LMPD Database

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LMP007272

UniProt Annotations

Entry Information
Gene NameLap2p
Protein EntryLKHA4_YEAST
UniProt IDQ10740
SpeciesYeast (S288c)
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic 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}; pH dependence: Optimum pH is about 7.3. {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475};
Catalytic Activity(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa- 7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12- dihydroxyicosa-6,8,10,14-tetraenoate. {ECO:0000269|PubMed:21146536}.
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21146536}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21146536};
Enzyme RegulationInhibited 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}.
FunctionAminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA(4) to form LTB(4) (in vitro). {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16024909, ECO:0000269|PubMed:16597475, ECO:0000269|PubMed:21146536}.
MiscellaneousPresent with 5590 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
PathwayLipid metabolism; leukotriene B4 biosynthesis.
SimilarityBelongs to the peptidase M1 family. {ECO:0000305}.
Subcellular LocationCytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.