |
More | 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 | Methanosarcina sp. |
More | 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 | Aquifex aeolicus |
More | 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 | Staphylococcus aureus |
More | 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 | Rhizobium etli |
octamer | 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Pseudomonas sp. |
octamer | 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanobacterium sp. |
octamer | 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanococcus sp. |
octamer | 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Aquifex aeolicus |
octamer | 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit | Methanosarcina sp. |
tetramer | 4 * 120000-130000, alpha4 | Staphylococcus aureus |
tetramer | 4 * 120000-130000, alpha4 | Mus musculus |
tetramer | 4 * 120000-130000, alpha4 | Homo sapiens |
tetramer | 4 * 120000-130000, alpha4 | Rattus norvegicus |
tetramer | 4 * 120000-130000, alpha4 | Saccharomyces cerevisiae |
tetramer | 4 * 120000-130000, alpha4 | Bos taurus |
tetramer | 4 * 120000-130000, alpha4 | Komagataella pastoris |
tetramer | 4 * 120000-130000, alpha4 | Ogataea angusta |
tetramer | 4 * 120000-130000, alpha4 | Rhizobium etli |
tetramer | 4 * 120000-130000, alpha4 | Geobacillus thermodenitrificans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | as MgATP2-, dependent on | Staphylococcus aureus | |
ATP | as MgATP2-, dependent on | Mus musculus | |
ATP | as MgATP2-, dependent on | Homo sapiens | |
ATP | as MgATP2-, dependent on | Rattus norvegicus | |
ATP | as MgATP2-, dependent on | Saccharomyces cerevisiae | |
ATP | as MgATP2-, dependent on | Bos taurus | |
ATP | as MgATP2-, dependent on | Pseudomonas sp. | |
ATP | as MgATP2-, dependent on | Komagataella pastoris | |
ATP | as MgATP2-, dependent on | Ogataea angusta | |
ATP | as MgATP2-, dependent on | Rhizobium etli | |
ATP | as MgATP2-, dependent on | Methanobacterium sp. | |
ATP | as MgATP2-, dependent on | Methanococcus sp. | |
ATP | as MgATP2-, dependent on | Aquifex aeolicus | |
ATP | as MgATP2-, dependent on | Geobacillus thermodenitrificans | |
ATP | as MgATP2-, dependent on | Methanosarcina sp. | |
biotin | dependent on | Pseudomonas sp. | |
biotin | dependent on | Methanobacterium sp. | |
biotin | dependent on | Methanococcus sp. | |
biotin | dependent on | Aquifex aeolicus | |
biotin | dependent on | Methanosarcina sp. | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Staphylococcus aureus | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Mus musculus | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Homo sapiens | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Rattus norvegicus | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Saccharomyces cerevisiae | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Bos taurus | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Komagataella pastoris | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Ogataea angusta | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus | Rhizobium etli | |
biotin | dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus, the main action of acetyl-CoA is to enhance the rate of the carboxylation of biotin in the overall reaction | Geobacillus thermodenitrificans |