| IED ID | IndEnz0005001149 |
| Enzyme Type ID | lipase001149 |
| Protein Name |
Esterase EstP EC 3.1.1.1 Autotransporter esterase EstP Palmitoyl-CoA hydrolase EC 3.1.2.2 |
| Gene Name | estP PP_0418 |
| Organism | Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas putida group Pseudomonas putida (Arthrobacter siderocapsulatus) Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) |
| Enzyme Sequence | MRKAPLLRFTLASLALACSQALAGPSPYSTLIVFGDSLADAGQFPDLVGGTPGARFTNRDADGNFAPVSPMILGGRLGVAPGDLNPSTSVGIQPDGNNWAVGGYTTQQILDSITTTSETVIPPGNPNAGLVLRERPGYLANGLRADPNALYYLTGGGNDFLQGLVNSPADAVAAGARLAASAQALQQGGARYIMVWLLPDLGQTPNFSGTPQQNPLSLLSAAFNQSLISQLGQIDAQIIPLNIPLLLSEALASPSQFGLASDQNLVGTCYSGDSCVENPVYGINGTTPDPTKLLFNDSVHPTIAGQQLIADYAYSILAAPWELTLLPEMAHASLRAHQDELRNQWQTPWQAVGQWQAFVASGAQDLDFDGQHSAASGDGRGYNLTVGGSYRLNDAWRLGLAGGANRQKLEAGEQDSDYKLNSYMASAFAQYRQDRWWADAALTAGHLDYSDLKRTFALGVNDRSEKGDTDGEAWAMSGRLGYNLAADTSNWQLAPFISADYARVKVDGYDEKSGRSTALGFDDQERTSRRLGVGLLGSVQVLPSTRLFAEVAQEHEFEDDEQDVTMHLTSLPANDFTLTGYTPHSDLTRASLGVSHELVAGVHLRGNYNWRKSDELTQQGISVGVSVDF |
| Enzyme Length | 629 |
| Uniprot Accession Number | Q88QS0 |
| Absorption | |
| Active Site | ACT_SITE 37; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 297; /evidence=ECO:0000250; ACT_SITE 300; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:20931591}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:20931591}; |
| DNA Binding | |
| EC Number | 3.1.1.1; 3.1.2.2 |
| Enzyme Function | FUNCTION: Esterase that catalyzes the hydrolysis of p-nitrophenyl esters of acyl chain lengths C4-C10 and Tween detergents. Has also a pronounced thioesterase activity towards palmitoyl-coenzyme A. {ECO:0000269|PubMed:20931591}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Signal peptide (1); Topological domain (11); Transmembrane (11) |
| Keywords | Cell outer membrane;Hydrolase;Membrane;Reference proteome;Serine esterase;Signal;Transmembrane;Transmembrane beta strand |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 67,176 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:20931591}; Vmax=85 umol/min/mg enzyme with p-nitrophenyl butyrate as substrate {ECO:0000269|PubMed:20931591}; Note=The N-terminal esterase domain, when expressed alone, shows activities five to ten times higher than those of the complete enzyme EstP towards all tested substrates, whereas substrate affinity and the activity profiles are still the same.; |
| Metal Binding | |
| Rhea ID | RHEA:21164; RHEA:16645 |
| Cross Reference Brenda |