Literature summary for 3.5.1.12 extracted from

Kothapalli, N.; Camporeale, G.; Kueh, A.; Chew, Y.C.; Oomme, A.M.; Griffin, J.B.; Zempleni, J.
Biological functions of biotinylated histones (2005), J. Nutr. Biochem., 16, 446-448.

Search for more literature for 3.5.1.12

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
biocytin + H2O	Homo sapiens	i.e. biotin-epsilon-lysine. The enzyme is involved in modification of histones by covalent attachment of the vitamin biotin. A reaction mechanism is proposed by which cleavage of biocytin by biotinidase leads to the formation of a biotinyl-thioester intermediate (cysteine-bound biotin) at or near the active site of biotinidase. In the next step, the biotinyl moiety is transferred from the thioester to the epsilon-amino group of lysine in histones. Biotinidase may catalyze both biotinylation and debiotinylation of histones	biotin + L-lysine	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
biocytin + H2O	i.e. biotin-epsilon-lysine. The enzyme is involved in modification of histones by covalent attachment of the vitamin biotin. A reaction mechanism is proposed by which cleavage of biocytin by biotinidase leads to the formation of a biotinyl-thioester intermediate (cysteine-bound biotin) at or near the active site of biotinidase. In the next step, the biotinyl moiety is transferred from the thioester to the epsilon-amino group of lysine in histones. Biotinidase may catalyze both biotinylation and debiotinylation of histones	Homo sapiens	biotin + L-lysine	-	?
biocytin + H2O	i.e. biotin-epsilon-lysine	Homo sapiens	biotin + L-lysine	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)