EC Number   |
Natural Substrates |
|---|
   3.5.1.12 | biocytin + H2O |
natural substrate, biotinidase is responsible for cleaving biocytin, thereby liberating and recycling biotin |
| 3.5.1.12 | biocytin + H2O |
biotinylation of histones by biotinidase depends on the hydrolytic cleavage of biocytin (biotinyl-epsilon-lysine), coupled to the transfer of biotinyl residue to free amino groups in histones. K4, K9 and K18 in histone H3 are good targets for biotinylation, K14 and K23 are relatively poor targets |
| 3.5.1.12 | 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 |
| 3.5.1.12 | biotin amide + H2O |
- |
| 3.5.1.12 | biotin amide + H2O |
very short biotinyl peptides, enzyme is not active when biotin is attached to large native proteins, for example intact holocarboxylases |
| 3.5.1.12 | biotin amide + H2O |
cleaves D-biotinylamides and esters, recycling of the vitamin |
| 3.5.1.12 | biotin amide + H2O |
soluble bound biotin |
| 3.5.1.12 | epsilon-N-(D,L-lipoyl)-L-lysine + H2O |
- |
| 3.5.1.12 | epsilon-N-biotinyl-L-lysine + H2O |
- |
| 3.5.1.12 | epsilon-N-biotinyl-L-lysine + H2O |
biocytin, soluble bound biotin |
