| IED ID | IndEnz0005000356 |
| Enzyme Type ID | lipase000356 |
| Protein Name |
Carboxylesterase EC 3.1.1.1 |
| Gene Name | |
| Organism | Thermobifida fusca (Thermomonospora fusca) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptosporangiales Nocardiopsaceae Thermobifida Thermobifida fusca (Thermomonospora fusca) |
| Enzyme Sequence | MEIVIRTGSGDVRGSKENGIAVFRGIPYAEPPVGAHRFTAPRPPRPWDGVRDATEFSATAPRPPYPEAIGALLIERFIPGDDYLTLNVWTPDPNAVGLPVMVWIHGGAFTNGSGSEPVYDGAAFARDGVVFVSFNYRLGIIGFADLPDAPSNRGLLDQIAALEWVRDNIARFGGDPGNVTVFGESAGAMSVCTLMATPRARGLFRRAILQSGAGNMAVAAEDATTIAAVIAHRLGVEPTAAALAHVPVAQLLDVQQQVAQEIQGAPDPAVWGERIAGGSVLLPFAPVIDGELLSQRPAEAIAGGAGHDVDLLFGTTTDEYRLFLAPTGLLPFITSDYVTAHLAKSGLDADAAKAYTAEGRGEEPGDILASIITDQVFRIPALRIAESRVDAPARTFGYEFAWRTPQLDGILGACHAVELPFVFRTLDRAASLVGTNPPEELAETVHNAWVRFATSGDPGWPAWNPETRSVMRFDHPVSEMVTDPYPATRALWDGVPL |
| Enzyme Length | 497 |
| Uniprot Accession Number | P86325 |
| Absorption | |
| Active Site | ACT_SITE 185; /note="Acyl-ester intermediate"; /evidence="ECO:0000250|UniProtKB:P21836, ECO:0000255|PROSITE-ProRule:PRU10039"; ACT_SITE 319; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P21836"; ACT_SITE 415; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:P37967" |
| 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:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|Ref.1}; |
| DNA Binding | |
| EC Number | 3.1.1.1 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius with cyclic PET trimers as substrate. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 with cyclic PET trimers as substrate (at 60 degrees Celsius). {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Direct protein sequencing;Hydrolase;Secreted;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,941 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.272 mM for p-nitrophenol acetate {ECO:0000269|Ref.1}; KM=0.164 mM for p-nitrophenol butyrate {ECO:0000269|Ref.1}; KM=0.198 mM for p-nitrophenol caprylate {ECO:0000269|Ref.1}; KM=0.468 mM for cyclic PET trimers {ECO:0000269|Ref.1}; Vmax=46 umol/min/mg enzyme with p-nitrophenol acetate as substrate {ECO:0000269|Ref.1}; Vmax=88 umol/min/mg enzyme with p-nitrophenol butyrate as substrate {ECO:0000269|Ref.1}; Vmax=64 umol/min/mg enzyme with p-nitrophenol caprylate as substrate {ECO:0000269|Ref.1}; Vmax=9.3 umol/min/mg enzyme with cyclic PET trimers as substrate {ECO:0000269|Ref.1}; |
| Metal Binding | |
| Rhea ID | RHEA:21164 |
| Cross Reference Brenda |