| 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 |