Detail Information for IndEnz0010000976
IED ID IndEnz0010000976
Enzyme Type ID esterase000976
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