6.3.4.14: biotin carboxylase
This is an abbreviated version!
For detailed information about biotin carboxylase, go to the full flat file.
Word Map on EC 6.3.4.14
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6.3.4.14
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carboxyltransferase
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carboxylases
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biotin-dependent
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malonyl-coa
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acetyl-coenzyme
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propionyl-coa
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carboxybiotin
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6.4.1.2
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biotin-carboxyl
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biotin-containing
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bicarbonate-dependent
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biotin-binding
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carboxyphosphate
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transcarboxylase
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mgatp-dependent
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accases
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atp-grasp
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medicine
- 6.3.4.14
- carboxyltransferase
- carboxylases
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biotin-dependent
- malonyl-coa
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acetyl-coenzyme
- propionyl-coa
- carboxybiotin
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6.4.1.2
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biotin-carboxyl
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biotin-containing
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bicarbonate-dependent
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biotin-binding
- carboxyphosphate
- transcarboxylase
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mgatp-dependent
- accases
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atp-grasp
- medicine
Reaction
Synonyms
ACC, AccA, AccBC, AccC, BC, biotin carboxylase, biotin carboxylase (component of acetyl CoA carboxylase), biotinoyl domain of acetyl-CoA carboxylase, BirA, Carboxylase, biotin, More, PC-beta
ECTree
6.3.4.14 biotin carboxylaseAdvanced search results
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results (Subunits
Subunits on EC 6.3.4.14 - biotin carboxylase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
homodimer
additional information
?
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x * 63400, calculation from nucleotide sequence, protein composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein
dimer
wild-type enzyme, dimerization is not an absolute requirement for the catalytic activity of the Escherichia coli biotin carboxylase subunit
homodimer
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2 * 50000, both subunits are required for activity and the two subunits must be in communication during enzyme function
additional information
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the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein
additional information
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geometry of the consensus Met-Lys-Met, MKM, motif, and structure of the biotinoyl domain of BCCP, overview. Binding pattern and interacting surfaces for the biotinoyl domain with BirA, overview
additional information
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3D structure of the hACC2 biotinoyl domain, geometry of the consensus Met-Lys-Met, MKM, motif, overview. The biotin group of hACC2 does not affect the structure of the biotinoyl domain, the human enzyme does not possess a thumb structure. Binding pattern and interacting surfaces for the ACC2 biotinoyl domain with Escherichia coli BirA enzyme, overview
additional information
biotin carboxylase contains three conserved domains, an N-terminal domain of carbamoyl-phosphate synthase L chain residues 73-181, a ATP binding domain of carbamoyl-phosphate synthase L chain, residues 186-395, and a C-terminal domain of biotin carboxylase
additional information
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biotin carboxylase contains three conserved domains, an N-terminal domain of carbamoyl-phosphate synthase L chain residues 73-181, a ATP binding domain of carbamoyl-phosphate synthase L chain, residues 186-395, and a C-terminal domain of biotin carboxylase
