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Literature summary extracted from

  • Jitrapakdee, S.; St Maurice, M.; Rayment, I.; Cleland, W.W.; Wallace, J.C.; Attwood, P.V.
    Structure, mechanism and regulation of pyruvate carboxylase (2008), Biochem. J., 413, 369-387.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.4.1.1 acetyl-CoA allosteric activator Mus musculus
6.4.1.1 acetyl-CoA allosteric activator Homo sapiens
6.4.1.1 acetyl-CoA allosteric activator Rattus norvegicus
6.4.1.1 acetyl-CoA allosteric activator Saccharomyces cerevisiae
6.4.1.1 acetyl-CoA allosteric activator Bos taurus
6.4.1.1 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
6.4.1.1 additional information starvation enhances pyruvate carboxylase activity. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively Homo sapiens
6.4.1.1 additional information starvation enhances pyruvate carboxylase activity. Pyruvate carboxylase and PEP carboxykinaseacts cooperatively Rattus norvegicus
6.4.1.1 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(Commentary)

EC Number Cloned (Comment) Organism
6.4.1.1 DNA and amino acid sequence determination and analysis Staphylococcus aureus
6.4.1.1 DNA and amino acid sequence determination and analysis Rhizobium etli
6.4.1.1 DNA and amino acid sequence determination and analysis, expression mutant enzymes and of the isolated biotin carboxylase domain Geobacillus thermodenitrificans
6.4.1.1 DNA and amino acid sequence determination and analysis, genetic structure, key cognate transcription factors regulating tissue-specific expression, transcriptional regulation, overview Mus musculus
6.4.1.1 DNA and amino acid sequence determination and analysis, genetic structure, key cognate transcription factors regulating tissue-specific expression, transcriptional regulation, overview Homo sapiens
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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 (Commentary)

EC Number Crystallization (Comment) Organism
6.4.1.1 crystal structure analysis Staphylococcus aureus
6.4.1.1 crystal structure analysis Rhizobium etli

Protein Variants

EC Number Protein Variants Comment Organism
6.4.1.1 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
6.4.1.1 M743I naturally occurring mutation involved in pyruvate carboxylase deficiency type A Homo sapiens
6.4.1.1 additional information 50% down-regulation of the enzyme in the RTG1 and the RTG2 mutants Saccharomyces cerevisiae
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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
6.4.1.1 additional information overexpression of v-MAFA in INS1 cells causes a 5fold increase of pyruvate carboxylase mRNA Rattus norvegicus
6.4.1.1 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
6.4.1.1 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
6.4.1.1 R451C naturally occurring mutation involved in pyruvate carboxylase deficiency type A, the mutant enzyme shows markedly decreased acetyl-CoA-dependent activation Homo sapiens
6.4.1.1 V145A naturally occurring mutation involved in pyruvate carboxylase deficiency type A Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.4.1.1 L-aspartate allosteric inhibitor Bos taurus
6.4.1.1 L-aspartate allosteric inhibitor Homo sapiens
6.4.1.1 L-aspartate allosteric inhibitor Mus musculus
6.4.1.1 L-aspartate allosteric inhibitor Rattus norvegicus
6.4.1.1 L-aspartate allosteric inhibitor Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.4.1.1 cytosol isozymes PYC1 and PYC2 Saccharomyces cerevisiae 5829
-
6.4.1.1 mitochondrial matrix
-
 Mus musculus 5759
-
6.4.1.1 mitochondrial matrix
-
 Homo sapiens 5759
-
6.4.1.1 mitochondrial matrix
-
 Rattus norvegicus 5759
-
6.4.1.1 mitochondrial matrix
-
 Bos taurus 5759
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.4.1.1 Mg2+ as MgATP2- Staphylococcus aureus
6.4.1.1 Mg2+ as MgATP2- Mus musculus
6.4.1.1 Mg2+ as MgATP2- Homo sapiens
6.4.1.1 Mg2+ as MgATP2- Rattus norvegicus
6.4.1.1 Mg2+ as MgATP2- Saccharomyces cerevisiae
6.4.1.1 Mg2+ as MgATP2- Bos taurus
6.4.1.1 Mg2+ as MgATP2- Pseudomonas sp.
6.4.1.1 Mg2+ as MgATP2- Komagataella pastoris
6.4.1.1 Mg2+ as MgATP2- Ogataea angusta
6.4.1.1 Mg2+ as MgATP2- Rhizobium etli
6.4.1.1 Mg2+ as MgATP2- Methanobacterium sp.
6.4.1.1 Mg2+ as MgATP2- Methanococcus sp.
6.4.1.1 Mg2+ as MgATP2- Aquifex aeolicus
6.4.1.1 Mg2+ as MgATP2- Geobacillus thermodenitrificans
6.4.1.1 Mg2+ as MgATP2- Methanosarcina sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.4.1.1 55000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Pseudomonas sp.
6.4.1.1 55000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanobacterium sp.
6.4.1.1 55000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanococcus sp.
6.4.1.1 55000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Aquifex aeolicus
6.4.1.1 55000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanosarcina sp.
6.4.1.1 70000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Pseudomonas sp.
6.4.1.1 70000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanobacterium sp.
6.4.1.1 70000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanococcus sp.
6.4.1.1 70000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Aquifex aeolicus
6.4.1.1 70000
-
 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanosarcina sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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 ?
-
 ?
6.4.1.1 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 ?
-
 ?
6.4.1.1 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 ?
-
 ?
6.4.1.1 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 ?
-
 ?
6.4.1.1 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

EC Number Organism UniProt Comment Textmining
6.4.1.1 Aquifex aeolicus
-
-
-
6.4.1.1 Bos taurus
-
-
-
6.4.1.1 Geobacillus thermodenitrificans
-
-
-
6.4.1.1 Homo sapiens
-
-
-
6.4.1.1 Komagataella pastoris
-
-
-
6.4.1.1 Methanobacterium sp.
-
-
-
6.4.1.1 Methanococcus sp.
-
-
-
6.4.1.1 Methanosarcina sp.
-
-
-
6.4.1.1 Mus musculus
-
-
-
6.4.1.1 Ogataea angusta
-
-
-
6.4.1.1 Pseudomonas sp.
-
-
-
6.4.1.1 Rattus norvegicus
-
-
-
6.4.1.1 Rhizobium etli
-
-
-
6.4.1.1 Saccharomyces cerevisiae
-
 two isozymes PYC1 and PYC2
-
6.4.1.1 Staphylococcus aureus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Staphylococcus aureus
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Mus musculus
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Homo sapiens
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Rattus norvegicus
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Saccharomyces cerevisiae
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Bos taurus
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Pseudomonas sp.
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Komagataella pastoris
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Ogataea angusta
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Rhizobium etli
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Methanobacterium sp.
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Methanococcus sp.
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Aquifex aeolicus
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Geobacillus thermodenitrificans
a
6.4.1.1 ATP + pyruvate + HCO3- + H+ = ADP + phosphate + oxaloacetate reaction mechanism, overview Methanosarcina sp.
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.4.1.1 3T3-L1 cell
-
 Mus musculus
-
6.4.1.1 adipocyte tight regulation of enzyme expression with differentiation Mus musculus
-
6.4.1.1 adipose tissue
-
 Mus musculus
-
6.4.1.1 adipose tissue
-
 Homo sapiens
-
6.4.1.1 adipose tissue
-
 Rattus norvegicus
-
6.4.1.1 adipose tissue
-
 Bos taurus
-
6.4.1.1 astrocyte
-
 Mus musculus
-
6.4.1.1 astrocyte
-
 Homo sapiens
-
6.4.1.1 astrocyte
-
 Rattus norvegicus
-
6.4.1.1 astrocyte
-
 Bos taurus
-
6.4.1.1 brain
-
 Mus musculus
-
6.4.1.1 brain
-
 Homo sapiens
-
6.4.1.1 brain
-
 Rattus norvegicus
-
6.4.1.1 brain
-
 Bos taurus
-
6.4.1.1 erythrocyte
-
 Mus musculus
-
6.4.1.1 erythrocyte
-
 Homo sapiens
-
6.4.1.1 erythrocyte
-
 Rattus norvegicus
-
6.4.1.1 erythrocyte
-
 Bos taurus
-
6.4.1.1 kidney cortex Mus musculus
-
6.4.1.1 kidney cortex Homo sapiens
-
6.4.1.1 kidney cortex Rattus norvegicus
-
6.4.1.1 kidney cortex Bos taurus
-
6.4.1.1 liver
-
 Mus musculus
-
6.4.1.1 liver
-
 Homo sapiens
-
6.4.1.1 liver
-
 Rattus norvegicus
-
6.4.1.1 liver
-
 Bos taurus
-
6.4.1.1 additional information tissue-specific expression Homo sapiens
-
6.4.1.1 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
-
6.4.1.1 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
-
6.4.1.1 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
-
6.4.1.1 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
-
6.4.1.1 neuron
-
 Mus musculus
-
6.4.1.1 neuron
-
 Homo sapiens
-
6.4.1.1 neuron
-
 Rattus norvegicus
-
6.4.1.1 neuron
-
 Bos taurus
-
6.4.1.1 pancreatic islet
-
 Mus musculus
-
6.4.1.1 pancreatic islet
-
 Homo sapiens
-
6.4.1.1 pancreatic islet
-
 Rattus norvegicus
-
6.4.1.1 pancreatic islet
-
 Bos taurus
-
6.4.1.1 small intestine
-
 Mus musculus
-
6.4.1.1 small intestine
-
 Homo sapiens
-
6.4.1.1 small intestine
-
 Rattus norvegicus
-
6.4.1.1 small intestine
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 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
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Staphylococcus aureus ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Mus musculus ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Homo sapiens ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Rattus norvegicus ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Saccharomyces cerevisiae ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Bos taurus ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Pseudomonas sp. ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Komagataella pastoris ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Ogataea angusta ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Rhizobium etli ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Methanobacterium sp. ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Methanococcus sp. ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Aquifex aeolicus ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
-
 Geobacillus thermodenitrificans ADP + phosphate + oxaloacetate
-
 ?
6.4.1.1 ATP + pyruvate + HCO3- + H+
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 Methanosarcina sp. ADP + phosphate + oxaloacetate
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 ?
6.4.1.1 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
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 ?
6.4.1.1 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
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 ?
6.4.1.1 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
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 ?
6.4.1.1 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
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 ?
6.4.1.1 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
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 ?
6.4.1.1 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 ?
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 ?
6.4.1.1 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 ?
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 ?
6.4.1.1 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 ?
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 ?
6.4.1.1 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 ?
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6.4.1.1 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 ?
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 ?
6.4.1.1 additional information ATP cleavage by the recombinantly expressed isolated biotin carboxylase domain, overview Geobacillus thermodenitrificans ?
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6.4.1.1 additional information the enzyme in adipocytes interacts with prohibitin, a protein involved in mitochondrial biogenesis Mus musculus ?
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6.4.1.1 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

EC Number Subunits Comment Organism
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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.
6.4.1.1 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.
6.4.1.1 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.
6.4.1.1 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.
6.4.1.1 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
6.4.1.1 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
6.4.1.1 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
6.4.1.1 octamer 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Pseudomonas sp.
6.4.1.1 octamer 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanobacterium sp.
6.4.1.1 octamer 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanococcus sp.
6.4.1.1 octamer 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Aquifex aeolicus
6.4.1.1 octamer 4 * 55000, about, alpha-subunit, + 4 * 70000, about, beta-subunit Methanosarcina sp.
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Staphylococcus aureus
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Mus musculus
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Homo sapiens
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Rattus norvegicus
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Saccharomyces cerevisiae
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Bos taurus
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Komagataella pastoris
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Ogataea angusta
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Rhizobium etli
6.4.1.1 tetramer 4 * 120000-130000, alpha4 Geobacillus thermodenitrificans

Cofactor

EC Number Cofactor Comment Organism Structure
6.4.1.1 ATP as MgATP2-, dependent on Staphylococcus aureus
6.4.1.1 ATP as MgATP2-, dependent on Mus musculus
6.4.1.1 ATP as MgATP2-, dependent on Homo sapiens
6.4.1.1 ATP as MgATP2-, dependent on Rattus norvegicus
6.4.1.1 ATP as MgATP2-, dependent on Saccharomyces cerevisiae
6.4.1.1 ATP as MgATP2-, dependent on Bos taurus
6.4.1.1 ATP as MgATP2-, dependent on Pseudomonas sp.
6.4.1.1 ATP as MgATP2-, dependent on Komagataella pastoris
6.4.1.1 ATP as MgATP2-, dependent on Ogataea angusta
6.4.1.1 ATP as MgATP2-, dependent on Rhizobium etli
6.4.1.1 ATP as MgATP2-, dependent on Methanobacterium sp.
6.4.1.1 ATP as MgATP2-, dependent on Methanococcus sp.
6.4.1.1 ATP as MgATP2-, dependent on Aquifex aeolicus
6.4.1.1 ATP as MgATP2-, dependent on Geobacillus thermodenitrificans
6.4.1.1 ATP as MgATP2-, dependent on Methanosarcina sp.
6.4.1.1 biotin dependent on Pseudomonas sp.
6.4.1.1 biotin dependent on Methanobacterium sp.
6.4.1.1 biotin dependent on Methanococcus sp.
6.4.1.1 biotin dependent on Aquifex aeolicus
6.4.1.1 biotin dependent on Methanosarcina sp.
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Staphylococcus aureus
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Mus musculus
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Homo sapiens
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Rattus norvegicus
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Saccharomyces cerevisiae
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Bos taurus
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Komagataella pastoris
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Ogataea angusta
6.4.1.1 biotin dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus Rhizobium etli
6.4.1.1 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