| IED ID | IndEnz0005001249 |
| Enzyme Type ID | lipase001249 |
| Protein Name |
GDSL lipase Rv0518 EC 3.1.1.- |
| Gene Name | Rv0518 |
| 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 | MSRPGTYVIGLTLLVGLVVGNPGCPRSYRPLTLDYRLNPVAVIGDSYTTGTDEGGLGSKSWTARTWQMLAARGVRIAADVAAEGRAGYGVPGDHGNVFEDLTARAVQPDDALVVFFGSRNDQGMDPEDPEMLAEKVRDTFDLARHRAPSASLLVIAPPWPTADVPGPMLRIRDVLGAQARAAGAVFVDPIADHWFVDRPELIGADGVHPNDAGHEYLADKIAPLISMELVG |
| Enzyme Length | 231 |
| Uniprot Accession Number | O33363 |
| Absorption | |
| Active Site | ACT_SITE 46; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P41734; ACT_SITE 205; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P41734; ACT_SITE 208; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P41734 |
| Activity Regulation | ACTIVITY REGULATION: Activity is inhibited by the serine modifier phenylmethylsulfonyl fluoride (PMSF). {ECO:0000269|PubMed:31125644}. |
| 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:31125644}; 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:31125644}; 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:31125644}; 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:31125644}; 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:31125644}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: GDSL lipase that catalyzes the hydrolysis of p-nitrophenyl (pNP) esters. pNP-decanoate (C10) is the preferred substrate. It can also use pNP-octanoate (C8), pNP-dodecanoate (C12) and pNP-tetradecanoate (C14). Has lower activity with pNP-butyrate (C4), pNP-palmitate (C16) and pNP-stearate (C18) (PubMed:31125644). Does not show phospholipase A1 activity (PubMed:31125644). Might help bacteria to utilize available lipids for its growth as well as provide resistance to various intracellular stresses by cell wall modulation resulting in enhanced intracellular survival (PubMed:31125644). {ECO:0000269|PubMed:31125644}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius (with pNP-decanoate as substrate). {ECO:0000269|PubMed:31125644}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (with pNP-decanoate as substrate). {ECO:0000269|PubMed:31125644}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Mutagenesis (5); Signal peptide (1); Site (2) |
| Keywords | Cell wall;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is up-regulated under nutrient starvation (in strain H37Ra). {ECO:0000269|PubMed:31125644}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:31125644}. Secreted, extracellular space {ECO:0000269|PubMed:31125644}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,636 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=400 uM for pNP-decanoate {ECO:0000269|PubMed:31125644}; Note=kcat is 14440 min(-1) with pNP-decanoate as substrate. {ECO:0000269|PubMed:31125644}; |
| Metal Binding | |
| Rhea ID | RHEA:59388; RHEA:47360; RHEA:47356; RHEA:47364; RHEA:47388 |
| Cross Reference Brenda |