| IED ID | IndEnz0010001787 |
| Enzyme Type ID | esterase001787 |
| Protein Name |
Thioesterase TesA EC 3.1.2.- Acetylesterase EC 3.1.1.6 Palmitoyl-CoA hydrolase EC 3.1.2.2 |
| Gene Name | tesA Rv2928 MTCY338.17 |
| 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 | MLARHGPRYGGSVNGHSDDSSGDAKQAAPTLYIFPHAGGTAKDYVAFSREFSADVKRIAVQYPGQHDRSGLPPLESIPTLADEIFAMMKPSARIDDPVAFFGHSMGGMLAFEVALRYQSAGHRVLAFFVSACSAPGHIRYKQLQDLSDREMLDLFTRMTGMNPDFFTDDEFFVGALPTLRAVRAIAGYSCPPETKLSCPIYAFIGDKDWIATQDDMDPWRDRTTEEFSIRVFPGDHFYLNDNLPELVSDIEDKTLQWHDRA |
| Enzyme Length | 261 |
| Uniprot Accession Number | P9WQD5 |
| Absorption | |
| Active Site | ACT_SITE 104; /evidence=ECO:0000305|PubMed:30292819; ACT_SITE 208; /evidence=ECO:0000305|PubMed:30292819; ACT_SITE 236; /evidence=ECO:0000305|PubMed:30292819 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited in vitro by CyC17, a monocyclic enol phosphate analog to Cyclipostins, which binds covalently to the catalytic Ser-104 residue leading to a total loss of enzyme activity (PubMed:30292819). Methyl arachidonyl fluorophosphonate (MAFP) inhibits esterase activity but it only reduces by approximately 50% thioesterase activity with palmitoyl-CoA as substrate (PubMed:31388991). Thioesterase activity is inhibited by tetrahydrolipstatin (THL) (PubMed:31388991). {ECO:0000269|PubMed:30292819, ECO:0000269|PubMed:31388991}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; Evidence={ECO:0000269|PubMed:31388991}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:30292819, ECO:0000269|PubMed:31388991}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:31388991}; 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:30292819}; CATALYTIC ACTIVITY: Reaction=H2O + pentanoate ester = an aliphatic alcohol + H(+) + pentanoate; Xref=Rhea:RHEA:48436, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:31011, ChEBI:CHEBI:50871; Evidence={ECO:0000269|PubMed:30292819}; 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:30292819}; |
| DNA Binding | |
| EC Number | 3.1.2.-; 3.1.1.6; 3.1.2.2 |
| Enzyme Function | FUNCTION: Involved in the synthesis of both phthiocerol dimycocerosates (PDIMs) and phenolic glycolipids (PGLs), which are structurally related lipids non-covalently bound to the outer cell wall layer of M.tuberculosis and are important virulence factors (PubMed:30292819). In vitro, TesA has both thioesterase and esterase activities (PubMed:30292819, PubMed:31388991). Exhibits thioesterase activity on acyl-CoA derivatives such as palmitoyl-CoA and decanoyl-CoA (PubMed:30292819, PubMed:31388991). Also displays hydrolytic activity on ester substrates, being more active on pNP esters with short carbon chain lengths (C2-C5) than with those bearing medium and long carbon chain lengths (C8-C18) (PubMed:30292819). {ECO:0000269|PubMed:30292819, ECO:0000269|PubMed:31388991}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius (with palmitoyl-CoA as substrate). {ECO:0000269|PubMed:31388991}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Helix (11); Mutagenesis (1); Region (1); Turn (2) |
| Keywords | 3D-structure;Hydrolase;Lipid biosynthesis;Lipid metabolism;Reference proteome;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 6FVJ; 6FW5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,152 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=57.44 uM for palmitoyl-CoA {ECO:0000269|PubMed:31388991}; Note=kcat is 0.00342 sec(-1) with palmitoyl-CoA as substrate. {ECO:0000269|PubMed:31388991}; |
| Metal Binding | |
| Rhea ID | RHEA:16781; RHEA:16645; RHEA:40059; RHEA:12957; RHEA:48436; RHEA:47356 |
| Cross Reference Brenda |