Detail Information for IndEnz0010000975
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