Detail Information for IndEnz0002002229
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