| IED ID | IndEnz0005000416 |
| Enzyme Type ID | lipase000416 |
| Protein Name |
Arylesterase A-esterase EC 3.1.1.2 Paraoxonase EC 3.1.8.1 |
| Gene Name | are |
| Organism | Saccharolobus solfataricus (Sulfolobus solfataricus) |
| Taxonomic Lineage | cellular organisms Archaea TACK group Crenarchaeota Thermoprotei Sulfolobales Sulfolobaceae Saccharolobus Saccharolobus solfataricus (Sulfolobus solfataricus) |
| Enzyme Sequence | MPLDPEVRNFLQVYYKANIIDFTKYQFQEIRQKVNELLAKAVPKDPVGETRDMKIKLEDYELPIRIYSPIKRTNNGLVMHFHGGAWILGSIETEDAISRILSNSCECTVISVDYRLAPEYKFPTAVYDCFNAIVWARDNAGELGIDKDKIATFGISAGGNLVAATSLLARDNKLKLTAQVPVVPFVYLDLASKSMNRYRKGYFLDINLPVDYGVKMYIRDEKDLYNPLFSPLIAEDLSNLPQAIVVTAEYDPLRDQGEAYAYRLMESGVPTLSFRVNGNVHAFLGSPRTSRQVTVMIGALLKDIFK |
| Enzyme Length | 306 |
| Uniprot Accession Number | B5BLW5 |
| Absorption | |
| Active Site | ACT_SITE 156; /evidence=ECO:0000305|PubMed:18931117; ACT_SITE 251; /evidence=ECO:0000305|PubMed:18931117; ACT_SITE 281; /evidence=ECO:0000305|PubMed:18931117 |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by chemical modifiers that are specific to Cys (HgCl(2) and p-chloromercuribenzoic acid), His (diethyl pyrocarbonate) and Ser (diisopropyl fluorophosphate and phenylmethanesulfonyl fluoride). No significant effect with chemical modifiers specific to Lys (pyridoxal 5'-phosphate) and Arg (phenylglyoxal). Not inhibited by inhibitors of A-esterases (paraoxon) or C-esterases (physostigmine/eserine). Activity is also not effected by incubation with 5 mM divalent cations for 30 minutes at 30 degrees Celsius or with 10 mM EDTA for 60 minutes at 75 degrees Celsius. {ECO:0000269|PubMed:18931117}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence={ECO:0000269|PubMed:18931117}; CATALYTIC ACTIVITY: Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:18931117}; |
| DNA Binding | |
| EC Number | 3.1.1.2; 3.1.8.1 |
| Enzyme Function | FUNCTION: Has a broad substrate specificity. Hydrolyzes various p-nitrophenyl phosphates, aromatic esters and p-nitrophenyl fatty acids in vitro. Most active against paraoxon, phenyl acetate and p-nitrophenyl caproate (C6), respectively. Has also tributyrinase activity, but shows no hydrolytic activity toward other triacylglycerols including tricaprylin, trimyristin, tripalmitin or triolein in vitro. {ECO:0000269|PubMed:18931117}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 94 degrees Celsius. Very thermostable, but rapidly inactivated above 94 degrees Celsius. Most of the activity is retained for 5 days at 50 degrees Celsius, and approximately 70% of the activity is retained after 5 days at 70 degrees Celsius. 52% of the activity is still retained after 50 hours at 90 degrees Celsius, but completely inactivated after 5 days at 90 degrees Celsius. {ECO:0000269|PubMed:18931117}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:18931117}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (10); Chain (1); Helix (13); Motif (1); Mutagenesis (6); Turn (5) |
| Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5L2P; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 82..84; /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 | 34,552 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for phenyl acetate (PA) {ECO:0000269|PubMed:18931117}; KM=29 uM for alpha-naphthyl acetate (alpha-NA) {ECO:0000269|PubMed:18931117}; KM=224 uM for p-nitrophenyl butyrate (C4) {ECO:0000269|PubMed:18931117}; KM=31 uM for p-nitrophenyl caproate (C6) {ECO:0000269|PubMed:18931117}; KM=28 uM for p-nitrophenyl caprylate (C8) {ECO:0000269|PubMed:18931117}; KM=81 uM for p-nitrophenyl caprate (C10) {ECO:0000269|PubMed:18931117}; KM=122 uM for p-nitrophenyl laurate (C12) {ECO:0000269|PubMed:18931117}; KM=276 uM for p-nitrophenyl palmitate (C16) {ECO:0000269|PubMed:18931117}; KM=234 uM for p-nitrophenyl phosphate {ECO:0000269|PubMed:18931117}; KM=5 uM for paraoxon {ECO:0000269|PubMed:18931117}; KM=246 uM for methyl paraoxon {ECO:0000269|PubMed:18931117}; Note=kcat is 521 sec(-1) with PA as substrate. kcat is 450 sec(-1) with alpha-NA as substrate. kcat is 285 sec(-1) with p-nitrophenyl butyrate (C4) as substrate. kcat is 467 sec(-1) with p-nitrophenyl caproate (C6) as substrate. kcat is 410 sec(-1) with p-nitrophenyl caprylate (C8) as substrate. kcat is 341 sec(-1) with p-nitrophenyl caprate (C10) as substrate. kcat is 264 sec(-1) with p-nitrophenyl laurate (C12) as substrate. kcat is 265 sec(-1) with p-nitrophenyl palmitate (C16) as substrate. kcat is 269 sec(-1) with p-nitrophenyl phosphate as substrate. kcat is 597 sec(-1) with paraoxon as substrate. kcat is 342 sec(-1) with methyl paraoxon as substrate. {ECO:0000269|PubMed:18931117}; |
| Metal Binding | |
| Rhea ID | RHEA:17309 |
| Cross Reference Brenda | 3.1.1.2;3.1.8.1; |