EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.5.1.12 | biocytin + H2O |
natural substrate, biotinidase is responsible for cleaving biocytin, thereby liberating and recycling biotin |
Homo sapiens |
biotin + L-lysine |
- |
? |
| 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 |
Homo sapiens |
biotin + L-lysine |
- |
? |
| 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 |
Homo sapiens |
biotin + L-lysine |
- |
? |
| 3.5.1.12 | biocytin + H2O |
i.e. biotin-epsilon-lysine |
Homo sapiens |
biotin + L-lysine |
- |
? |
| 3.5.1.12 | biocytin + H2O |
i.e. biotin-epsilon-lysine. Because polylysine is readily biotinylated by biotinidase in the presence of biocytin, whereas polyarginine is not biotinylated, the enzyme likely transfers biotin to the epsilon-amino group of lysyl residues |
Homo sapiens |
biotin + L-lysine |
- |
? |
| 3.5.1.12 | biocytin + H2O |
the enzyme belongs to the nitrilase superfamily |
Homo sapiens |
biotin + L-lysine |
- |
? |
| 3.5.1.12 | biotin amide + H2O |
- |
Cavia porcellus |
? |
- |
? |
| 3.5.1.12 | biotin amide + H2O |
- |
Homo sapiens |
? |
- |
? |
| 3.5.1.12 | biotin amide + H2O |
- |
Sus scrofa |
? |
- |
? |
| 3.5.1.12 | biotin amide + H2O |
- |
Oryctolagus cuniculus |
? |
- |
? |
