KEGG   ENZYME: 6.2.1.61
Entry
EC 6.2.1.61                 Enzyme                                 

Name
salicylate---[aryl-carrier protein] ligase;
pmsE (gene name);
pchD (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
Sysname
salicylate:holo-[non-ribosomal peptide synthase] ligase
Reaction(IUBMB)
ATP + salicylate + holo-[non-ribosomal peptide synthase] = AMP + diphosphate + salicyl-[non-ribosomal peptide synthase] (overall reaction);
(1a) ATP + salicylate = diphosphate + (salicyl)adenylate;
(1b) (salicyl)adenylate + holo-[non-ribosomal peptide synthase] = AMP + salicyl-[non-ribosomal peptide synthase]
Substrate
ATP [CPD:C00002];
salicylate [CPD:C00805];
holo-[non-ribosomal peptide synthase];
(salicyl)adenylate [CPD:C22233]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
salicyl-[non-ribosomal peptide synthase];
(salicyl)adenylate [CPD:C22233]
Comment
The enzyme catalyses the activation of salicylate to (salicyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein, which is often a domain of a larger non-ribosimal peptide synthase. The PmsE enzyme is involved in pseudomonine biosynthesis and transfers the activated salicylate first to itself, and then to a PmsG protein. The PchD enzyme is involved in pyochelin biosynthesis and transfers the activated salicylate directly to the PchE protein.
History
EC 6.2.1.61 created 2019
Pathway
ec01053  Biosynthesis of siderophore group nonribosomal peptides
Orthology
K12238  salicylate---[aryl-carrier protein] ligase
Genes
PAE: PA4228(pchD)
PAEV: N297_4360
PAEI: N296_4360
PAU: PA14_09240(pchD)
PAP: PSPA7_0872(pchD)
PAG: PLES_06991(pchD)
PAF: PAM18_0709(pchD)
PNC: NCGM2_5473(pchD)
PAEB: NCGM1900_0731(pchD)
PDK: PADK2_03530
PAEP: PA1S_03680
PAEM: U769_03710
PAEL: T223_03610
PAEU: BN889_04703(pchD)
PAEG: AI22_00230
PAEC: M802_4358
PAEO: M801_4226
PFL: PFL_3496(pchD)
PPRC: PFLCHA0_c35370(dhbE)
PPRO: PPC_3650(pchD)
PSEM: TO66_17000
PSOS: POS17_3639(pchD)
BPS: BPSS0584(pchD)
BPM: BURPS1710b_A2148(pchD)
BPL: BURPS1106A_A0784(dhbE)
BPD: BURPS668_A0874(dhbE)
BPSE: BDL_3813
BPSM: BBQ_5609(dhbE)
BPSU: BBN_3985(dhbE)
BPSD: BBX_5650(dhbE)
BPZ: BP1026B_II0644(pchD)
BPK: BBK_3906(dhbE)
BPSH: DR55_4766
BPSA: BBU_5461(dhbE)
BPSO: X996_3765
BUT: X994_4034
BTE: BTH_II1830(pchD)
BTQ: BTQ_5114(dhbE)
BTJ: BTJ_3742(dhbE)
BTZ: BTL_4600(dhbE)
BTV: BTHA_5629
BTHE: BTN_4239
BTHM: BTRA_3854(dhbE)
BTHA: DR62_4288
BTHL: BG87_4571
BCN: Bcen_3367
BCJ: BCAM2232(pchD)
BCEO: I35_6123(pchD)
BCED: DM42_5762
BSEM: WJ12_31065
BGP: BGL_1c20600(pchD)
PDE: Pden_3008
SECH: B18_04285
ALI: AZOLI_p20159(pchD)
 » show all
Reference
1  [PMID:10555976]
  Authors
Quadri LE, Keating TA, Patel HM, Walsh CT
  Title
Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF.
  Journal
Biochemistry 38:14941-54 (1999)
DOI:10.1021/bi991787c
  Sequence
[pae:PA4228]
Reference
2  [PMID:18710233]
  Authors
Sattely ES, Walsh CT
  Title
A latent oxazoline electrophile for N-O-C bond formation in pseudomonine biosynthesis.
  Journal
J Am Chem Soc 130:12282-4 (2008)
DOI:10.1021/ja804499r
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.61
IUBMB Enzyme Nomenclature: 6.2.1.61
ExPASy - ENZYME nomenclature database: 6.2.1.61
BRENDA, the Enzyme Database: 6.2.1.61

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