| IED ID | IndEnz0005001143 |
| Enzyme Type ID | lipase001143 |
| 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 |