DB code: D00871

RLCP classification 3.1177.220085.58 : Transfer
1.51.790.101 : Hydrolysis
3.1197.15025.150 : Transfer
CATH domain 3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1 Catalytic domain
3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1 Catalytic domain
E.C. 2.3.1.179
CSA 1kas
M-CSA 1kas
MACiE

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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0AAI5 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
KAS II
NP_415613.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489363.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]
Q6G441 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
YP_033372.1 (Protein)
NC_005956.1 (DNA/RNA sequence)
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]
Q8YFP7 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
NP_540390.1 (Protein)
NC_003317.1 (DNA/RNA sequence)
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]
A4JL30 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
YP_001116448.1 (Protein)
NC_009255.1 (DNA/RNA sequence)
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]
P73283 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
KAS II
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)
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]
Q5SL80 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
YP_143679.1 (Protein)
NC_006461.1 (DNA/RNA sequence)
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]
Q8NXE1 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
KAS II
NP_645683.1 (Protein)
NC_003923.1 (DNA/RNA sequence)
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]
Q8Y574 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
NP_465725.1 (Protein)
NC_003210.1 (DNA/RNA sequence)
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]
Q9FBC2 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC 2.3.1.179
PF00109 (ketoacyl-synt)
PF02801 (Ketoacyl-synt_C)
[Graphical View]

KEGG enzyme name
beta-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)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0AAI5 FABF_ECOLI (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. Homodimer.
Q6G441 Q6G441_BARHE
Q8YFP7 Q8YFP7_BRUME (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
A4JL30 A4JL30_BURVG (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
P73283 FABF_SYNY3 (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. Homodimer.
Q5SL80 Q5SL80_THET8
Q8NXE1 FABF_STAAW (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
Q8Y574 Q8Y574_LISMO (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
Q9FBC2 Q9FBC2_STRPN

KEGG Pathways
Map code Pathways E.C.
MAP00061 Fatty acid biosynthesis

Compound table
Substrates Products Intermediates
KEGG-id C01209 L00039 C00001 C00288 C00229 L00040 I00138 I00139 I00140 I00134 I00141
E.C.
Compound malonyl-[acyl-carrier-protein] (Z)-hexadec-11-enoyl-[acyl-carrier protein] H2O Bicabonate(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]
Type carbohydrate,carboxyl group,peptide/protein,phosphate group/phosphate ion,sulfide group carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group H2O carboxyl group carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfhydryl group carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group
ChEBI 15377
15377
17544
17544
PubChem 22247451
962
22247451
962
22647601
769
22647601
769
1b3nA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:CER
1kas001 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gfvA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gfwA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gfxA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gfyA01 Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:DAO Unbound Unbound Unbound
3g0yA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3g11A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3hnzA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3ho2A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3ho9A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3i8pA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3e60A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3e60B01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3kzuA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3kzuB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3kzuC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4ddoA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4f32A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4f32B01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1e5mA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1j3nA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1j3nB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gqdA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gqdB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3o04A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ox0A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxhA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxhB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxhC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxhD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2almA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2rjtA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2rjtB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2rjtC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2rjtD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b3nA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kas002 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gfvA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gfwA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gfxA02 Analogue:PMN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gfyA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3g0yA02 Analogue:P9A Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3g11A02 Analogue:P9C Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3hnzA02 Analogue:PMN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3ho2A02 Analogue:N32 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3ho9A02 Analogue:N3A Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3i8pA02 Analogue:840 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3e60A02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3e60B02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3kzuA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3kzuB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3kzuC02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4ddoA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4f32A02 Analogue:N32 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4f32B02 Analogue:N32 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1e5mA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1j3nA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1j3nB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gqdA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2gqdB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3o04A02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ox0A02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxhA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxhB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxhC02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxhD02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2almA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2rjtA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2rjtB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2rjtC02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2rjtD02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [1], [8], [10], [13], [14], [15], [16], [17], [20], [24], [30] [31] & CSA;1dd8

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1b3nA01 CYS 163 CYS 163
1kas001 CYS 163 CYS 163
2gfvA01 mutant C163Q
2gfwA01 CYS 163 CYS 163
2gfxA01 mutant C163Q
2gfyA01 CYS 163 CYS 163
3g0yA01 mutant C163Q
3g11A01 mutant C163Q
3hnzA01 mutant C163A
3ho2A01 mutant C163A
3ho9A01 mutant C163A
3i8pA01 mutant C163A
3e60A01 CYS 170 CYS 170
3e60B01 CYS 170 CYS 170
3kzuA01 CYS 170 CYS 170
3kzuB01 CYS 170 CYS 170
3kzuC01 CYS 170 CYS 170
4ddoA01 CYS 172 CYS 172
4f32A01 CSU 172(Cysteine-S-Sulfonic acid) CSU 172
4f32B01 CSU 172(Cysteine-S-Sulfonic acid) CSU 172
1e5mA01 CYS 167 CYS 167
1j3nA01 CYS 161 CYS 161
1j3nB01 CYS 161 CYS 161
2gqdA01 CYS 165 CYS 165
2gqdB01 CYS 165 CYS 165
3o04A01 CYS 164 CYS 164
1ox0A01 CYS 164 CYS 164
1oxhA01 CYS 164 CYS 164
1oxhB01 CYS 164 CYS 164
1oxhC01 CYS 164 CYS 164
1oxhD01 CYS 164 CYS 164
2almA01 CYS 164 CYS 164
2rjtA01 CYS 164 CYS 164
2rjtB01 CYS 164 CYS 164
2rjtC01 CYS 164 CYS 164
2rjtD01 CYS 164 CYS 164
1b3nA02 HIS 303;LYS 335;HIS 340 PHE 400
1kas002 HIS 303;LYS 335;HIS 340 PHE 400
2gfvA02 HIS 303;LYS 335;HIS 340 PHE 400
2gfwA02 HIS 303;LYS 335;HIS 340 PHE 400
2gfxA02 HIS 303;LYS 335;HIS 340 PHE 400
2gfyA02 HIS 303;;HIS 340 PHE 400 mutant K335A
3g0yA02 HIS 303;LYS 335;HIS 340 PHE 400
3g11A02 HIS 303;LYS 335;HIS 340 PHE 400
3hnzA02 HIS 303;LYS 335;HIS 340 PHE 400
3ho2A02 HIS 303;LYS 335;HIS 340 PHE 400
3ho9A02 HIS 303;LYS 335;HIS 340 PHE 400
3i8pA02 HIS 303;LYS 335;HIS 340 PHE 400
3e60A02 HIS 311;LYS 342;HIS 347 PHE 406
3e60B02 HIS 311;LYS 342;HIS 347 PHE 406
3kzuA02 HIS 311;LYS 342;HIS 347 PHE 406
3kzuB02 HIS 311;LYS 342;HIS 347 PHE 406
3kzuC02 HIS 311;LYS 342;HIS 347 PHE 406
4ddoA02 HIS 313;LYS 344;HIS 349 PHE 409
4f32A02 HIS 313;LYS 344;HIS 349 PHE 409
4f32B02 HIS 313;LYS 344;HIS 349 PHE 409
1e5mA02 HIS 307;LYS 339;HIS 344 PHE 403
1j3nA02 HIS 301;LYS 333;HIS 338 PHE 396
1j3nB02 HIS 301;LYS 333;HIS 338 PHE 396
2gqdA02 HIS 304;LYS 336;HIS 341 PHE 400
2gqdB02 HIS 304;LYS 336;HIS 341 PHE 400
3o04A02 HIS 303;LYS 335;HIS 340 PHE 399
1ox0A02 HIS 303;LYS 332;HIS 337 PHE 396
1oxhA02 HIS 303;LYS 332;HIS 337 PHE 396
1oxhB02 HIS 303;LYS 332;HIS 337 PHE 396
1oxhC02 HIS 303;LYS 332;HIS 337 PHE 396
1oxhD02 HIS 303;LYS 332;HIS 337 PHE 396
2almA02 ;LYS 332;HIS 337 PHE 396 mutant H303A, G379A
2rjtA02 HIS 303;LYS 332;HIS 337 PHE 396 mutant E22A, E94A, E325A, E383A, E409A
2rjtB02 HIS 303;LYS 332;HIS 337 PHE 396 mutant E22A, E94A, E325A, E383A, E409A
2rjtC02 HIS 303;LYS 332;HIS 337 PHE 396 mutant E22A, E94A, E325A, E383A, E409A
2rjtD02 HIS 303;LYS 332;HIS 337 PHE 396 mutant E22A, E94A, E325A, E383A, E409A

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID
PubMed ID 9482715
Journal EMBO J
Year 1998
Volume 17
Pages 1183-91
Authors Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y
Title Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.
Related PDB 1kas
Related UniProtKB P0AAI5
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
Medline ID
PubMed ID 10037680
Journal J Biol Chem
Year 1999
Volume 274
Pages 6031-4
Authors Moche M, Schneider G, Edwards P, Dehesh K, Lindqvist Y
Title Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.
Related PDB 1b3n
Related UniProtKB P0AAI5
[3]
Resource
Comments
Medline ID
PubMed ID 11171140
Journal Biochem Soc Trans
Year 2000
Volume 28
Pages 601-7
Authors von Wettstein-Knowles P, Olsen J, Arnvig Mcguire K, Larsen S
Title Molecular aspects of beta-ketoacyl synthase (KAS) catalysis.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID
PubMed ID 10673437
Journal Structure
Year 2000
Volume 8
Pages 185-95
Authors Davies C, Heath RJ, White SW, Rock CO
Title The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Related PDB 1ebl
Related UniProtKB P0A6R0
[5]
Resource
Comments
Medline ID
PubMed ID 11502177
Journal Biochemistry
Year 2001
Volume 40
Pages 9836-45
Authors McGuire KA, Siggaard-Andersen M, Bangera MG, Olsen JG, von Wettstein-Knowles P
Title beta-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
Medline ID
PubMed ID 11152607
Journal J Mol Biol
Year 2001
Volume 305
Pages 491-503
Authors Moche M, Dehesh K, Edwards P, Lindqvist Y
Title The 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 PDB 1e5m
Related UniProtKB P73283
[7]
Resource
Comments
Medline ID
PubMed ID 12196027
Journal Biochemistry
Year 2002
Volume 41
Pages 10877-87
Authors Witkowski A, Joshi AK, Smith S
Title Mechanism of the beta-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12837788
Journal J Bacteriol
Year 2003
Volume 185
Pages 4136-43
Authors Price AC, Rock CO, White SW
Title The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae.
Related PDB 1ox0 1oxh
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 12866053
Journal Proteins
Year 2003
Volume 52
Pages 427-35
Authors Dawe JH, Porter CT, Thornton JM, Tabor AB
Title A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 15286722
Journal Nat Struct Mol Biol
Year 2004
Volume 11
Pages 888-93
Authors Keatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM
Title An antibiotic factory caught in action.
Related PDB 1tqy
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 15952903
Journal Annu Rev Biochem
Year 2005
Volume 74
Pages 791-831
Authors White SW, Zheng J, Zhang YM, Rock
Title The structural biology of type II fatty acid biosynthesis.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 16356722
Journal Trends Biochem Sci
Year 2005
Volume 31
Pages 64-71
Authors Haapalainen AM, Merilainen G, Wierenga RK
Title The thiolase superfamily: condensing enzymes with diverse reaction specificities.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 16618705
Journal J Biol Chem
Year 2006
Volume 281
Pages 17390-9
Authors Zhang YM, Hurlbert J, White SW, Rock CO
Title Roles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae.
Related PDB 2alm
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 16710421
Journal Nature
Year 2006
Volume 441
Pages 358-61
Authors Wang 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
Title Platensimycin is a selective FabF inhibitor with potent antibiotic properties.
Related PDB 2gfv 2gfw 2gfx 2gfy
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 18453702
Journal Acta Crystallogr Sect F Struct Biol Cryst Commun
Year 2008
Volume 64
Pages 358-66
Authors Bagautdinov B, Ukita Y, Miyano M, Kunishima N
Title Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.
Related PDB 1j3n
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 18824113
Journal Mol Phylogenet Evol
Year 2008
Volume 49
Pages 691-701
Authors Jiang C, Kim SY, Suh DY
Title Divergent evolution of the thiolase superfamily and chalcone synthase family.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 19233644
Journal Bioorg Med Chem Lett
Year 2009
Volume 19
Pages 1623-7
Authors Shen 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
Title Synthesis and biological evaluation of platensimycin analogs.
Related PDB 3g0y 3g11
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 19581087
Journal Bioorg Med Chem Lett
Year 2009
Volume 19
Pages 4756-9
Authors Singh SB, Ondeyka JG, Herath KB, Zhang C, Jayasuriya H, Zink DL, Parthasarathy G, Becker JW, Wang J, Soisson SM
Title Isolation, enzyme-bound structure and antibacterial activity of platencin A1 from Streptomyces platensis.
Related PDB 3hnz 3ho2 3ho9 3i8p
Related UniProtKB

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.

Created Updated
2009-11-17 2012-07-24