| IED ID | IndEnz0005000372 |
| Enzyme Type ID | lipase000372 |
| Protein Name |
Carboxylesterase/lipase Culp6 EC 3.1.1.- Cell wall lipase Cutinase-like protein 6 Culp6 |
| Gene Name | cut6 Rv3802c |
| 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 | MAKNSRRKRHRILAWIAAGAMASVVALVIVAVVIMLRGAESPPSAVPPGVLPPGPTPAHPHKPRPAFQDASCPDVQMISVPGTWESSPQQNPLNPVQFPKALLLKVTGPIAQQFAPARVQTYTVAYTAQFHNPLTTDNQMSYNDSRAEGTRAMVAAMTDMNNRCPLTSYVLIGFSQGAVIAGDVASDIGNGRGPVDEDLVLGVTLIADGRRQQGVGNQVPPSPRGEGAEITLHEVPVLSGLGLTMTGPRPGGFGALDGRTNEICAQGDLICAAPAQAFSPANLPTTLNTLAGGAGQPVHAMYATPEFWNSDGEPATEWTLNWAHQLIENAPHPKHR |
| Enzyme Length | 336 |
| Uniprot Accession Number | O53581 |
| Absorption | |
| Active Site | ACT_SITE 175; /evidence="ECO:0000305|PubMed:19225166, ECO:0000305|PubMed:29247008"; ACT_SITE 268; /evidence="ECO:0000305|PubMed:19225166, ECO:0000305|PubMed:29247008"; ACT_SITE 299; /evidence="ECO:0000305|PubMed:19225166, ECO:0000305|PubMed:29247008" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by tetrahydrolipstatin (THL), a specific lipase inhibitor, and by derivatives of THL (PubMed:19169353, PubMed:20656688, PubMed:21384024). Inhibited by high concentrations of paraoxon (PubMed:19225166). Also inhibited by a Furan-based urea derivative, 1-(3,5-difluorophenyl)-3-(furan-2-ylmethyl)urea (PubMed:31741730). {ECO:0000269|PubMed:19169353, ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688, ECO:0000269|PubMed:21384024, ECO:0000269|PubMed:31741730}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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 + hexadecanoate ester = an aliphatic alcohol + H(+) + hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:19225166};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393; Evidence={ECO:0000269|PubMed:19225166}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoate ester = an aliphatic alcohol + H(+) + octadecanoate; Xref=Rhea:RHEA:47396, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75925; Evidence={ECO:0000269|PubMed:19225166};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47397; Evidence={ECO:0000269|PubMed:19225166}; 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:19225166, ECO:0000269|PubMed:20656688};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H(+); Xref=Rhea:RHEA:47328, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905; Evidence={ECO:0000269|PubMed:19169353};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47329; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:19169353};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-acyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40651, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:58168, ChEBI:CHEBI:75063; Evidence={ECO:0000269|PubMed:19169353};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40652; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000269|PubMed:19169353};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000269|PubMed:19169353}; 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; Evidence={ECO:0000269|PubMed:19169353};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000269|PubMed:19169353}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:19169353};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000269|PubMed:19169353}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Shows esterase and phospholipase A activities (PubMed:19169353, PubMed:19225166, PubMed:20656688, PubMed:29247008). May be involved in cell wall biosynthesis and/or maintenance (PubMed:19169353, PubMed:19225166, PubMed:20656688). Can hydrolyze various substrates, including pNP-laurate (C12), pNP-myristate (C14), pNP-palmitate (C16), pNP-stearate (C18), pNP-butyrate (C4), phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, 4-methylumbelliferyl heptanoate and palmitic acid and arachidonic acid containing phospholipids (PubMed:19169353, PubMed:19225166, PubMed:20656688). Does not exhibit cutinase activity (PubMed:19225166). {ECO:0000269|PubMed:19169353, ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20656688, ECO:0000269|PubMed:29247008}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is above 7.0 for lipase activity. {ECO:0000269|PubMed:19225166}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (8); Chain (1); Compositional bias (1); Disulfide bond (2); Helix (10); Mutagenesis (5); Region (1); Transmembrane (1); Turn (6) |
| Keywords | 3D-structure;Cell membrane;Cell wall;Disulfide bond;Hydrolase;Membrane;Reference proteome;Secreted;Serine esterase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:19225166}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5W95; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,448 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.52 mM for nitrophenyl butyrate {ECO:0000269|PubMed:19169353}; KM=0.017 mM for palmitoyl-S-CoA {ECO:0000269|PubMed:19169353}; KM=2.28 mM for decanoyl-S-CoA {ECO:0000269|PubMed:19169353}; KM=4.52 mM for pNP-butyrate {ECO:0000269|PubMed:20656688}; KM=19.88 uM for 4-methylumbelliferyl heptanoate {ECO:0000269|PubMed:29247008}; Vmax=1.62 mol/min/mg enzyme with nitrophenyl butyrate as substrate {ECO:0000269|PubMed:19169353}; Vmax=1.35 mol/min/mg enzyme with palmitoyl-S-CoA as substrate {ECO:0000269|PubMed:19169353}; Vmax=1.11 mol/min/mg enzyme with decanoyl-S-CoA as substrate {ECO:0000269|PubMed:19169353}; Vmax=241 nmol/min/mg enzyme with pNP-butyrate as substrate {ECO:0000269|PubMed:20656688}; Note=kcat is 0.00881 sec(-1) with nitrophenyl butyrate as substrate. kcat is 0.0733 sec(-1) with palmitoyl-S-CoA as substrate. kcat is 0.0845 sec(-1) with decanoyl-S-CoA as substrate (PubMed:19169353). kcat is 0.143 sec(-1) with pNP-butyrate as substrate (PubMed:20656688). kcat is 10.05 min(-1) with 4-methylumbelliferyl heptanoate as substrate (PubMed:29247008). {ECO:0000269|PubMed:19169353, ECO:0000269|PubMed:20656688, ECO:0000269|PubMed:29247008}; |
| Metal Binding | |
| Rhea ID | RHEA:47364; RHEA:47365; RHEA:47388; RHEA:47389; RHEA:47392; RHEA:47393; RHEA:47396; RHEA:47397; RHEA:47348; RHEA:47349; RHEA:47328; RHEA:47329; RHEA:41223; RHEA:41224; RHEA:40651; RHEA:40652; RHEA:40431; RHEA:40432; RHEA:16645; RHEA:16646; RHEA:40059; RHEA:40060 |
| Cross Reference Brenda |