| IED ID | IndEnz0010000975 |
| Enzyme Type ID | esterase000975 |
| Protein Name |
GDSL-like esterase Rv1075c EC 3.1.-.- Acetylesterase EC 3.1.1.6 |
| Gene Name | Rv1075c |
| 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 | MPRRSTIALATAGALASTGTAYLGARNLLVGQATHARTVIPKSFDAPPRADGVYTRGGGPVQRWRREVPFDVHLMIFGDSTATGYGCASAEEVPGVLIARGLAEQTGKRIRLSTKAIVGATSKGVCGQVDAMFVVGPPPDAAVIMIGANDITALNGIGPSAQRLADCVRRLRTRGAVVVVGTCPDLGVITAIPQPLRALAHTRGVRLARAQTAAVKAAGGVPVPLGHLLAPKFRAMPELMFSADRYHPSAPAYALAADLLFLALRDALTEKLDIPIHETPSRPGTATLEPGHTRHSMMSRLRRPRPARAVPTGG |
| Enzyme Length | 314 |
| Uniprot Accession Number | O53423 |
| Absorption | |
| Active Site | ACT_SITE 80; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P41734; ACT_SITE 244; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P41734; ACT_SITE 247; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P41734 |
| Activity Regulation | ACTIVITY REGULATION: Esterase activity is significantly inhibited by the serine modifier phenylmethylsulfonyl fluoride (PMSF). Completely inhibited by diethyl pyrocarbonate. {ECO:0000269|PubMed:31001637}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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; EC=3.1.1.6; Evidence={ECO:0000269|PubMed:31001637}; 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:31001637}; CATALYTIC ACTIVITY: Reaction=H2O + triacetin = acetate + diacetylglycerol + H(+); Xref=Rhea:RHEA:48028, ChEBI:CHEBI:9661, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:88156; Evidence={ECO:0000269|PubMed:31001637}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:31001637}; |
| DNA Binding | |
| EC Number | 3.1.-.-; 3.1.1.6 |
| Enzyme Function | FUNCTION: Esterase that preferentially hydrolyzes short-chain fatty acids, particularly pNP-acetate (C2) and pNP-butyrate (C4). Has also weak activity with pNP-hexanoate (C6) and pNP-octanoate (C8). It can also hydrolyze short-chain tryglycerides such as triacetin and tributyrin (PubMed:31001637). Important for intracellular survival (PubMed:31001637). {ECO:0000269|PubMed:31001637}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius (with pNP-acetate as substrate). {ECO:0000269|PubMed:31001637}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (with pNP-acetate as substrate). {ECO:0000269|PubMed:31001637}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Mutagenesis (3); Region (1); Signal peptide (1); Site (2) |
| Keywords | Hydrolase;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Induced under acidic conditions. {ECO:0000269|PubMed:31001637}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,879 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=753 uM for pNP-acetate {ECO:0000269|PubMed:31001637}; |
| Metal Binding | |
| Rhea ID | RHEA:12957; RHEA:47348; RHEA:48028; RHEA:40475 |
| Cross Reference Brenda |