EzCatDB: D00509
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DB codeD00509
CATH domainDomain 13.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1Catalytic domain
Domain 23.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1Catalytic domain
E.C.2.3.1.-

CATH domainRelated DB codes (homologues)
3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1D00090,D00411,D00825,D00826,D00867,D00871

Enzyme Name
UniProtKB

P48391
Protein name2-pyrone synthase
Synonyms2-PS
EC 2.3.1.-
G2ps1
PfamPF02797 (Chal_sti_synt_C)
PF00195 (Chal_sti_synt_N)
[Graphical view]


UniProtKB:Accession NumberP48391
Entry name2PS_GERHY
Activity
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00083C00024C00010C02752C00011






CompoundMalonyl-CoAAcetyl-CoACoATriacetate lactoneCO2Monoketide intermediateEnolic acetyl-CoAAcetoacetyl-CoA Diketide intermediateTriketide CoA thioesterTriketide intermediateCyclized triketide
Typeamine group,carbohydrate,carboxyl group,nucleotide,peptide/protein,sulfide groupamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupamine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl grouparomatic ring (with hetero atoms other than nitrogen atoms)others






ChEBI15531
15351
15346
16458
16526







PubChem644066
10663
6302
444493
87642
6816
54675757
280







                    
1ee0A01UnboundUnboundUnboundUnboundUnbound  Unbound    
1ee0B01UnboundUnboundUnboundUnboundUnbound  Unbound    
1qlvA01UnboundUnboundUnboundUnboundUnbound  Unbound    
1qlvB01UnboundUnboundUnboundUnboundUnbound  Unbound    
1ee0A02UnboundUnboundUnboundUnboundUnbound  Intermediate-bound:CAA    
1ee0B02UnboundUnboundUnboundUnboundUnbound  Intermediate-bound:CAA    
1qlvA02UnboundUnboundUnboundUnboundUnbound  Unbound    
1qlvB02UnboundUnboundUnboundUnboundUnbound  Unbound    

Active-site residues
resource
Swiss-prot;P48391
pdbCatalytic residuesModified residues
          
1ee0A01       ;PHE 220
CSD 169(Double Oxidized)
1ee0B01       ;PHE 220
CSD 169(Double Oxidized)
1qlvA01       ;PHE 220
CSD 169(Double Oxidized)
1qlvB01       ;PHE 220
CSD 169(Double Oxidized)
1ee0A02HIS 308;ASN 341
 
1ee0B02HIS 308;ASN 341
 
1qlvA02HIS 308;ASN 341
 
1qlvB02HIS 308;ASN 341
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.5, p.923-9245
[3]p.14836-14837

references
[1]
JournalNature
Year1998
Volume396
Pages387-90
AuthorsEckermann S, Schroeder G, Schmidt J, Strack D, Edrada RA, Helariutta Y, Elomaa P, Kotilainen M, Kilpelaeinen I, Proksch P, Teeri TH, Schroeder J
TitleNew pathway to polyketides in plants.
Related UniProtKBP48391
[2]
CommentsX-ray crystallography
PubMed ID11137815
JournalChem Biol
Year2000
Volume7
Pages919-30
AuthorsJez JM, Austin MB, Ferrer J, Bowman ME, Schroder J, Noel JP
TitleStructural control of polyketide formation in plant-specific polyketide synthases.
Related PDB1ee0
[3]
PubMed ID11732902
JournalBiochemistry
Year2001
Volume40
Pages14829-38
AuthorsJez JM, Bowman ME, Noel JP
TitleStructure-guided programming of polyketide chain-length determination in chalcone synthase.
Related PDB1i86,1i88,1i89,1i8b

comments
The enzyme reactions of this enzyme seems to be similar to those of its homologous enzyme, Chalcone synthase (D00411 in EzCatDB).
According to the literature [2], this enzyme catalyzes the following reactions:
(A) Transfer of acyl group from sulfur atom of acetyl-CoA to the nucleophilic cysteine residue, forming monoketide intermediate:
(B) Eliminative double-bond formation; Elimination of CO2 from malonyl-CoA, giving enolic acetyl-CoA:
(C) Transfer of acyl group (monoketide) from the cysteine residue to the carbon atom of enolic acetyl-CoA, forming diketide CoA thioester (acetoacetyl-CoA):
(D) Transfer of acyl group (diketide) from sulfur atom of acetoacetyl-CoA to the cysteine residue, forming diketide intermediate:
(E) Eliminative double-bond formation; Elimination of CO2 from malonyl-CoA, giving enolic acetyl-CoA:
(F) Transfer of acyl group (diketide) from the cysteine residue to the carbon atom of enolic acetyl-CoA, forming triketide CoA thioester:
(G) Transfer of acyl group (triketide) from sulfur atom of triketide CoA thioester to the cysteine residue, forming triketide intermediate:
(H) Isomerization of triketide intermediate, forming enolic triketide intermediate:
(I) Intramolecular transfer of acyl group from the cysteine to the enolic oxygen of the enolic triketide intermediate (Cyclization):
(J) Isomerization of carbonyl oxygen to hydroxyl oxygen:

createdupdated
2002-11-252009-02-26


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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