IED ID | IndEnz0002002223 |
Enzyme Type ID | protease002223 |
Protein Name |
Leucine aminopeptidase 2 EC 3.4.11.- Epoxide hydrolase EC 3.3.2.10 Leukotriene A-4 hydrolase homolog LTA-4 hydrolase |
Gene Name | SCY_4744 |
Organism | Saccharomyces cerevisiae (strain YJM789) (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 YJM789) (Baker's yeast) |
Enzyme Sequence | MFLLPFVIRHSSSIYLPTLRFRGLLTVISRNIHISTPHKMLPLSIEQRRPSRSPEYDQSTLSNYKDFAVLHTDLNLSVSFEKSAISGSVTFQLKKLHEGKNKSDELHLDTSYLDVQEVHIDGSKADFQIEQRKEPLGSRLVINNASCNDNFTLNIQFRTTDKCTALQWLNSKQTKGGKPYVFSQLEAIHARSLFPCFDTPSVKSTFTASIESPLPVVFSGIRIEDTSKDTNIYRFEQKVPIPAYLIGIASGDLSSAPIGPRSTVYTEPFRLKDCQWEFENDVEKFIQTAEKIIFEYEWGTYDILVNVDSYPYGGMESPNMTFATPTLIAHDRSNIDVIAHELAHSWSGNLVTNCSWNHFWLNEGWTVYLERRIIGAIHGEPTRHFSALIGWSDLQNSIDSMKDPERFSTLVQNLNDNTDPDDAFSTVPYEKGFNLLFHLETILGGKAEFDPFIRHYFKKFAKKSLDTFQFLDTLYEFYPEKKEILDSVDWETWLYKPGMPPRPHFITALADNVYQLADKWVEMAQHLKTTEDFRSEFNAIDIKDFNSNQLVLFLETLTQNGHSNKKPKDFDWAKFPVASRALLDIYQDNIVKSQNAEVVFKMFKFQIFAKLQEEYKHLADWLGTVGRMKFVRPGYRLLNSVDRRLALATFDKFKDTYHPICKALVKQDLGL |
Enzyme Length | 671 |
Uniprot Accession Number | A6ZS33 |
Absorption | |
Active Site | ACT_SITE 341; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 429; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
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:0000250|UniProtKB:Q10740}. |
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:0000250|UniProtKB:Q10740}; |
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:0000250|UniProtKB:Q10740}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Metal binding (3); Region (2) |
Keywords | Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10740}. Nucleus {ECO:0000250|UniProtKB:Q10740}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 77,353 |
Kinetics | |
Metal Binding | METAL 340; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 344; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 363; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | RHEA:19037 |
Cross Reference Brenda |