| IED ID | IndEnz0010000062 |
| Enzyme Type ID | esterase000062 |
| Protein Name |
Carboxylesterase Culp1 EC 3.1.1.- CFP21 Cutinase-like protein 1 Culp1 |
| Gene Name | cut7 Rv1984c MTCY39.35 |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Enzyme Sequence | MTPRSLVRIVGVVVATTLALVSAPAGGRAAHADPCSDIAVVFARGTHQASGLGDVGEAFVDSLTSQVGGRSIGVYAVNYPASDDYRASASNGSDDASAHIQRTVASCPNTRIVLGGYSQGATVIDLSTSAMPPAVADHVAAVALFGEPSSGFSSMLWGGGSLPTIGPLYSSKTINLCAPDDPICTGGGNIMAHVSYVQSGMTSQAATFAANRLDHAG |
| Enzyme Length | 217 |
| Uniprot Accession Number | P9WP43 |
| Absorption | |
| Active Site | ACT_SITE 118; /note=Nucleophile; /evidence=ECO:0000305|PubMed:20103719; ACT_SITE 181; /evidence=ECO:0000305|PubMed:20103719; ACT_SITE 193; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:20103719 |
| Activity Regulation | ACTIVITY REGULATION: Almost completely inhibited by paraoxon (PubMed:19225166). Inhibited by tetrahydrolipstatin (THL), a specific lipase inhibitor (PubMed:20103719). {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748; Evidence={ECO:0000269|PubMed:16716602, ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719, ECO:0000269|PubMed:23843969};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59389; Evidence={ECO:0000269|PubMed:16716602, ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719, ECO:0000269|PubMed:23843969}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:16716602, ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:16716602, ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719}; CATALYTIC ACTIVITY: Reaction=H2O + pentanoate ester = an aliphatic alcohol + H(+) + pentanoate; Xref=Rhea:RHEA:48436, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31011, ChEBI:CHEBI:50871; Evidence={ECO:0000269|PubMed:20103719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48437; Evidence={ECO:0000269|PubMed:20103719}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000269|PubMed:20103719, ECO:0000269|PubMed:23843969};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47353; Evidence={ECO:0000269|PubMed:20103719, ECO:0000269|PubMed:23843969}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:20103719, ECO:0000269|PubMed:23843969};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47357; Evidence={ECO:0000269|PubMed:20103719, ECO:0000269|PubMed:23843969}; CATALYTIC ACTIVITY: Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658; Evidence={ECO:0000269|PubMed:20103719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47361; Evidence={ECO:0000269|PubMed:20103719}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:19225166};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47365; Evidence={ECO:0000269|PubMed:19225166}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:19225166};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47389; Evidence={ECO:0000269|PubMed:19225166}; CATALYTIC ACTIVITY: Reaction=H2O + octanoylglycerol = glycerol + H(+) + octanoate; Xref=Rhea:RHEA:48500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25646, ChEBI:CHEBI:88070; Evidence={ECO:0000269|PubMed:20103719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48501; Evidence={ECO:0000269|PubMed:20103719}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Shows esterase activity, with a preference for short- and medium-chain fatty acids (PubMed:19225166, PubMed:20103719, PubMed:16716602, PubMed:23843969). Has also weak lipase activity, but does not exhibit cutinase activity (PubMed:19225166, PubMed:23843969). Hydrolyzes various p-nitrophenol-linked aliphatic esters, including pNP-butyrate (C4), pNP-valerate (C5), pNP-hexanoate (C6), pNP-octanoate (C8) and pNP-decanoate (C10) (PubMed:19225166, PubMed:20103719, PubMed:16716602). Can use pNP-laurate (C12) and pNP-myristate (C14), with lower efficiency (PubMed:19225166). Can also hydrolyze monocaprylin and triolein, with a slow turnover (PubMed:20103719). {ECO:0000269|PubMed:16716602, ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719, ECO:0000269|PubMed:23843969}.; FUNCTION: Induces a strong delayed-type hypersensitivity (DTH) response in animal model of tuberculosis, cellular and humoral immune responses (PubMed:9673225, PubMed:10076913, PubMed:16716602). Induces interferon-gamma (IFN-gamma) release in animal models and in human TB patients (PubMed:9673225, PubMed:10076913, PubMed:16716602). Also induces IL-12 responses in mouse model (PubMed:16716602). {ECO:0000269|PubMed:10076913, ECO:0000269|PubMed:16716602, ECO:0000269|PubMed:9673225}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:20103719}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:20103719}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Mutagenesis (7); Signal peptide (1); Site (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:9673225}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000269|PubMed:9673225 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,782 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:59388; RHEA:59389; RHEA:47348; RHEA:47349; RHEA:48436; RHEA:48437; RHEA:47352; RHEA:47353; RHEA:47356; RHEA:47357; RHEA:47360; RHEA:47361; RHEA:47364; RHEA:47365; RHEA:47388; RHEA:47389; RHEA:48500; RHEA:48501 |
| Cross Reference Brenda |