D00825
type: Enzyme
active site residues resources: Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme.
active site residues resources: Mechanism of chalcone synthase. pKa of the catalytic cysteine and the role of the conserved histidine in a plant polyketide synthase.
active site residues resources: 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.
active site residues resources: Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway.
active site residues resources: First X-ray cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling.
active site residues resources: Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity.
active site residues resources: Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A.
active site residues resources: Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus.
active site residues resources: Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates.
active site residues resources: Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
active site residues resources: O67185
active site residues resources: P0A6R0
active site residues resources: P43711
active site residues resources: Q6GIA4
active site residues resources: Q820T1
active site residues resources: Q8NXE2
cath: Peroxisomal Thiolase; Chain A, domain 1
ec: https://purl.uniprot.org/enzyme/2.3.1.180
kegg enzyme: Beta-ketoacyl-acyl-carrier-protein synthase III
kegg intermediate: Peptidyl-Cys-tetrahedral-acetyl-CoA
kegg intermediate: Peptidyl-Cys-S-acetyl
kegg intermediate: [Acyl-carrier protein]-decarboxylated malonyl group (Peptidyl-Ser-phosphopantetheine-S-enolate)
kegg intermediate: Peptidyl-Cys-tetrahedral-acetyl-keto-[acyl-carrier protein]
kegg pathway: Fatty acid biosynthesis
kegg product: acetoacetyl-[acyl-carrier protein]
kegg product: CoA
kegg product: CO2
kegg substrate: acetyl-CoA
kegg substrate: malonyl-[acyl-carrier protein]
pdb: 1d9bA01
pdb: 1d9bB01
pdb: 1eblA01
pdb: 1eblB01
pdb: 1hn9A01
pdb: 1hn9B01
pdb: 1hndA01
pdb: 1hnhA01
pdb: 1hnjA01
pdb: 1hnkA01
pdb: 1mzsA01
pdb: 2eftA01
pdb: 2eftB01
pdb: 2gyoA01
pdb: 2gyoB01
pdb: 3il9A01
pdb: 3il9B01
pdb: 3il3A01
pdb: 3il7A01
pdb: 3il7B01
pdb: 1zowA01
pdb: 1zowB01
pdb: 1zowC01
pdb: 1zowD01
pdb: 1d9bA02
pdb: 1d9bB02
pdb: 1eblA02
pdb: 1eblB02
pdb: 1hn9A02
pdb: 1hn9B02
pdb: 1hndA02
pdb: 1hnhA02
pdb: 1hnjA02
pdb: 1hnkA02
pdb: 1mzsA02
pdb: 2eftA02
pdb: 2eftB02
pdb: 2gyoA02
pdb: 2gyoB02
pdb: 3il9A02
pdb: 3il9B02
pdb: 3il3A02
pdb: 3il7A02
pdb: 3il7B02
pdb: 1zowA02
pdb: 1zowB02
pdb: 1zowC02
pdb: 1zowD02
rlcp: p38
rlcp: p66

Peroxisomal Thiolase; Chain A, domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.47.10

Fatty acid biosynthesis
type: KeggPathway
references: KEGG:MAP00061

The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.
type: BibliographicResource
authors:
  item: Olsen JG
  item: Kadziola A
  item: von Wettstein-Knowles P
  item: Siggaard-Andersen M
  item: Lindquist Y
  item: Larsen S
journal: FEBS Lett
pages: 46-52
published year: 1999
volume: 460
references: http://www.ncbi.nlm.nih.gov/pubmed/10571059
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A953
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes.
type: BibliographicResource
authors:
  item: Dawe JH
  item: Porter CT
  item: Thornton JM
  item: Tabor AB
journal: Proteins
pages: 427-35
published year: 2003
volume: 52
references: http://www.ncbi.nlm.nih.gov/pubmed/12866053

The structural biology of type II fatty acid biosynthesis.
type: BibliographicResource
authors:
  item: White SW
  item: Zheng J
  item: Zhang YM
  item: Rock
journal: Annu Rev Biochem
pages: 791-831
published year: 2005
volume: 74
references: http://www.ncbi.nlm.nih.gov/pubmed/15952903

The thiolase superfamily: condensing enzymes with diverse reaction specificities.
type: BibliographicResource
authors:
  item: Haapalainen AM
  item: Merilainen G
  item: Wierenga RK
journal: Trends Biochem Sci
pages: 64-71
published year: 2005
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/16356722

Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes.
type: BibliographicResource
authors:
  item: Alhamadsheh MM
  item: Musayev F
  item: Komissarov AA
  item: Sachdeva S
  item: Wright HT
  item: Scarsdale N
  item: Florova G
  item: Reynolds KA
journal: Chem Biol
pages: 513-24
published year: 2007
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/17524982
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis.
type: BibliographicResource
authors:
  item: Qiu X
  item: Janson CA
  item: Konstantinidis AK
  item: Nwagwu S
  item: Silverman C
  item: Smith WW
  item: Khandekar S
  item: Lonsdale J
  item: Abdel-Meguid SS
journal: J Biol Chem
pages: 36465-71
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/10593943
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A6R0
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH.
type: BibliographicResource
authors:
  item: Sachdeva S
  item: Musayev FN
  item: Alhamadsheh MM
  item: Scarsdale JN
  item: Wright HT
  item: Reynolds KA
journal: Chem Biol
pages: 402-12
published year: 2008
volume: 15
references: http://www.ncbi.nlm.nih.gov/pubmed/18420147
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Divergent evolution of the thiolase superfamily and chalcone synthase family.
type: BibliographicResource
authors:
  item: Jiang C
  item: Kim SY
  item: Suh DY
journal: Mol Phylogenet Evol
pages: 691-701
published year: 2008
volume: 49
references: http://www.ncbi.nlm.nih.gov/pubmed/18824113

The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
type: BibliographicResource
authors:
  item: Davies C
  item: Heath RJ
  item: White SW
  item: Rock CO
journal: Structure
pages: 185-95
published year: 2000
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/10673437
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A6R0
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III.
type: BibliographicResource
authors:
  item: Scarsdale JN
  item: Kazanina G
  item: He X
  item: Reynolds KA
  item: Wright HT
journal: J Biol Chem
pages: 20516-22
published year: 2001
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/11278743
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A574
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III.
type: BibliographicResource
authors:
  item: Zhang YM
  item: Rao MS
  item: Heath RJ
  item: Price AC
  item: Olson AJ
  item: Rock CO
  item: White SW
journal: J Biol Chem
pages: 8231-8
published year: 2001
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/11078736

Refined structures of beta-ketoacyl-acyl carrier protein synthase III.
type: BibliographicResource
authors:
  item: Qiu X
  item: Janson CA
  item: Smith WW
  item: Head M
  item: Lonsdale J
  item: Konstantinidis AK
journal: J Mol Biol
pages: 341-56
published year: 2001
volume: 307
references: http://www.ncbi.nlm.nih.gov/pubmed/11243824
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A6R0
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway.
type: BibliographicResource
authors:
  item: Pan H
  item: Tsai S
  item: Meadows ES
  item: Miercke LJ
  item: Keatinge-Clay AT
  item: O'Connell J
  item: Khosla C
  item: Stroud RM
journal: Structure
pages: 1559-68
published year: 2002
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/12429097
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q9F6D4
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

First X-ray cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling.
type: BibliographicResource
authors:
  item: Daines RA
  item: Khandekar SS
  item: Silverman C
  item: Head MS
  item: Pendrak I
  item: Sham K
  item: Van Aller GS
  item: Konstantinidis AK
  item: Lonsdale JT
  item: Janson CA
  item: Qiu X
  item: Brandt M
journal: J Med Chem
pages: 5-8
published year: 2003
volume: 46
references: http://www.ncbi.nlm.nih.gov/pubmed/12502353
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity.
type: BibliographicResource
authors:
  item: Brown AK
  item: Sridharan S
  item: Kremer L
  item: Lindenberg S
  item: Dover LG
  item: Sacchettini JC
  item: Besra GS
journal: J Biol Chem
pages: 32539-47
published year: 2005
volume: 280
references: http://www.ncbi.nlm.nih.gov/pubmed/16040614
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A.
type: BibliographicResource
authors:
  item: Musayev F
  item: Sachdeva S
  item: Scarsdale JN
  item: Reynolds KA
  item: Wright HT
journal: J Mol Biol
pages: 1313-21
published year: 2005
volume: 346
references: http://www.ncbi.nlm.nih.gov/pubmed/15713483
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus.
type: BibliographicResource
authors:
  item: Qiu X
  item: Choudhry AE
  item: Janson CA
  item: Grooms M
  item: Daines RA
  item: Lonsdale JT
  item: Khandekar SS
journal: Protein Sci
pages: 2087-94
published year: 2005
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/15987898
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates.
type: BibliographicResource
authors:
  item: Sachdeva S
  item: Musayev F
  item: Alhamadsheh MM
  item: Neel Scarsdale J
  item: Tonie Wright H
  item: Reynolds KA
journal: Bioorg Chem
pages: 85-90
published year: 2008
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/18096200

Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
type: BibliographicResource
authors:
  item: Gajiwala KS
  item: Margosiak S
  item: Lu J
  item: Cortez J
  item: Su Y
  item: Nie Z
  item: Appelt K
journal: FEBS Lett
pages: 2939-46
published year: 2009
volume: 583
references: http://www.ncbi.nlm.nih.gov/pubmed/19665020
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme.
type: BibliographicResource
authors:
  item: Abbadi A
  item: Brummel M
  item: Schutt BS
  item: Slabaugh MB
  item: Schuch R
  item: Spener F
journal: Biochem J
pages: 153-60
published year: 2000
volume: 345 Pt 1
references: http://www.ncbi.nlm.nih.gov/pubmed/10600651

Mechanism of chalcone synthase. pKa of the catalytic cysteine and the role of the conserved histidine in a plant polyketide synthase.
type: BibliographicResource
authors:
  item: Jez JM
  item: Noel JP
journal: J Biol Chem
pages: 39640-6
published year: 2000
volume: 275
references: http://www.ncbi.nlm.nih.gov/pubmed/11006298

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.
type: BibliographicResource
authors:
  item: McGuire KA
  item: Siggaard-Andersen M
  item: Bangera MG
  item: Olsen JG
  item: von Wettstein-Knowles P
journal: Biochemistry
pages: 9836-45
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11502177

1eblA01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1ebl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebl

1eblB01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1ebl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebl

1hndA01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1hnd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hnd

1hnhA01
type: Pdb
catalytic residue: ;ASP 140
main chain in catalysis: SCY 112
modified residue: SCY 112(S-acetyl-cysteine)
references: 1hnh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hnh

1hnjA01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1hnj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hnj

2eftA01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 2eft
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2eft

2gyoA01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 2gyo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gyo

1d9bA01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1d9b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d9b

1d9bA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1d9b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d9b

1d9bB01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1d9b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d9b

1d9bB02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1d9b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d9b

1eblA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1ebl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebl

1eblB02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1ebl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ebl

1hn9A01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1hn9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hn9

1hn9A02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1hn9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hn9

1hn9B01
type: Pdb
catalytic residue: CYS 1112;ASP 1140
main chain in catalysis: CYS 1112
references: 1hn9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hn9

1hn9B02
type: Pdb
catalytic residue: HIS 1244;ASN 1274;SER 1276
main chain in catalysis: GLY 1306
references: 1hn9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hn9

1hndA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1hnd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hnd

1hnhA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1hnh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hnh

1hnjA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1hnj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hnj

1hnkA01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1hnk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hnk
comment: invisible 84-86, 146-152

1hnkA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
references: 1hnk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hnk
comment: invisible 185-217, 305-307

1mzsA01
type: Pdb
catalytic residue: ;ASP 140
main chain in catalysis: OCS 112
modified residue: OCS 112(sulfinocysteine)
references: 1mzs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mzs

1mzsA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 1mzs
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1mzs

1zowA01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1zow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zow

1zowA02
type: Pdb
catalytic residue: HIS 238;ASN 268;SER 270
main chain in catalysis: GLY 300
references: 1zow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zow

1zowB01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1zow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zow

1zowB02
type: Pdb
catalytic residue: HIS 238;ASN 268;SER 270
main chain in catalysis: GLY 300
references: 1zow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zow

1zowC01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1zow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zow

1zowC02
type: Pdb
catalytic residue: HIS 238;ASN 268;SER 270
main chain in catalysis: GLY 300
references: 1zow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zow

1zowD01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 1zow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zow

1zowD02
type: Pdb
catalytic residue: HIS 238;ASN 268;SER 270
main chain in catalysis: GLY 300
references: 1zow
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zow

2eftA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 2eft
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2eft

2eftB01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 2eft
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2eft

2eftB02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 2eft
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2eft

2gyoA02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 2gyo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gyo

2gyoB01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 2gyo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gyo

2gyoB02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 2gyo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2gyo

3il3A01
type: Pdb
catalytic residue: ;ASP 140
main chain in catalysis: SCY 112
modified residue: SCY 112(S-acetyl-cysteine)
references: 3il3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il3

3il3A02
type: Pdb
catalytic residue: HIS 243;ASN 273;SER 275
main chain in catalysis: GLY 305
references: 3il3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il3

3il7A01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 3il7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il7

3il7A02
type: Pdb
catalytic residue: HIS 238;ASN 268;SER 270
main chain in catalysis: GLY 300
references: 3il7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il7

3il7B01
type: Pdb
catalytic residue: CYS 112;ASP 140
main chain in catalysis: CYS 112
references: 3il7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il7

3il7B02
type: Pdb
catalytic residue: HIS 238;ASN 268;SER 270
main chain in catalysis: GLY 300
references: 3il7
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il7

3il9A01
type: Pdb
catalytic residue: ;ASP 140
main chain in catalysis: CSW 112
modified residue: CSW 112(cystein-S-dioxide)
references: 3il9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il9

3il9A02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 3il9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il9

3il9B01
type: Pdb
catalytic residue: ;ASP 140
main chain in catalysis: CSW 112
modified residue: CSW 112(cystein-S-dioxide)
references: 3il9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il9

3il9B02
type: Pdb
catalytic residue: HIS 244;ASN 274;SER 276
main chain in catalysis: GLY 306
references: 3il9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3il9

CoA
type: KeggProduct
compound type: amine group
compound type: carbohydrate
compound type: nucleotide
compound type: peptide/protein
compound type: sulfhydryl group
references: KEGG:C00010
references: CHEBI:15346
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

CO2
type: KeggProduct
compound type: others
references: KEGG:C00011
references: CHEBI:16526
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

acetyl-CoA
type: KeggSubstrate
compound type: amine group
compound type: carbohydrate
compound type: nucleotide
compound type: peptide/protein
compound type: sulfide group
references: KEGG:C00024
references: CHEBI:15351
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

malonyl-[acyl-carrier protein]
type: KeggSubstrate
compound type: carbohydrate
compound type: carboxyl group
compound type: peptide/protein
compound type: phosphate group/phosphate ion
compound type: sulfide group
references: KEGG:C01209

acetoacetyl-[acyl-carrier protein]
type: KeggProduct
compound type: carbohydrate
compound type: peptide/protein
compound type: phosphate group/phosphate ion
compound type: sulfide group
references: KEGG:C05744

Peptidyl-Cys-tetrahedral-acetyl-CoA
type: KeggIntermediate
references: KEGG:I00132

Peptidyl-Cys-S-acetyl
type: KeggIntermediate
references: KEGG:I00133

[Acyl-carrier protein]-decarboxylated malonyl group (Peptidyl-Ser-phosphopantetheine-S-enolate)
type: KeggIntermediate
references: KEGG:I00134

Peptidyl-Cys-tetrahedral-acetyl-keto-[acyl-carrier protein]
type: KeggIntermediate
references: KEGG:I00135

3-Oxoacyl:ACP synthase III
type: KeggEnzyme

3-Ketoacyl-acyl carrier protein synthase III
type: KeggEnzyme

KASIII
type: KeggEnzyme

KAS III
type: KeggEnzyme

FabH
type: KeggEnzyme

Beta-ketoacyl-acyl carrier protein synthase III
type: KeggEnzyme

Beta-ketoacyl-ACP synthase III
type: KeggEnzyme

Beta-ketoacyl (acyl carrier protein) synthase III
type: KeggEnzyme

Beta-ketoacyl-[acyl-carrier-protein] synthase III
type: KeggEnzyme

Acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase
type: KeggEnzyme

IntermediateBound
compound: Peptidyl-Cys-S-acetyl
ligand het code: SCY
pdb: 1hnhA01

IntermediateAnalogue
compound: Peptidyl-Cys-S-acetyl
ligand het code: MEE-CYS_112
pdb: 2eftA01

IntermediateAnalogue
compound: Peptidyl-Cys-S-acetyl
ligand het code: MEE-CYS_112
pdb: 2gyoA01

IntermediateAnalogue
compound: Peptidyl-Cys-S-acetyl
ligand het code: CSW
pdb: 3il9A01

IntermediateBound
compound: Peptidyl-Cys-S-acetyl
ligand het code: SCY
pdb: 3il3A01

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.6A, p.36467-36470

ReferenceForCatalyticMechanism
reference index: 3
reference section: Scheme 1, p.158-160

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.7b, 3p.190-192

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.349-352

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.1561-1565

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.6b, p.806-809

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig.6, p.32544-32547

ReferenceForCatalyticMechanism
reference index: 15
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 18
reference section: Fig.1B

ReferenceForCatalyticMechanism
reference index: 21
reference section: Fig.5, p.696-697