The enzyme catalyzes the hydrolysis of a wide range of N-terminal amino acid residues from proteins and polypeptides. It is a monomer which uses a dinuclear zinc-binding site to perform the catalysis (PMID12176384).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 901 A | ZN | zinc | zinc | dinuclear | Increases nucleophilicity Coordinates substrate Increases acidity Increases electrophilicity |
| ZN 902 A | ZN | zinc | zinc | dinuclear | Coordinates substrate Increases acidity Electrostatic stabiliser Increases nucleophilicity |
*It refers to the MACiE reference pdb: 1lok
| Metal/s Properties in Resting State | ||||||
| ZN 901 A | Resting state enzyme (1rtq) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | trigonalBipyramidal | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| ZN 902 A | Resting state enzyme (1rtq) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 5 | |||||
| Notes | - | |||||
| References |
| -Desmarais W, Bienvenue DL, Bzymek KP, Petsko GA, Ringe D, Holz RC The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica. J Biol Inorg Chem. 2006 Jun;11(4):398-408. Epub 2006 Apr 5.(MEDLINE:16596389) |
| -Stamper C, Bennett B, Edwards T, Holz RC, Ringe D, Petsko G Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis. Biochemistry. 2001 Jun 19;40(24):7035-46.(MEDLINE:11401547) |
| - Some information have been also deduced from the MACiE mechanism model |