| IED ID | IndEnz0002002229 |
| Enzyme Type ID | protease002229 |
| Protein Name |
Leucine aminopeptidase 2 EC 3.4.11.- Epoxide hydrolase EC 3.3.2.10 Leucyl aminopeptidase yscIV AP IV Leukotriene A-4 hydrolase homolog LTA-4 hydrolase |
| Gene Name | LAP2 YNL045W N2535 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MFLLPFVIRHSSSIYLPTLRFRGLLTVISRNIHISTPHKMLPLSIEQRRPSRSPEYDQSTLSNYKDFAVLHTDLNLSVSFEKSAISGSVTFQLKKLHEGKNKSDELHLDTSYLDVQEVHIDGSKADFQIEQRKEPLGSRLVINNASCNDNFTLNIQFRTTDKCTALQWLNSKQTKGGKPYVFSQLEAIHARSLFPCFDTPSVKSTFTASIESPLPVVFSGIRIEDTSKDTNIYRFEQKVPIPAYLIGIASGDLSSAPIGPRSTVYTEPFRLKDCQWEFENDVEKFIQTAEKIIFEYEWGTYDILVNVDSYPYGGMESPNMTFATPTLIAHDRSNIDVIAHELAHSWSGNLVTNCSWNHFWLNEGWTVYLERRIIGAIHGEPTRHFSALIGWSDLQNSIDSMKDPERFSTLVQNLNDNTDPDDAFSTVPYEKGFNLLFHLETILGGKAEFDPFIRHYFKKFAKKSLDTFQFLDTLYEFYPEKKEILDSVDWETWLYKPGMPPRPHFITALADNVYQLADKWVEMAQHLKTTEDFRSEFNAIDIKDFNSNQLVLFLETLTQNGHSNKKPKDFDWAKFPVASRALLDIYQDNIVKSQNAEVVFKMFKFQIFAKLQEEYKHLADWLGTVGRMKFVRPGYRLLNSVDRRLALATFDKFKDTYHPICKALVKQDLGL |
| Enzyme Length | 671 |
| Uniprot Accession Number | Q10740 |
| Absorption | |
| Active Site | ACT_SITE 341; /note=Proton acceptor; ACT_SITE 429; /note=Proton donor |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 3-(4-benzyloxyphenyl)-2-(R)-amino-1-propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4-benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The aminopeptidase activity is stimulated by LTA(4). {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:16024909}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037, ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594; EC=3.3.2.10; Evidence={ECO:0000269|PubMed:21146536}; |
| DNA Binding | |
| EC Number | 3.4.11.-; 3.3.2.10 |
| Enzyme Function | FUNCTION: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro). {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16024909, ECO:0000269|PubMed:16597475, ECO:0000269|PubMed:21146536, ECO:0000269|PubMed:6352682}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 7.3. {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (29); Chain (1); Helix (33); Metal binding (3); Mutagenesis (9); Region (2); Turn (9) |
| Keywords | 3D-structure;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 2XPY; 2XPZ; 2XQ0; |
| Mapped Pubmed ID | 10341423; 11283351; 11805826; 12140549; 14558145; 16429126; 16554755; 16606443; 16652171; 16884526; 18467557; 19185714; 19536198; 20624488; 21936842; |
| Motif | |
| Gene Encoded By | |
| Mass | 77,353 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for Leu-p-nitroanilide {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; KM=1.8 mM for Met-p-nitroanilide {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; KM=2.0 mM for Ala-p-nitroanilide {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; Vmax=520 nmol/min/mg enzyme with Leu-p-nitroanilide as substrate {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; Vmax=360 nmol/min/mg enzyme with Met-p-nitroanilide as substrate {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; Vmax=170 nmol/min/mg enzyme with Ala-p-nitroanilide as substrate {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475}; |
| Metal Binding | METAL 340; /note=Zinc; catalytic; METAL 344; /note=Zinc; catalytic; METAL 363; /note=Zinc; catalytic |
| Rhea ID | RHEA:19037 |
| Cross Reference Brenda |