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 [RN:R12640];
(1b) (salicyl)adenylate + holo-[non-ribosomal peptide synthase] = AMP + salicyl-[non-ribosomal peptide synthase]
Reaction(KEGG)
R12640;
(other) R12804 R12805
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
PAEPA4228(pchD)
PAEVN297_4360
PAEIN296_4360
PAUPA14_09240(pchD)
PAPPSPA7_0872(pchD)
PAGPLES_06991(pchD)
PAFPAM18_0709(pchD)
PNCNCGM2_5473(pchD)
PAEBNCGM1900_0731(pchD)
PDKPADK2_03530
PSGG655_03565
PAEPPA1S_03680
PAERPA1R_gp2119
PAEMU769_03710
PAELT223_03610
PAESSCV20265_0733
PAEUBN889_04703(pchD)
PAEGAI22_00230
PAECM802_4358
PAEOM801_4226
PPAAB7D75_03615
PFLPFL_3496(pchD)
PPRCPFLCHA0_c35370(dhbE)
PPROPPC_3650(pchD)
PVRPverR02_15510
PCZPCL1606_27840
PSEMTO66_17000
PSOSPOS17_3639(pchD)
PSEPC4K39_5489
BPSBPSS0584(pchD)
BPMBURPS1710b_A2148(pchD)
BPLBURPS1106A_A0784(dhbE)
BPDBURPS668_A0874(dhbE)
BPSEBDL_3813
BPSMBBQ_5609(dhbE)
BPSUBBN_3985(dhbE)
BPSDBBX_5650(dhbE)
BPZBP1026B_II0644(pchD)
BPQBPC006_II0830
BPKBBK_3906(dhbE)
BPSHDR55_4766
BPSABBU_5461(dhbE)
BPSOX996_3765
BUTX994_4034
BTEBTH_II1830(pchD)
BTQBTQ_5114(dhbE)
BTJBTJ_3742(dhbE)
BTZBTL_4600(dhbE)
BTVBTHA_5629
BTHEBTN_4239
BTHMBTRA_3854(dhbE)
BTHADR62_4288
BTHLBG87_4571
BURBcep18194_B0670
BCMBcenmc03_5287
BCHBcen2424_5000
BCJBCAM2232(pchD)
BCEOI35_6123(pchD)
BCEDDM42_5762
BCEPAPZ15_27900
BSEMWJ12_31065
BSTLBBJ41_24885
BARINLX30_26095
BGPBGL_1c20600(pchD)
BPLAbpln_1g19120
PDEPden_3008
PPANESD82_00855
SECHB18_04285
ALIAZOLI_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
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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