EzCatDB: D00871
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DB codeD00871
RLCP classification3.1177.220085.58 : Transfer
1.51.790.101 : Hydrolysis
3.1197.15025.150 : Transfer
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.2.3.1.179
CSA1kas

CATH domainRelated DB codes (homologues)
3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1D00090,D00411,D00509,D00825,D00826,D00867

Enzyme Name
UniProtKBKEGG

P0AAI5Q6G441Q8YFP7A4JL30P73283Q5SL80Q8NXE1Q8Y574Q9FBC2
Protein name3-oxoacyl-[acyl-carrier-protein] synthase 23-oxoacyl-[acyl-carrier-protein] synthase 23-oxoacyl-[acyl-carrier-protein] synthase 23-oxoacyl-[acyl-carrier-protein] synthase 23-oxoacyl-[acyl-carrier-protein] synthase 23-oxoacyl-[acyl-carrier-protein] synthase 23-oxoacyl-[acyl-carrier-protein] synthase 23-oxoacyl-[acyl-carrier-protein] synthase 23-oxoacyl-[acyl-carrier-protein] synthase 2beta-ketoacyl-acyl-carrier-protein synthase II
KASII
KAS II
FabF
3-oxoacyl-acyl carrier protein synthase I
beta-ketoacyl-ACP synthase II
(Z)-hexadec-11-enoyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating)
SynonymsEC 2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
KAS II
EC 2.3.1.179
EC 2.3.1.179
EC 2.3.1.179
EC 2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
KAS II
EC 2.3.1.179
EC 2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
KAS II
EC 2.3.1.179
EC 2.3.1.179
RefSeqNP_415613.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489363.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
YP_033372.1 (Protein)
NC_005956.1 (DNA/RNA sequence)
NP_540390.1 (Protein)
NC_003317.1 (DNA/RNA sequence)
YP_001116448.1 (Protein)
NC_009255.1 (DNA/RNA sequence)
NP_440631.1 (Protein)
NC_000911.1 (DNA/RNA sequence)
YP_005650690.1 (Protein)
NC_017277.1 (DNA/RNA sequence)
YP_007450514.1 (Protein)
NC_020286.1 (DNA/RNA sequence)
YP_143679.1 (Protein)
NC_006461.1 (DNA/RNA sequence)
NP_645683.1 (Protein)
NC_003923.1 (DNA/RNA sequence)
NP_465725.1 (Protein)
NC_003210.1 (DNA/RNA sequence)

PfamPF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00061Fatty acid biosynthesis

UniProtKB:Accession NumberP0AAI5Q6G441Q8YFP7A4JL30P73283Q5SL80Q8NXE1Q8Y574Q9FBC2
Entry nameFABF_ECOLIQ6G441_BARHEQ8YFP7_BRUMEA4JL30_BURVGFABF_SYNY3Q5SL80_THET8FABF_STAAWQ8Y574_LISMOQ9FBC2_STRPN
Activity(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
SubunitHomodimer.


Homodimer.



Subcellular location








Cofactor









Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC01209L00039C00001C00288C00229L00040I00138I00139I00140I00134I00141
Compoundmalonyl-[acyl-carrier-protein](Z)-hexadec-11-enoyl-[acyl-carrier protein]H2OBicabonate(HCO3-)[acyl-carrier-protein](Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein]Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-[acyl-carrier protein]Peptidyl-Cys-S-(Z)-hexadec-11-enoyl[Acyl-carrier protein]-tetrahedral-malonyl group[Acyl-carrier protein]-decarboxylated malonyl group (Peptidyl-Ser-phosphopantetheine-S-enolate)Peptidyl-Cys-tetrahedral-(Z)-hexadec-11-enoyl-keto-[acyl-carrier protein]
Typecarbohydrate,carboxyl group,peptide/protein,phosphate group/phosphate ion,sulfide groupcarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide groupH2Ocarboxyl groupcarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfhydryl groupcarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group




ChEBI

15377
17544







PubChem

962
22247451
769
22647601







                   
1b3nA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:CER
1kas001UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gfvA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gfwA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gfxA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gfyA01UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:DAOUnboundUnboundUnbound
3g0yA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3g11A01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3hnzA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3ho2A01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3ho9A01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3i8pA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3e60A01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3e60B01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3kzuA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3kzuB01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3kzuC01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
4ddoA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
4f32A01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
4f32B01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1e5mA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1j3nA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1j3nB01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gqdA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gqdB01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3o04A01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ox0A01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxhA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxhB01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxhC01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxhD01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2almA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2rjtA01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2rjtB01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2rjtC01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2rjtD01UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1b3nA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1kas002UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gfvA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gfwA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gfxA02Analogue:PMNUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gfyA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3g0yA02Analogue:P9AUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3g11A02Analogue:P9CUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3hnzA02Analogue:PMNUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3ho2A02Analogue:N32Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3ho9A02Analogue:N3AUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3i8pA02Analogue:840Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3e60A02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3e60B02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3kzuA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3kzuB02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3kzuC02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
4ddoA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
4f32A02Analogue:N32Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
4f32B02Analogue:N32Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1e5mA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1j3nA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1j3nB02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gqdA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2gqdB02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3o04A02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ox0A02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxhA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxhB02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxhC02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxhD02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2almA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2rjtA02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2rjtB02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2rjtC02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2rjtD02UnboundUnbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [1], [8], [10], [13], [14], [15], [16], [17], [20], [24], [30] [31] & CSA;1dd8
pdbCatalytic residuesModified residuesMain-chain involved in catalysiscomment
            
1b3nA01CYS 163
                                 
CYS 163
 
1kas001CYS 163
                                 
CYS 163
 
2gfvA01       
                                 
       
mutant C163Q
2gfwA01CYS 163
                                 
CYS 163
 
2gfxA01       
                                 
       
mutant C163Q
2gfyA01CYS 163
                                 
CYS 163
 
3g0yA01       
                                 
       
mutant C163Q
3g11A01       
                                 
       
mutant C163Q
3hnzA01       
                                 
       
mutant C163A
3ho2A01       
                                 
       
mutant C163A
3ho9A01       
                                 
       
mutant C163A
3i8pA01       
                                 
       
mutant C163A
3e60A01CYS 170
                                 
CYS 170
 
3e60B01CYS 170
                                 
CYS 170
 
3kzuA01CYS 170
                                 
CYS 170
 
3kzuB01CYS 170
                                 
CYS 170
 
3kzuC01CYS 170
                                 
CYS 170
 
4ddoA01CYS 172
                                 
CYS 172
 
4f32A01       
CSU 172(Cysteine-S-Sulfonic acid)
CSU 172
 
4f32B01       
CSU 172(Cysteine-S-Sulfonic acid)
CSU 172
 
1e5mA01CYS 167
                                 
CYS 167
 
1j3nA01CYS 161
                                 
CYS 161
 
1j3nB01CYS 161
                                 
CYS 161
 
2gqdA01CYS 165
                                 
CYS 165
 
2gqdB01CYS 165
                                 
CYS 165
 
3o04A01CYS 164
                                 
CYS 164
 
1ox0A01CYS 164
                                 
CYS 164
 
1oxhA01CYS 164
                                 
CYS 164
 
1oxhB01CYS 164
                                 
CYS 164
 
1oxhC01CYS 164
                                 
CYS 164
 
1oxhD01CYS 164
                                 
CYS 164
 
2almA01CYS 164
                                 
CYS 164
 
2rjtA01CYS 164
                                 
CYS 164
 
2rjtB01CYS 164
                                 
CYS 164
 
2rjtC01CYS 164
                                 
CYS 164
 
2rjtD01CYS 164
                                 
CYS 164
 
1b3nA02HIS 303;LYS 335;HIS 340
 
PHE 400
 
1kas002HIS 303;LYS 335;HIS 340
 
PHE 400
 
2gfvA02HIS 303;LYS 335;HIS 340
 
PHE 400
 
2gfwA02HIS 303;LYS 335;HIS 340
 
PHE 400
 
2gfxA02HIS 303;LYS 335;HIS 340
 
PHE 400
 
2gfyA02HIS 303;       ;HIS 340
 
PHE 400
mutant K335A
3g0yA02HIS 303;LYS 335;HIS 340
 
PHE 400
 
3g11A02HIS 303;LYS 335;HIS 340
 
PHE 400
 
3hnzA02HIS 303;LYS 335;HIS 340
 
PHE 400
 
3ho2A02HIS 303;LYS 335;HIS 340
 
PHE 400
 
3ho9A02HIS 303;LYS 335;HIS 340
 
PHE 400
 
3i8pA02HIS 303;LYS 335;HIS 340
 
PHE 400
 
3e60A02HIS 311;LYS 342;HIS 347
 
PHE 406
 
3e60B02HIS 311;LYS 342;HIS 347
 
PHE 406
 
3kzuA02HIS 311;LYS 342;HIS 347
 
PHE 406
 
3kzuB02HIS 311;LYS 342;HIS 347
 
PHE 406
 
3kzuC02HIS 311;LYS 342;HIS 347
 
PHE 406
 
4ddoA02HIS 313;LYS 344;HIS 349
 
PHE 409
 
4f32A02HIS 313;LYS 344;HIS 349
 
PHE 409
 
4f32B02HIS 313;LYS 344;HIS 349
 
PHE 409
 
1e5mA02HIS 307;LYS 339;HIS 344
 
PHE 403
 
1j3nA02HIS 301;LYS 333;HIS 338
 
PHE 396
 
1j3nB02HIS 301;LYS 333;HIS 338
 
PHE 396
 
2gqdA02HIS 304;LYS 336;HIS 341
 
PHE 400
 
2gqdB02HIS 304;LYS 336;HIS 341
 
PHE 400
 
3o04A02HIS 303;LYS 335;HIS 340
 
PHE 399
 
1ox0A02HIS 303;LYS 332;HIS 337
 
PHE 396
 
1oxhA02HIS 303;LYS 332;HIS 337
 
PHE 396
 
1oxhB02HIS 303;LYS 332;HIS 337
 
PHE 396
 
1oxhC02HIS 303;LYS 332;HIS 337
 
PHE 396
 
1oxhD02HIS 303;LYS 332;HIS 337
 
PHE 396
 
2almA02       ;LYS 332;HIS 337
 
PHE 396
mutant H303A, G379A
2rjtA02HIS 303;LYS 332;HIS 337
 
PHE 396
mutant E22A, E94A, E325A, E383A, E409A
2rjtB02HIS 303;LYS 332;HIS 337
 
PHE 396
mutant E22A, E94A, E325A, E383A, E409A
2rjtC02HIS 303;LYS 332;HIS 337
 
PHE 396
mutant E22A, E94A, E325A, E383A, E409A
2rjtD02HIS 303;LYS 332;HIS 337
 
PHE 396
mutant E22A, E94A, E325A, E383A, E409A

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.1186-1189
[3]Fig.1B, p.603-604
[5]p.9842-9844
[6]Table 4, p.496-498
[7]Fig.6, p.10883-10887
[8]p.4139-4141
[9]Fig.8, p.431-433
[11]Fig.7c, p.810-814
[13]Fig.6, p.17396-17398
[15]p.361-363
[16]Fig.5, p.696-697

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed ID9482715
JournalEMBO J
Year1998
Volume17
Pages1183-91
AuthorsHuang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y
TitleCrystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.
Related PDB1kas
Related UniProtKBP0AAI5
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
PubMed ID10037680
JournalJ Biol Chem
Year1999
Volume274
Pages6031-4
AuthorsMoche M, Schneider G, Edwards P, Dehesh K, Lindqvist Y
TitleStructure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.
Related PDB1b3n
Related UniProtKBP0AAI5
[3]
PubMed ID11171140
JournalBiochem Soc Trans
Year2000
Volume28
Pages601-7
Authorsvon Wettstein-Knowles P, Olsen J, Arnvig Mcguire K, Larsen S
TitleMolecular aspects of beta-ketoacyl synthase (KAS) catalysis.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed ID10673437
JournalStructure
Year2000
Volume8
Pages185-95
AuthorsDavies C, Heath RJ, White SW, Rock CO
TitleThe 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Related PDB1ebl
Related UniProtKBP0A6R0
[5]
PubMed ID11502177
JournalBiochemistry
Year2001
Volume40
Pages9836-45
AuthorsMcGuire KA, Siggaard-Andersen M, Bangera MG, Olsen JG, von Wettstein-Knowles P
Titlebeta-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
PubMed ID11152607
JournalJ Mol Biol
Year2001
Volume305
Pages491-503
AuthorsMoche M, Dehesh K, Edwards P, Lindqvist Y
TitleThe crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54 A resolution and its relationship to other condensing enzymes.
Related PDB1e5m
Related UniProtKBP73283
[7]
PubMed ID12196027
JournalBiochemistry
Year2002
Volume41
Pages10877-87
AuthorsWitkowski A, Joshi AK, Smith S
TitleMechanism of the beta-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase.
[8]
PubMed ID12837788
JournalJ Bacteriol
Year2003
Volume185
Pages4136-43
AuthorsPrice AC, Rock CO, White SW
TitleThe 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae.
Related PDB1ox0,1oxh
[9]
PubMed ID12866053
JournalProteins
Year2003
Volume52
Pages427-35
AuthorsDawe JH, Porter CT, Thornton JM, Tabor AB
TitleA template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes.
[10]
PubMed ID15286722
JournalNat Struct Mol Biol
Year2004
Volume11
Pages888-93
AuthorsKeatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM
TitleAn antibiotic factory caught in action.
Related PDB1tqy
[11]
PubMed ID15952903
JournalAnnu Rev Biochem
Year2005
Volume74
Pages791-831
AuthorsWhite SW, Zheng J, Zhang YM, Rock
TitleThe structural biology of type II fatty acid biosynthesis.
[12]
PubMed ID16356722
JournalTrends Biochem Sci
Year2005
Volume31
Pages64-71
AuthorsHaapalainen AM, Merilainen G, Wierenga RK
TitleThe thiolase superfamily: condensing enzymes with diverse reaction specificities.
[13]
PubMed ID16618705
JournalJ Biol Chem
Year2006
Volume281
Pages17390-9
AuthorsZhang YM, Hurlbert J, White SW, Rock CO
TitleRoles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae.
Related PDB2alm
[14]
PubMed ID16710421
JournalNature
Year2006
Volume441
Pages358-61
AuthorsWang J, Soisson SM, Young K, Shoop W, Kodali S, Galgoci A, Painter R, Parthasarathy G, Tang YS, Cummings R, Ha S, Dorso K, Motyl M, Jayasuriya H, Ondeyka J, Herath K, Zhang C, Hernandez L, Allocco J, Basilio A, Tormo JR, Genilloud O, Vicente F, Pelaez F, Colwell L, Lee SH, Michael B, Felcetto T, Gill C, Silver LL, Hermes JD, Bartizal K, Barrett J, Schmatz D, Becker JW, Cully D, Singh SB
TitlePlatensimycin is a selective FabF inhibitor with potent antibiotic properties.
Related PDB2gfv,2gfw,2gfx,2gfy
[15]
PubMed ID18453702
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Year2008
Volume64
Pages358-66
AuthorsBagautdinov B, Ukita Y, Miyano M, Kunishima N
TitleStructure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.
Related PDB1j3n
[16]
PubMed ID18824113
JournalMol Phylogenet Evol
Year2008
Volume49
Pages691-701
AuthorsJiang C, Kim SY, Suh DY
TitleDivergent evolution of the thiolase superfamily and chalcone synthase family.
[17]
PubMed ID19233644
JournalBioorg Med Chem Lett
Year2009
Volume19
Pages1623-7
AuthorsShen HC, Ding FX, Singh SB, Parthasarathy G, Soisson SM, Ha SN, Chen X, Kodali S, Wang J, Dorso K, Tata JR, Hammond ML, Maccoss M, Colletti SL
TitleSynthesis and biological evaluation of platensimycin analogs.
Related PDB3g0y,3g11
[18]
PubMed ID19581087
JournalBioorg Med Chem Lett
Year2009
Volume19
Pages4756-9
AuthorsSingh SB, Ondeyka JG, Herath KB, Zhang C, Jayasuriya H, Zink DL, Parthasarathy G, Becker JW, Wang J, Soisson SM
TitleIsolation, enzyme-bound structure and antibacterial activity of platencin A1 from Streptomyces platensis.
Related PDB3hnz,3ho2,3ho9,3i8p

comments
This enzyme belongs to thiolase superfamily (see [11] and [12]). This enzyme belongs to the subfamily of type I and type II of beta-ketoacyl-acyl-carrier protein synthase (KAS I & KAS II). This enzyme is KAS II, whereas the counterpart enzyme is KAS I (EC 2.3.1.41; D00824 in EzCatDB), with a similar catalytic site.
Moreover, its homologous enzymes, which belong to KAS III subfamily, use acetyl-CoA as primer substrate, instead of acyl-ACP (EC 2.3.1.180; D00825, D00826, D00867 in EzCatDB), unlike KAS I and KAS II.
According to the literatre, this enzyme catalyzes the following reactions:
(A) Transfer of acyl group from sulfur atom of acyl-ACP to catalytic cysteine (see [15]):
(A0) Lys335 modulates the activity of His303 and His340.
(A1) His340 (of 1b3n) may act as a general base to deprotonate the nucleophile, Cys163. (Helix dipole moment may also activate the cysteine sidechain.)
(A2) The activated thiol group of Cys163 makes a nucleophilic attack on the acyl group of acyl-ACP, leading to a transition-state (I00138). The oxyanion hole, composed of the mainchain amide groups of Cys163 and Phe400, stabilizes the negative charge of the oxyanion on the tetrahedral transition-state (I00138).
(A3) His303 may act as a general acid to protonate the leaving sulfur atom of ACP, generating an acyl group on Cys163 (I00139).
(B) Hydrolysis of carbon-carbon bond one of which is carboxyl carbon of malonyl-ACP,forming carbanion/enolate transition-state (I00134) (see [7] and [13]):
(B0) Lys335 modulates the activity of His303 and His340.
(B1) His303 acts as a general base to deprotonate a nearby water molecule to activate it.
(B2) The activated water makes a nucleophilic attack on the carboxyl carbon (C3), forming a tetrahedral transition-state (I00140).
(B3) The tetrahedral transition-state collapses, to form the carbanion/enolate transition-state (I00134) and to release bicarbonate. Here, His340 acts as a second oxyanion hole, to stabilize the negative charge on the enolate oxygen, which is generated during the formation of the carbanion at the C2 carbon of malonyl group (I00134).
(C) Transfer of acyl group from catalytic cysteine to carbanion on the transition-state (I00134):
(C0) Protonated His340 stabilizes the enol group of the transition-state (I00134).
(C1) The carbanion makes a nucleophilic attack on the acyl group of the intermediate (I00139), forming a tetrahedral transition-state (I00141). The oxyanion of the tetrahedral transition-state (I00141) is stabilized by the oxyanion hole composed of the mainchain amide groups of Cys163 and Phe400.
(C2) His340 may act as a general acid to protonate the leaving catalytic residue, Cys163.

createdupdated
2009-11-172012-07-24


Copyright: Nozomi Nagano, JST & CBRC-AIST
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