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Literature summary extracted from
- Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction (2008), Nat. Struct. Mol. Biol., 15, 295-302.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 6.4.1.1 | acetyl-CoA | - |
Homo sapiens |  |
| 6.4.1.1 | acetyl-CoA | - |
Staphylococcus aureus | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 6.4.1.1 | expression of the C-terminal region, excluding the mitochondrial targeting sequence, in Escherichia coli strain BL21(DE3) | Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 6.4.1.1 | C-terminal region, and wild-type and F1077A mutant enzymes, microseeding, room temprarture, sitting drop method using a reservoir solution containing 0.8% w/v PEG 3350 and 90 mM MnCl for the wild-type and 15% w/v PEG 3350 and 200 mM ammonium tartrate for the mutant, X-ray diffraction structure determination and analysis at 2.8 A resolution | Homo sapiens |
| 6.4.1.1 | purified enzyme in presence of 5 mM ATP and 5 mM oxaloacetic acid, sitting drop method, room temperature, the reservoir solution contains 20% w/v PEG 3350 and 200 mM ammonium tartrate, X-ray diffraction structure determination and analysis at 2.8 A resolution | Staphylococcus aureus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 6.4.1.1 | F1077A | mutant cyrstal structure, overview | Homo sapiens |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 6.4.1.1 | Mg2+ | - |
Staphylococcus aureus | |
| 6.4.1.1 | Mg2+ | the biotin carboxylase domain requires divalent cations for binding of the ATP substrate and for catalysis | Homo sapiens | |
| 6.4.1.1 | Mn2+ | the carboxytransferase domain contains a tightly bound Mn2+ | Homo sapiens | |
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 enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, and other cellular processes | ADP + phosphate + oxaloacetate | - |
? | |
| 6.4.1.1 | ATP + pyruvate + HCO3- | Homo sapiens | the enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, insulin secretion and other cellular processes | ADP + phosphate + oxaloacetate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 6.4.1.1 | Homo sapiens | P11498 | - |
- |
| 6.4.1.1 | Staphylococcus aureus | A0A0H3JRU9 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 6.4.1.1 | recombinant C-terminal region from Escherichia coli strain BL21(DE3) | Homo sapiens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 6.4.1.1 | ATP + pyruvate + HCO3- | - |
Staphylococcus aureus | ADP + phosphate + oxaloacetate | - |
? | |
| 6.4.1.1 | ATP + pyruvate + HCO3- | the enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, and other cellular processes | Staphylococcus aureus | ADP + phosphate + oxaloacetate | - |
? | |
| 6.4.1.1 | ATP + pyruvate + HCO3- | the enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, insulin secretion and other cellular processes | Homo sapiens | ADP + phosphate + oxaloacetate | - |
? | |
| 6.4.1.1 | ATP + pyruvate + HCO3- | 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 | Homo sapiens | ADP + phosphate + oxaloacetate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 6.4.1.1 | More | localization of a BCCP domain is located in the active site of the carboxytransferase domain that participates in the carboxyltransfer reaction | Homo sapiens |
| 6.4.1.1 | More | localization of a BCCP domain is located in the active site of the carboxytransferase domain that participates in the carboxyltransfer reaction | Staphylococcus aureus |
| 6.4.1.1 | tetramer | tetrameric organization of wild-type and isolated C-terminal region, the PC tetramerization, PT, domain is important for oligomerization, conserved mode of tetramerization | Staphylococcus aureus |
| 6.4.1.1 | 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 | Homo sapiens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 6.4.1.1 | 7.5 | - |
assay at | Homo sapiens |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 6.4.1.1 | ATP | dependent on | Homo sapiens | |
| 6.4.1.1 | ATP | dependent on | Staphylococcus aureus | |
| 6.4.1.1 | biotin | dependent on | Homo sapiens | |
| 6.4.1.1 | biotin | dependent on | Staphylococcus aureus | |
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Release 2023.1 (January 2023)
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