Detail Information for IndEnz0002002102
IED ID IndEnz0002002102
Enzyme Type ID protease002102
Protein Name Leucine aminopeptidase 2-2
EC 3.4.11.-
Epoxide hydrolase
EC 3.3.2.10
Leukotriene A-4 hydrolase homolog 2
LTA-4 hydrolase 2
Gene Name PGUG_02354
Organism Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Meyerozyma Meyerozyma guilliermondii (Yeast) (Candida guilliermondii) Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii)
Enzyme Sequence MNVNELRSRAASQEQDPCTLSNYRGFEVVQSSLDLNVSFEKKNVSGTVTYELKNLKSTTEVVLDTSFLDIEQAFVDEKAVDFKLEARKEPFGSPLVIKLANVVEKLKISIKFATTENCSALQFIDKEATDSKVCDYLFSQCQAIHARSLFPCFDTPAVKSPYSFHVKSPSYTLMSGRPVECSEENTYRFEQPIPIPSYLVAIASGNLAGAPIGPRSTVYTEPPNLKACQWEFEKDMENFLVVAEDLIYKYEWLKYDALILPSSFPYGGMENPNITFATPTLISKDRSQVKVMAHELAHSWSGNLVTNCTWEHFWLNEGWTVYLERRILGGVASYEAKQRGEKDYVDAGEKVRHFAAILGWNDLVDTVKTIPSQYTRLVWDLKTVTPDDAFSKIPYEKGFSFLFYLETVLGGTDEFDPFMKHYFKKYRYKSLDSYQFIDTLYEFFEPKGKKDVLDSVDWNTWLYGEGVPPFTPKYDTRLADECYHLRDKWAAYEQNKGQFSASDIEHFEVNQHLLFLGTLTELFSNKKPAPEVYEELRKVYHQYSEASNCEIIASWNDLLLKSENFKPSDKIVQNFATWLGTVGRMKFARPGYKLLKDYVDKDLAIATFRKFESRYHPICKAMVRKDLGLDS
Enzyme Length 631
Uniprot Accession Number A5DGF3
Absorption
Active Site ACT_SITE 295; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 395; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation
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;Reference proteome;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 72,546
Kinetics
Metal Binding METAL 294; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 298; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 317; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Rhea ID RHEA:19037
Cross Reference Brenda