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Literature summary for 6.4.1.1 extracted from

  • Xiang, S.; Tong, L.
    Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction (2008), Nat. Struct. Mol. Biol., 15, 295-302.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
acetyl-CoA
-
Homo sapiens
acetyl-CoA
-
Staphylococcus aureus

Cloned(Commentary)

Cloned (Comment) Organism
expression of the C-terminal region, excluding the mitochondrial targeting sequence, in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
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
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

Protein Variants Comment Organism
F1077A mutant cyrstal structure, overview Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Staphylococcus aureus
Mg2+ the biotin carboxylase domain requires divalent cations for binding of the ATP substrate and for catalysis Homo sapiens
Mn2+ the carboxytransferase domain contains a tightly bound Mn2+ Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens P11498
-
-
Staphylococcus aureus A0A0H3JRU9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminal region from Escherichia coli strain BL21(DE3) Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate + HCO3-
-
Staphylococcus aureus ADP + phosphate + oxaloacetate
-
?
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
-
?
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
-
?
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

Subunits Comment Organism
More localization of a BCCP domain is located in the active site of the carboxytransferase domain that participates in the carboxyltransfer reaction Homo sapiens
More localization of a BCCP domain is located in the active site of the carboxytransferase domain that participates in the carboxyltransfer reaction Staphylococcus aureus
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
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Homo sapiens
ATP dependent on Staphylococcus aureus
biotin dependent on Homo sapiens
biotin dependent on Staphylococcus aureus