| IED ID | IndEnz0005000499 |
| Enzyme Type ID | lipase000499 |
| Protein Name |
Esterase EstD EC 3.1.1.1 |
| Gene Name | estD TM_0336 THEMA_03040 Tmari_0334 |
| Organism | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| Taxonomic Lineage | cellular organisms Bacteria Thermotogae Thermotogae Thermotogales Thermotogaceae Thermotoga Thermotoga maritima Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| Enzyme Sequence | MRLTVFLSLFLGVMVFGAFDQEAFLFVQHLTSENFESALNMCSNQVKAQLSVQSLSNIWNSLKAQLSDFREIAGYEKIIQAEYEIYNFTLKFDRGEISALVTMDREGKVAGLFFKQATKTEYELPDYVDPESFEEKDITVNGLPGKITIPKGSGPFPAVVLVHGSGPNDMDETIGPNKIFKDIAYGLSSKGIIVLRYHKRTFVEKVDPTTLTVEKEVIEDALEAVKILKERKDVSRVYVLGHSLGAMLTPEIAERSKADGVVMIAPPARPLEEVMEDQLKYLQSLGLASNVEETLNILEKLKRKEIPPDEFVLGAPAKYFYDLRERDPASIAKRLTIPMLLIFGGRDYQVTEKDQEIWLKELSGRENVKILVFDDLNHLMISGEGKSTPVEYMKKGHVDKRVIDEIARWMVK |
| Enzyme Length | 412 |
| Uniprot Accession Number | Q9WYH1 |
| Absorption | |
| Active Site | ACT_SITE 243; /note=Nucleophile; /evidence=ECO:0000305|PubMed:17466017; ACT_SITE 347; /note=Charge relay system; /evidence=ECO:0000305|PubMed:17466017; ACT_SITE 378; /note=Charge relay system; /evidence=ECO:0000305|PubMed:17466017 |
| Activity Regulation | ACTIVITY REGULATION: Is strongly inhibited by phenylmethylsulfonyl fluoride, a serine protease inhibitor, and by mercury chloride. Diethyl pyrocarbonate, a histidine modifier, also inhibits the reaction, albeit less pronounced than phenylmethylsulfonyl fluoride. EDTA and dithiothreitol have no effect on enzyme activity. {ECO:0000269|PubMed:17466017}. |
| 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:17466017}; |
| DNA Binding | |
| EC Number | 3.1.1.1 |
| Enzyme Function | FUNCTION: Exhibits significant esterase activity with a preference for short acyl chain esters (C4-C8) in vitro. Its physiological function is not known. Displays neither proteolytic activity using casein as substrate, nor peptidase activity when assayed with L-leucine p-nitroanilide and L-proline p-nitroanilide. {ECO:0000269|PubMed:17466017}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 95 degrees Celsius. Shows >70% of its maximal activity in the pH range of 5-9. Displays a relatively high thermostability with a half-life of 1 hour at 100 degrees Celsius. {ECO:0000269|PubMed:17466017}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:17466017}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Mutagenesis (3); Signal peptide (1) |
| Keywords | Hydrolase;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 46,550 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=148 uM for pNP-acetate (at pH 7 and 70 degrees Celsius) {ECO:0000269|PubMed:17466017}; KM=227 uM for pNP-butyrate (at pH 7 and 70 degrees Celsius) {ECO:0000269|PubMed:17466017}; KM=66 uM for pNP-valerate (at pH 7 and 70 degrees Celsius) {ECO:0000269|PubMed:17466017}; KM=11 uM for pNP-octanoate (at pH 7 and 70 degrees Celsius) {ECO:0000269|PubMed:17466017}; KM=72 uM for pNP-decanoate (at pH 7 and 70 degrees Celsius) {ECO:0000269|PubMed:17466017}; Note=kcat is 1.0 sec(-1) with pNP-acetate as substrate. kcat is 14.9 sec(-1) with pNP-butyrate as substrate. kcat is 10.2 sec(-1) with pNP-valerate as substrate. kcat is 1.6 sec(-1) with pNP-octanoate as substrate. kcat is 1.3 sec(-1) with pNP-decanoate as substrate (at pH 7 and 70 degrees Celsius). {ECO:0000269|PubMed:17466017}; |
| Metal Binding | |
| Rhea ID | RHEA:21164 |
| Cross Reference Brenda |