Detail Information for IndEnz0010000902
IED ID IndEnz0010000902
Enzyme Type ID esterase000902
Protein Name Esterase/beta-lactamase LipL
EC 3.1.1.-
EC 3.5.2.6
Gene Name lipL Rv1497
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 MMVDTGVDHRAVSSHDGPDAGRRVFGAADPRFACVVRAFASMFPGRRFGGGALAVYLDGQPVVDVWKGWADRAGWVPWSADSAPMVFSATKGMTATVIHRLADRGLIDYEAPVAEYWPAFGANGKATLTVRDVMRHQAGLSGLRGATQQDLLDHVVMEERLAAAVPGRLLGKSAYHALTFGWLMSGLARAVTGKDMRLLFREELAEPLDTDGLHLGRPPADAPTRVAEIIMPQDIAANAVLTCAMRRLAHRFSGGFRSMYFPGAIAAVQGEAPLLDAEIPAANGVATARALARMYGAIANGGEIDGIRFLSRELVTGLTRNRRQVLPDRNLLVPLNFHLGYHGMPIGNVMPGFGHVGLGGSIGWTDPETGVAFALVHNRLLSPLVMTDHAGFVGIYHLIRQAAAQARKRGYQPVTPFGAPYSEPGAAAG
Enzyme Length 429
Uniprot Accession Number P71778
Absorption
Active Site ACT_SITE 88; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q9Y7D1
Activity Regulation ACTIVITY REGULATION: Esterase and beta-lactamase activities are inhibited by the active site residue modifiers phenylmethanesulfonylflouride (PMSF) and diethylpyrocarbonate (DEPC). {ECO:0000269|PubMed:26672466}.
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:26672466}; 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:26398213, ECO:0000269|PubMed:26672466}; 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:26398213, ECO:0000269|PubMed:26672466}; 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:26398213, ECO:0000269|PubMed:26672466}; 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:26672466}; 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:26398213, ECO:0000269|PubMed:26672466}; 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:26398213, ECO:0000269|PubMed:26672466}; 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, ECO:0000269|PubMed:26672466}; 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:26398213, ECO:0000269|PubMed:26672466}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000269|PubMed:26398213}; CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:26672466};
DNA Binding
EC Number 3.1.1.-; 3.5.2.6
Enzyme Function FUNCTION: Shows both esterase and beta-lactamase activities, with a much higher activity against phenyl esters than against beta-lactams (PubMed:26398213, PubMed:26672466). Shows esterase activity against both long-chain and short-chain p-nitrophenol (pNP) esters, with a preference for shorter chain esters (PubMed:26398213, PubMed:26672466). Hydrolyzes substrates containing beta-lactam ring such as nitrocefin and ampicillin (PubMed:26672466). Functions as an immunogen that activates both humoral and cell-mediated responses (PubMed:26398213). {ECO:0000269|PubMed:26398213, ECO:0000269|PubMed:26672466}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius (with pNP-butyrate as substrate). {ECO:0000269|PubMed:26672466};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 (with pNP-butyrate as substrate). {ECO:0000269|PubMed:26672466};
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Mutagenesis (8)
Keywords Cell membrane;Cell wall;Hydrolase;Membrane;Reference proteome;Secreted
Interact With
Induction INDUCTION: Up-regulated in acidic and oxidative stress conditions. {ECO:0000269|PubMed:26672466}.
Subcellular Location SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:26398213}. Cell membrane {ECO:0000269|PubMed:26398213}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 45,816
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.14 mM for pNP-butyrate {ECO:0000269|PubMed:26672466}; Note=kcat is 0.0932 sec(-1) with pNP-butyrate as substrate. {ECO:0000269|PubMed:26672466};
Metal Binding
Rhea ID RHEA:59388; RHEA:12957; RHEA:47348; RHEA:47356; RHEA:47360; RHEA:47364; RHEA:47388; RHEA:47392; RHEA:47396; RHEA:47352; RHEA:20401
Cross Reference Brenda