| IED ID | IndEnz0010000912 |
| Enzyme Type ID | esterase000912 |
| Protein Name |
Lipase LipV EC 3.1.1.1 |
| Gene Name | lipV Rv3203 |
| 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 | MIIDLHVQRYGPSGPARVLTIHGVTEHGRIWHRLAHHLPEIPIAAPDLLGHGRSPWAAPWTIDANVSALAALLDNQGDGPVVVVGHSFGGAVAMHLAAARPDQVAALVLLDPAVALDGSRVREVVDAMLASPDYLDPAEARAEKATGAWADVDPPVLDAELDEHLVALPNGRYGWRISLPAMVCYWSELARDIVLPPVGTATTLVRAVRASPAYVSDQLLAALDKRLGADFELLDFDCGHMVPQAKPTEVAAVIRSRLGPR |
| Enzyme Length | 261 |
| Uniprot Accession Number | L0TC47 |
| Absorption | |
| Active Site | ACT_SITE 87; /note=Nucleophile; /evidence=ECO:0000305|PubMed:24234750; ACT_SITE 217; /note=Charge relay system; /evidence=ECO:0000305|PubMed:24234750; ACT_SITE 240; /note=Charge relay system; /evidence=ECO:0000305|PubMed:24234750 |
| Activity Regulation | ACTIVITY REGULATION: Is inbibited by tetrahydrolipstatin, a specific lipase inhibitor and RHC 80267, a diacylglycerol lipase inhibitor, but not by phenylglyoxal and iodoacetate. {ECO:0000269|PubMed:24234750}. |
| 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:24234750}; 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:24234750}; 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:24234750}; 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:24234750}; 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:24234750}; 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:24234750}; 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:24234750}; 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:24234750}; |
| DNA Binding | |
| EC Number | 3.1.1.1 |
| Enzyme Function | FUNCTION: Lipase that displays broad substrate specificity and preferentially hydrolyzes p-nitrophenyl myristate in vitro. Also shows significant activity with pNP-butyrate (68%), pNP-octanoate (82%), pNP-decanoate (90%), and pNP-laurate (74%). Is probably involved in lipid catabolism. Is active at low pH, and might play some important role in mycobacterial biology in macrophages where the bacteria encounters acidic stress. {ECO:0000269|PubMed:24234750}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:24234750}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Retains nearly 60% enzyme activity at pH 6.0. The relative stability of purified enzyme is high at acidic pH and neutral pH (4.0-7.0) as compared to its relative stability at higher pH (9.0-10.0). {ECO:0000269|PubMed:24234750}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Frameshift (1); Mutagenesis (4) |
| Keywords | Direct protein sequencing;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Serine esterase |
| Interact With | |
| Induction | INDUCTION: Expression is early up-regulated during acidic stress as compared to normal whereas no expression is observed under nutrient and oxidative stress conditions. {ECO:0000269|PubMed:24234750}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,868 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=714.28 uM for pNP-myristate {ECO:0000269|PubMed:24234750}; Note=kcat is 1312 sec(-1) with pNP-myristate as substrate. {ECO:0000269|PubMed:24234750}; |
| Metal Binding | |
| Rhea ID | RHEA:21164; RHEA:47388; RHEA:47360; RHEA:47356; RHEA:47364; RHEA:47348; RHEA:47392; RHEA:47396 |
| Cross Reference Brenda |