Literature summary for 6.3.4.14 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 .

Search for more literature for 6.3.4.14

Cloned(Commentary)

Cloned (Comment)	Organism
-	Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism

Organism	UniProt	Comment	Textmining
Haemophilus influenzae	P43873	-	-
Haemophilus influenzae DSM 11121	P43873	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?
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

Synonyms	Comment	Organism
AccC	-	Haemophilus influenzae

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Release 2023.1 (January 2023)