IED ID | IndEnz0010000787 |
Enzyme Type ID | esterase000787 |
Protein Name |
Esterase PE16 EC 3.1.1.- PE family protein PE16 |
Gene Name | PE16 Rv1430 |
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 | MSFVFAVPEMVAATASDLASLGAALSEATAAAAIPTTQVLAAAADEVSAAIAELFGAHGQEFQALSAQASAFHDRFVRALSAAAGWYVDAEAANAALVDTAATGASELGSGGRTALILGSTGTPRPPFDYMQQVYDRYIAPHYLGYAFSGLYTPAQFQPWTGIPSLTYDQSVAEGAGYLHTAIMQQVAAGNDVVVLGFSQGASVATLEMRHLASLPAGVAPSPDQLSFVLLGNPNNPNGGILARFPGLYLQSLGLTFNGATPDTDYATTIYTTQYDGFADFPKYPLNILADVNALLGIYYSHSLYYGLTPEQVASGIVLPVSSPDTNTTYILLPNEDLPLLQPLRGIVPEPLLDLIEPDLRAIIELGYDRTGYADVPTPAALFPVHIDPIAVPPQIGAAIGGPLTALDGLLDTVINDQLNPVVTSGIYQAGAELSVAAAGYGAPAGVTNAIFIGQQVLPILVEGPGALVTADTHYLVDAIQDLAAGDLSGFNQNLQLIPATNIALLVFAAGIPAVAAVAILTGQDFPV |
Enzyme Length | 528 |
Uniprot Accession Number | L7N697 |
Absorption | |
Active Site | ACT_SITE 199; /evidence=ECO:0000305|PubMed:23383323 |
Activity Regulation | ACTIVITY REGULATION: Esterase activity is significantly inhibited by the serine modifier phenylmethylsulfonyl fluoride (PMSF). {ECO:0000269|PubMed:23383323}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | 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:23383323}; 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:23383323}; 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:23383323}; |
DNA Binding | |
EC Number | 3.1.1.- |
Enzyme Function | FUNCTION: Esterase that hydrolyzes short to medium chain fatty acid esters with the highest specific activity for p-nitrophenyl caproate (pNPC6). Has lower activity with p-nitrophenyl caprylate (pNPC8) and p-nitrophenyl butyrate (pNPC4). Has weak activity with p-nitrophenyl caprate (pNPC10) and p-nitrophenyl laurate (pNPC12). Does not possess lipolytic activity and cutinase activity. {ECO:0000269|PubMed:23383323}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-38 degrees Celsius. {ECO:0000269|PubMed:23383323}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:23383323}; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Domain (2); Mutagenesis (1); Region (1); Transmembrane (1) |
Keywords | Hydrolase;Membrane;Reference proteome;Serine esterase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 54,584 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.2 mM for pNPC4 {ECO:0000269|PubMed:23383323}; KM=5.15 mM for pNPC6 {ECO:0000269|PubMed:23383323}; KM=10 mM for pNPC8 {ECO:0000269|PubMed:23383323}; Note=kcat is 341 sec(-1) with pNPC4 as substrate. kcat is 534 sec(-1) with pNPC6 as substrate. kcat is 305 sec(-1) with pNPC8 as substrate. {ECO:0000269|PubMed:23383323}; |
Metal Binding | |
Rhea ID | RHEA:47352; RHEA:47356; RHEA:47348 |
Cross Reference Brenda |