Detail Information for IndEnz0010000183
IED ID IndEnz0010000183
Enzyme Type ID esterase000183
Protein Name Acetyl esterase
EC 3.1.1.-
EcE
Gene Name aes ybaC b0476 JW0465
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MKPENKLPVLDLISAEMKTVVNTLQPDLPPWPATGTIAEQRQYYTLERRFWNAGAPEMATRAYMVPTKYGQVETRLFCPQPDSPATLFYLHGGGFILGNLDTHDRIMRLLASYSQCTVIGIDYTLSPEARFPQAIEEIVAACCYFHQQAEDYQINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKVAGVLLWYGLYGLRDSVTRRLLGGVWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTREVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQFFTAQL
Enzyme Length 319
Uniprot Accession Number P23872
Absorption
Active Site ACT_SITE 165; /evidence=ECO:0000305; ACT_SITE 262; /evidence=ECO:0000305; ACT_SITE 292; /evidence=ECO:0000305
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.1.-
Enzyme Function FUNCTION: Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity. {ECO:0000269|PubMed:11867639, ECO:0000269|PubMed:12374803, ECO:0000269|PubMed:9576853}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:9576853};
Pathway
nucleotide Binding
Features Active site (3); Beta strand (10); Chain (1); Frameshift (1); Helix (14); Motif (1); Mutagenesis (9); Sequence conflict (2); Turn (6)
Keywords 3D-structure;Cytoplasm;Direct protein sequencing;Hydrolase;Reference proteome;Serine esterase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9576853}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 4KRX; 4KRY;
Mapped Pubmed ID 12878309; 16606699; 23934774;
Motif MOTIF 91..93; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3
Gene Encoded By
Mass 36,034
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for p-nitrophenylacetate (at pH 7.1 and 25 degrees Celsius) {ECO:0000269|PubMed:9576853}; KM=0.7 mM for p-nitrophenylpropionate (at pH 7.1 and 25 degrees Celsius) {ECO:0000269|PubMed:9576853}; KM=0.5 mM for p-nitrophenylbutyrate (at pH 7.1 and 25 degrees Celsius) {ECO:0000269|PubMed:9576853}; KM=0.26 mM for p-nitrophenylvalerate (at pH 7.1 and 25 degrees Celsius) {ECO:0000269|PubMed:9576853}; KM=0.22 mM for p-nitrophenylhexanoate (at pH 7.1 and 25 degrees Celsius) {ECO:0000269|PubMed:9576853}; KM=0.16 mM for p-nitrophenyloctanoate (at pH 7.1 and 25 degrees Celsius) {ECO:0000269|PubMed:9576853}; Vmax=34.2 umol/min/mg enzyme toward p-nitrophenylbutyrate (at pH 5.6 and 30 degrees Celsius) {ECO:0000269|PubMed:9576853}; Vmax=3.67 umol/min/mg enzyme toward tributyrylglycerol (at pH 5.6 and 30 degrees Celsius) {ECO:0000269|PubMed:9576853}; Vmax=0.22 umol/min/mg enzyme toward trioleylglycerol (at pH 5.6 and 30 degrees Celsius) {ECO:0000269|PubMed:9576853};
Metal Binding
Rhea ID
Cross Reference Brenda 3.1.1.6;