| IED ID | IndEnz0005001120 |
| Enzyme Type ID | lipase001120 |
| Protein Name |
Carboxylesterase LipF EC 3.1.1.1 |
| 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 | MRAPGVRAADGAGRVVLYLHGGAFVMCGPNSHSRIVNALSGFAESPVLIVDYRLIPKHSLGMALDDCHDAYQWLRARGYRPEQIVLAGDSAGGYLALALAQRLQCDDEKPAAIVAISPLLQLAKGPKQDHPNIGTDAMFPARAFDALAAWVRAAAAKNMVDGRPEDLYEPLDHIESSLPPTLIHVSGSEVLLHDAQLGAGKLAAAGVCAEVRVWPGQAHLFQLATPLVPEATRSLRQIGQFIRDATADSSLSPVHRSRYVAGSPRAASRGAFGQSPI |
| Enzyme Length | 277 |
| Uniprot Accession Number | O06350 |
| Absorption | |
| Active Site | ACT_SITE 90; /evidence=ECO:0000305|PubMed:15939293; ACT_SITE 189; /evidence=ECO:0000305|PubMed:15939293; ACT_SITE 219; /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}; |
| DNA Binding | |
| EC Number | 3.1.1.1 |
| Enzyme Function | FUNCTION: Hydrolyzes short-chain esters. Shows maximal activity with triacetin and p-nitrophenyl acetate. {ECO:0000269|PubMed:15939293}. |
| 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); Motif (1); Mutagenesis (3) |
| Keywords | Hydrolase;Reference proteome;Serine esterase;Stress response |
| Interact With | |
| Induction | INDUCTION: Induced by acidic pH. {ECO:0000269|PubMed:15939293}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 20..22; /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 | 29,430 |
| 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.; |
| Metal Binding | |
| Rhea ID | RHEA:21164 |
| Cross Reference Brenda | 3.1.4.3; |