Detail Information for IndEnz0005000364
IED ID IndEnz0005000364
Enzyme Type ID lipase000364
Protein Name Isoamyl acetate-hydrolyzing esterase
EC 3.1.1.112
Gene Name IAH1 EST2 YOR126C O3287 YOR3287C
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 MDYEKFLLFGDSITEFAFNTRPIEDGKDQYALGAALVNEYTRKMDILQRGFKGYTSRWALKILPEILKHESNIVMATIFLGANDACSAGPQSVPLPEFIDNIRQMVSLMKSYHIRPIIIGPGLVDREKWEKEKSEEIALGYFRTNENFAIYSDALAKLANEEKVPFVALNKAFQQEGGDAWQQLLTDGLHFSGKGYKIFHDELLKVIETFYPQYHPKNMQYKLKDWRDVLDDGSNIMS
Enzyme Length 238
Uniprot Accession Number P41734
Absorption
Active Site ACT_SITE 12; /note=Nucleophile; /evidence=ECO:0000305|PubMed:21069734; ACT_SITE 187; /note=Proton donor; /evidence=ECO:0000305|PubMed:21069734; ACT_SITE 190; /note=Proton acceptor; /evidence=ECO:0000305|PubMed:21069734
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=3-methylbutyl acetate + H2O = 3-methylbutanol + acetate + H(+); Xref=Rhea:RHEA:60436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15837, ChEBI:CHEBI:30089, ChEBI:CHEBI:31725; EC=3.1.1.112; Evidence={ECO:0000269|PubMed:10855721, ECO:0000269|PubMed:21069734, ECO:0000269|Ref.2};
DNA Binding
EC Number 3.1.1.112
Enzyme Function FUNCTION: Plays a crucial role in the hydrolysis of isoamyl acetate in sake mash (Ref.2). Hydrolyzes short chain esters from acetate (C2) to hexanoate (C6), showing more specificity for shorter chain exters. No activity for decanoate (C10) esters (PubMed:21069734). {ECO:0000269|PubMed:21069734, ECO:0000269|Ref.2}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:10855721};
Pathway
nucleotide Binding
Features Active site (3); Beta strand (6); Chain (1); Helix (13); Mutagenesis (1); Site (2); Turn (4)
Keywords 3D-structure;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3MIL;
Mapped Pubmed ID 16002012; 22940803; 24384752;
Motif
Gene Encoded By
Mass 27,346
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40.3 mM for 3-mehtylbutyl acetate {ECO:0000269|PubMed:10855721};
Metal Binding
Rhea ID RHEA:60436
Cross Reference Brenda 3.1.1.112;