| IED ID | IndEnz0002004944 |
| Enzyme Type ID | protease004944 |
| Protein Name |
Esterase LipU EC 3.1.1.- |
| Gene Name | lipU Rv1076 |
| 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 | MAVRPVLAVGSYLPHAPWPWGVIDQAARVLLPASTTVRAAVSLPNASAQLVRASGVLPADGTRRAVLYLHGGAFLTCGANSHGRLVELLSKFADSPVLVVDYRLIPKHSIGMALDDCHDGYRWLRLLGYEPEQIVLAGDSAGGYLALALAQRLQEVGEEPAALVAISPLLQLAKEHKQAHPNIKTDAMFPARAFDALDALVASAAARNQVDGEPEELYEPLEHITPGLPRTLIHVSGSEVLLHDAQLAAAKLAAAGVPAEVRVWPGQVHDFQVAASMLPEAIRSLRQIGEYIREATG |
| Enzyme Length | 297 |
| Uniprot Accession Number | O53424 |
| Absorption | |
| Active Site | ACT_SITE 140; /evidence="ECO:0000305|PubMed:28164792, ECO:0000305|PubMed:28327423"; ACT_SITE 239; /evidence="ECO:0000305|PubMed:28327423"; ACT_SITE 269; /evidence="ECO:0000305|PubMed:28164792, ECO:0000305|PubMed:28327423" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the ionic detergent SDS and by the serine protease inhibitor PMSF (PubMed:28164792). Inhibited by the FDA approved drugs Diosmin, Acarbose and Ouabain. These drugs remain bound in the active site pocket and could be probable drug candidates to combat TB disease (PubMed:29557724). {ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:29557724}. |
| 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:26398213, ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; 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:28164792, ECO:0000269|PubMed:28327423}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; 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:28164792, ECO:0000269|PubMed:28327423}; 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:28164792, ECO:0000269|PubMed:28327423}; 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:28164792, ECO:0000269|PubMed:28327423}; 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:26398213}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Esterase that shows preference for short chain fatty acids (PubMed:26398213, PubMed:28164792, PubMed:28327423). Contributes to the growth of M.tuberculosis during the nutritive stress (PubMed:28164792). Elicits strong humoral response in both extrapulmonary and relapsed cases of tuberculosis patients (PubMed:28327423). {ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius (with pNP-butyrate as substrate). {ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 (with pNP-butyrate as substrate). {ECO:0000269|PubMed:28164792, ECO:0000269|PubMed:28327423}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Mutagenesis (4) |
| Keywords | Hydrolase;Reference proteome;Secreted |
| Interact With | |
| Induction | INDUCTION: Up-regulated in nutritive stress but not in acidic and oxidative stress. {ECO:0000269|PubMed:28164792}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28327423}. Note=Extracellular. {ECO:0000269|PubMed:28327423}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,681 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.73 uM for pNP-butyrate {ECO:0000269|PubMed:28164792}; KM=333 uM for pNP-butyrate {ECO:0000269|PubMed:28327423}; Note=kcat is 49.8 min(-1) with pNP-butyrate as substrate. {ECO:0000269|PubMed:28164792}; |
| Metal Binding | |
| Rhea ID | RHEA:59388; RHEA:47348; RHEA:12957; RHEA:47360; RHEA:47356; RHEA:47364; RHEA:47392 |
| Cross Reference Brenda |