Any feedback?
Literature summary for 3.4.11.1 extracted from
- Development of a working model of the active site in bovine lens leucine aminopeptidase: a density functional investigation (2002), ChemBioChem, 3, 101-104.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | active site bound, coordination is mainly due to steric effects not electrostatic and/or electronic interactions, bimetallic complex, modeling, Ala333 is involved, functional study | Bos taurus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low | reaction mechanism, active site structure, conformation models using crystal structure | Bos taurus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| lens | - |
Bos taurus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| b/LAP | - |
Bos taurus |
| bovine lens/leucine aminopeptidase | - |
Bos taurus |
| leucine aminopeptidase | - |
Bos taurus |
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)
Legal
Curated at
Member of
