| IED ID | IndEnz0005001215 |
| Enzyme Type ID | lipase001215 |
| 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; |