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Literature summary extracted from

  • Broussard, T.C.; Pakhomova, S.; Neau, D.B.; Bonnot, R.; Waldrop, G.L.
    Structural analysis of substrate, reaction intermediate, and product binding in Haemophilus influenzae biotin carboxylase (2015), Biochemistry, 54, 3860-3870 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.4.14
-
Haemophilus influenzae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.14 in complex with hydrogencarbonate, the ATP analogue AMP-PCP, phosphonoacetamide and phosphonoformate, ADP and phosphate and the carboxybiotin analogue N1'-methoxycarbonyl biotin methyl ester. Hydrogencarbonate, phosphate, and the methyl ester of the carboxyl group of N1'-methoxycarbonyl biotin methyl ester all bind in the same pocket in the active site of biotin carboxylase Haemophilus influenzae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.3.15 [biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA Haemophilus influenzae
-
[biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.15 Haemophilus influenzae
-
-
-
6.3.4.14 Haemophilus influenzae P43873
-
-
6.3.4.14 Haemophilus influenzae DSM 11121 P43873
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.15 [biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA
-
Haemophilus influenzae [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
-
?
6.3.4.14 additional information during the catalytic mechanism, the binding pocket that binds tetrahedral phosphate also accommodates and stabilizes a tetrahedral dianionic transition state resulting from direct transfer of CO2 from the carboxyphosphate intermediate to biotin Haemophilus influenzae ?
-
?
6.3.4.14 additional information during the catalytic mechanism, the binding pocket that binds tetrahedral phosphate also accommodates and stabilizes a tetrahedral dianionic transition state resulting from direct transfer of CO2 from the carboxyphosphate intermediate to biotin Haemophilus influenzae DSM 11121 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.1.3.15 acetyl-CoA carboxylase the enzyme is composed of three proteins: biotin carboxylase, a biotin carboxyl carrier protein, and carboxyltransferase Haemophilus influenzae
2.1.3.15 carboxyltransferase
-
Haemophilus influenzae
6.3.4.14 AccC
-
Haemophilus influenzae