| IED ID | IndEnz0010000530 |
| Enzyme Type ID | esterase000530 |
| Protein Name |
Carboxylesterase/phospholipase LipF EC 3.1.1.1 EC 3.1.4.3 |
| Gene Name | lipF Rv3487c |
| 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 | MSSYYARRPLQSSGCSNSDSCWDGAPIEITESGPSVAGRLAALASRMTIKPLMTVGSYLSPLPLPLGFVDFACRVWRPGQGTVRTTINLPNATAQLVRAPGVRAADGAGRVVLYLHGGAFVMCGPNSHSRIVNALSGFAESPVLIVDYRLIPKHSLGMALDDCHDAYQWLRARGYRPEQIVLAGDSAGGYLALALAQRLQCDDEKPAAIVAISPLLQLAKGPKQDHPNIGTDAMFPARAFDALAAWVRAAAAKNMVDGRPEDLYEPLDHIESSLPPTLIHVSGSEVLLHDAQLGAGKLAAAGVCAEVRVWPGQAHLFQLATPLVPEATRSLRQIGQFIRDATADSSLSPVHRSRYVAGSPRAASRGAFGQSPI |
| Enzyme Length | 373 |
| Uniprot Accession Number | O06350 |
| Absorption | |
| Active Site | ACT_SITE 186; /evidence=ECO:0000305|PubMed:15939293; ACT_SITE 285; /evidence=ECO:0000305|PubMed:15939293; ACT_SITE 315; /evidence=ECO:0000305|PubMed:15939293 |
| 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:0000269|PubMed:15939293}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3; Evidence={ECO:0000269|PubMed:18535356};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605; Evidence={ECO:0000269|PubMed:18535356}; |
| DNA Binding | |
| EC Number | 3.1.1.1; 3.1.4.3 |
| Enzyme Function | FUNCTION: Hydrolyzes short-chain esters. Shows maximal activity with triacetin and p-nitrophenyl acetate. Has no enzyme activity on triacylglycerides or p-nitrophenyl esters (p-NP) with long fatty acids (tricaprin, p-NP caprylate, or p-NP caprate); experiments performed with enzyme missing the first 97 residues (PubMed:15939293). Has phospholipase C activity, making 1,2-DAG phosphocholine; experiments performed with enzyme missing the first 97 residues (PubMed:18535356). {ECO:0000269|PubMed:15939293, ECO:0000269|PubMed:18535356}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:15939293}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:15939293}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Erroneous initiation (1); Motif (1); Mutagenesis (3); Propeptide (1) |
| Keywords | Cell wall;Direct protein sequencing;Hydrolase;Reference proteome;Secreted;Serine esterase;Stress response |
| Interact With | |
| Induction | INDUCTION: Induced by acidic pH. {ECO:0000269|PubMed:15939293}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305|PubMed:18535356}. Note=Detected by antibodies in a wild-type strain and upon expression of a probably truncated form in M.smegmatis. {ECO:0000269|PubMed:18535356}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 116..118; /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 | 39,611 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for triacetin {ECO:0000269|PubMed:15939293}; KM=0.24 mM for tributyrin {ECO:0000269|PubMed:15939293}; KM=0.25 mM for tricaproin {ECO:0000269|PubMed:15939293}; KM=1.46 mM for tricaprylin {ECO:0000269|PubMed:15939293}; KM=0.16 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:15939293}; KM=0.18 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:15939293}; KM=0.58 mM for p-nitrophenyl caproate {ECO:0000269|PubMed:15939293}; Note=kcat is 581.2 sec(-1) for triacetin. kcat is 223.7 sec(-1) for tributyrin. kcat is 122.9 sec(-1) for tricaproin. kcat is 15.6 sec(-1) for tricaprylin. kcat is 501.8 sec(-1) for p-nitrophenyl acetate. kcat is 119.7 sec(-1) for p-nitrophenyl butyrate. kcat is 33.1 sec(-1) for p-nitrophenyl caproate. {ECO:0000269|PubMed:15939293}; |
| Metal Binding | |
| Rhea ID | RHEA:21164; RHEA:10604; RHEA:10605 |
| Cross Reference Brenda | 3.1.4.3; |