DB code: D00826
| RLCP classification | 3.1177.220080.38 : Transfer | |
|---|---|---|
| 5.115.129300.66 : Elimination | ||
| 3.1197.15020.136 : 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. | 2.3.1.180 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.40.47.10 : Peroxisomal Thiolase; Chain A, domain 1 | D00090 D00411 D00509 D00825 D00867 D00871 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0A574 |
3-oxoacyl-[acyl-carrier-protein] synthase 3
|
EC
2.3.1.180
3-oxoacyl-[acyl-carrier-protein] synthase III Beta-ketoacyl-ACP synthase III KAS III MtFabH |
NP_215047.1
(Protein)
NC_000962.3 (DNA/RNA sequence) NP_334966.1 (Protein) NC_002755.2 (DNA/RNA sequence) YP_006513866.1 (Protein) NC_018143.1 (DNA/RNA sequence) |
PF08545
(ACP_syn_III)
PF08541 (ACP_syn_III_C) [Graphical View] |
| Q7SI99 |
3-oxoacyl-[acyl-carrier-protein] synthase 3
|
EC
2.3.1.180
3-oxoacyl-[acyl-carrier-protein] synthase III Beta-ketoacyl-ACP synthase III |
PF08545
(ACP_syn_III)
PF08541 (ACP_syn_III_C) [Graphical View] |
|
| Q9F6D4 |
3-oxoacyl-[acyl-carrier-protein] synthase 3
|
EC
2.3.1.180
3-oxoacyl-[acyl-carrier-protein] synthase III Beta-ketoacyl-ACP synthase III KAS III |
PF08545
(ACP_syn_III)
PF08541 (ACP_syn_III_C) [Graphical View] |
| KEGG enzyme name |
|---|
|
Beta-ketoacyl-acyl-carrier-protein synthase III
3-Oxoacyl:ACP synthase III 3-Ketoacyl-acyl carrier protein synthase III KASIII KAS III FabH Beta-ketoacyl-acyl carrier protein synthase III Beta-ketoacyl-ACP synthase III Beta-ketoacyl (acyl carrier protein) synthase III Beta-ketoacyl-[acyl-carrier-protein] synthase III Acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0A574 | FABH_MYCTU | Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO(2). | Homodimer. | Cytoplasm. | |
| Q7SI99 | Q7SI99_THETH | Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO(2). | Homodimer (By similarity). | Cytoplasm (By similarity). | |
| Q9F6D4 | FABH_STRLI | Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO(2). | Homodimer. | Cytoplasm (Probable). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00061 | Fatty acid biosynthesis |
| Compound table | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||||||
| KEGG-id | C00024 | C01209 | C05744 | C00010 | C00011 | I00132 | I00133 | I00134 | I00135 | |||||
| E.C. | ||||||||||||||
| Compound | acetyl-CoA | malonyl-[acyl-carrier protein] | acetoacetyl-[acyl-carrier protein] | CoA | CO2 | Peptidyl-Cys-tetrahedral-acetyl-CoA | Peptidyl-Cys-S-acetyl | [Acyl-carrier protein]-decarboxylated malonyl group (Peptidyl-Ser-phosphopantetheine-S-enolate) | Peptidyl-Cys-tetrahedral-acetyl-keto-[acyl-carrier protein] | |||||
| Type | amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group | carbohydrate,carboxyl group,peptide/protein,phosphate group/phosphate ion,sulfide group | carbohydrate,peptide/protein,phosphate group/phosphate ion,sulfide group | amine group,carbohydrate,nucleotide ,peptide/protein,sulfhydryl group | others | |||||||||
| ChEBI |
15351 15351 |
15346 15346 |
16526 16526 |
|||||||||||
| PubChem |
444493 6302 444493 6302 |
6816 87642 6816 87642 |
280 280 |
|||||||||||
| 1hzpA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1hzpB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1m1mA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1m1mB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1u6eA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1u6eB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1u6sA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1u6sB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2ahbA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2ahbB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2aj9A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2aj9B01 |
|
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qnxA01 |
|
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|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:MDX-CYS_112 | Unbound | Unbound |
| 2qnxB01 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:MDX-CYS_112 | Unbound | Unbound |
| 2qnyA01 |
|
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|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:DFD-CYS_112 | Unbound | Unbound |
| 2qnyB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:DFD-CYS_112 | Unbound | Unbound |
| 2qnzA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:DFD-CYS_112 | Unbound | Unbound |
| 2qnzB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:DFD-CYS_112 | Unbound | Unbound |
| 2qo0A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:D1T-CYS_112 | Unbound | Unbound |
| 2qo0B01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:D1T-CYS_112 | Unbound | Unbound |
| 2qo1A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:D1T-CYS_112 | Unbound | Unbound |
| 2qo1B01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:D1T-CYS_112 | Unbound | Unbound |
| 2qx1A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Bound:COA | Unbound | Unbound | Intermediate-analogue:D1T-CYS_112 | Unbound | Unbound |
| 2qx1B01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:D1T-CYS_112 | Unbound | Unbound |
| 1ub7A01 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ub7B01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ub7C01 |
|
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|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ub7D01 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1mzjA01 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:COA-ACE-CYS_121 | Unbound | Unbound | Unbound |
| 1mzjB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:COA-ACE-CYS_121 | Unbound | Unbound | Unbound |
| 1hzpA02 |
|
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|
|
Unbound | Analogue:DAO | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1hzpB02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1m1mA02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1m1mB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1u6eA02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1u6eB02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1u6sA02 |
|
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|
|
Analogue:DCC | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1u6sB02 |
|
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|
Analogue:DCC | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2ahbA02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2ahbB02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2aj9A02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2aj9B02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qnxA02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:UDT | Unbound |
| 2qnxB02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:UDT | Unbound |
| 2qnyA02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qnyB02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qnzA02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qnzB02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qo0A02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qo0B02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qo1A02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:VZZ | Unbound |
| 2qo1B02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:VZZ | Unbound |
| 2qx1A02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2qx1B02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ub7A02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ub7B02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ub7C02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ub7D02 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1mzjA02 |
|
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|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1mzjB02 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature [2], [3], [5], [9], [10], [13], [14], [15], [18], [21] & Swiss-prot;A5TZR3, P0A574, Q9F6D4 | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1hzpA01 |
|
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|
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|
CYS 112;GLU 140 | CYS 112 | |||
| 1hzpB01 |
|
|
|
|
|
CYS 112;GLU 140 | CYS 112 | |||
| 1m1mA01 |
|
|
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CYS 123;GLU 151 | CYS 123 | |||
| 1m1mB01 |
|
|
|
|
|
CYS 123;GLU 151 | CYS 123 | |||
| 1u6eA01 |
|
|
|
|
|
;GLU 140 | mutant C112A | |||
| 1u6eB01 |
|
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;GLU 140 | mutant C112A | |||
| 1u6sA01 |
|
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|
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;GLU 140 | mutant C112A | |||
| 1u6sB01 |
|
|
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;GLU 140 | mutant C112A | |||
| 2ahbA01 |
|
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CYS 122;GLU 150 | CYS 122 | mutant R46A, R161A | ||
| 2ahbB01 |
|
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CYS 122;GLU 150 | CYS 122 | mutant R46A, R161A | ||
| 2aj9A01 |
|
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|
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CYS 122;GLU 150 | CYS 122 | mutant W42A, R161A | ||
| 2aj9B01 |
|
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CYS 122;GLU 150 | CYS 122 | mutant W42A, R161A | ||
| 2qnxA01 |
|
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CYS 112;GLU 140 | CYS 112 | |||
| 2qnxB01 |
|
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CYS 112;GLU 140 | CYS 112 | |||
| 2qnyA01 |
|
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|
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CYS 112;GLU 140 | CYS 112 | |||
| 2qnyB01 |
|
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CYS 112;GLU 140 | CYS 112 | |||
| 2qnzA01 |
|
|
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|
|
CYS 112;GLU 140 | CYS 112 | |||
| 2qnzB01 |
|
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CYS 112;GLU 140 | CYS 112 | |||
| 2qo0A01 |
|
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CYS 112;GLU 140 | CYS 112 | |||
| 2qo0B01 |
|
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CYS 112;GLU 140 | CYS 112 | |||
| 2qo1A01 |
|
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CYS 112;GLU 140 | CYS 112 | |||
| 2qo1B01 |
|
|
|
|
|
CYS 112;GLU 140 | CYS 112 | |||
| 2qx1A01 |
|
|
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|
|
CYS 112;GLU 140 | CYS 112 | |||
| 2qx1B01 |
|
|
|
|
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CYS 112;GLU 140 | CYS 112 | |||
| 1ub7A01 |
|
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|
|
;GLU 138 | CSO 110(S-hydroxycystein) | CSO 110 | ||
| 1ub7B01 |
|
|
|
|
|
;GLU 138 | CSO 110(S-hydroxycystein) | CSO 110 | ||
| 1ub7C01 |
|
|
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|
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;GLU 138 | CSO 110(S-hydroxycystein) | CSO 110 | ||
| 1ub7D01 |
|
|
|
|
|
;GLU 138 | CSO 110(S-hydroxycystein) | CSO 110 | ||
| 1mzjA01 |
|
|
|
|
|
CYS 121;GLU 149 | CYS 121 | |||
| 1mzjB01 |
|
|
|
|
|
CYS 121;GLU 149 | CYS 121 | |||
| 1hzpA02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 1hzpB02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 1m1mA02 |
|
|
|
|
|
HIS 259;ASN 290;SER 292 | ALA 322 | |||
| 1m1mB02 |
|
|
|
|
|
HIS 259;ASN 290;SER 292 | ALA 322 | |||
| 1u6eA02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 1u6eB02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 1u6sA02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 1u6sB02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 2ahbA02 |
|
|
|
|
|
HIS 258;ASN 289;SER 291 | ALA 321 | |||
| 2ahbB02 |
|
|
|
|
|
HIS 258;ASN 289;SER 291 | ALA 321 | |||
| 2aj9A02 |
|
|
|
|
|
HIS 258;ASN 289;SER 291 | ALA 321 | |||
| 2aj9B02 |
|
|
|
|
|
HIS 258;ASN 289;SER 291 | ALA 321 | |||
| 2qnxA02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 2qnxB02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 2qnyA02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | mutant A246F | ||
| 2qnyB02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | mutant A246F | ||
| 2qnzA02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 2qnzB02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 2qo0A02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | mutant A246F | ||
| 2qo0B02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | mutant A246F | ||
| 2qo1A02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 2qo1B02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 2qx1A02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 2qx1B02 |
|
|
|
|
|
HIS 244;ASN 274;SER 276 | ALA 306 | |||
| 1ub7A02 |
|
|
|
|
|
HIS 246;ASN 276;SER 278 | ALA 308 | |||
| 1ub7B02 |
|
|
|
|
|
HIS 246;ASN 276;SER 278 | ALA 308 | |||
| 1ub7C02 |
|
|
|
|
|
HIS 246;ASN 276;SER 278 | ALA 308 | |||
| 1ub7D02 |
|
|
|
|
|
HIS 246;ASN 276;SER 278 | ALA 308 | |||
| 1mzjA02 |
|
|
|
|
|
HIS 257;ASN 288;SER 290 | ALA 320 | |||
| 1mzjB02 |
|
|
|
|
|
HIS 257;ASN 288;SER 290 | ALA 320 | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[2]
|
Fig.6A, p.36467-36470 | |
|
[3]
|
Scheme 1, p.158-160 | |
|
[5]
|
Fig.7b, 3p.190-192 | |
|
[9]
|
p.349-352 | |
|
[10]
|
p.1561-1565 | |
|
[13]
|
Fig.6b, p.806-809 | |
|
[14]
|
Fig.6, p.32544-32547 | |
|
[15]
|
Fig.1 | |
|
[18]
|
Fig.1B | |
|
[21]
|
Fig.5, p.696-697 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 10571059 |
| Journal | FEBS Lett |
| Year | 1999 |
| Volume | 460 |
| Pages | 46-52 |
| Authors | Olsen JG, Kadziola A, von Wettstein-Knowles P, Siggaard-Andersen M, Lindquist Y, Larsen S |
| Title | The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I. |
| Related PDB | 1dd8 |
| Related UniProtKB | P0A953 |
| [2] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 10593943 |
| Journal | J Biol Chem |
| Year | 1999 |
| Volume | 274 |
| Pages | 36465-71 |
| Authors | Qiu X, Janson CA, Konstantinidis AK, Nwagwu S, Silverman C, Smith WW, Khandekar S, Lonsdale J, Abdel-Meguid SS |
| Title |
Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. |
| Related PDB | 1d9b 1hn9 |
| Related UniProtKB | P0A6R0 |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10600651 |
| Journal | Biochem J |
| Year | 2000 |
| Volume | 345 Pt 1 |
| Pages | 153-60 |
| Authors | Abbadi A, Brummel M, Schutt BS, Slabaugh MB, Schuch R, Spener F |
| Title |
Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11006298 |
| Journal | J Biol Chem |
| Year | 2000 |
| Volume | 275 |
| Pages | 39640-6 |
| Authors | Jez JM, Noel JP |
| Title |
Mechanism of chalcone synthase. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| 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 |
| [6] | |
| 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 | |
| [7] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 11278743 |
| Journal | J Biol Chem |
| Year | 2001 |
| Volume | 276 |
| Pages | 20516-22 |
| Authors | Scarsdale JN, Kazanina G, He X, Reynolds KA, Wright HT |
| Title | Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III. |
| Related PDB | 1hzp |
| Related UniProtKB | P0A574 |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11078736 |
| Journal | J Biol Chem |
| Year | 2001 |
| Volume | 276 |
| Pages | 8231-8 |
| Authors | Zhang YM, Rao MS, Heath RJ, Price AC, Olson AJ, Rock CO, White SW |
| Title | Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 11243824 |
| Journal | J Mol Biol |
| Year | 2001 |
| Volume | 307 |
| Pages | 341-56 |
| Authors | Qiu X, Janson CA, Smith WW, Head M, Lonsdale J, Konstantinidis AK |
| Title | Refined structures of beta-ketoacyl-acyl carrier protein synthase III. |
| Related PDB | 1hnd 1hnh 1hnj 1hnk |
| Related UniProtKB | P0A6R0 |
| [10] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 12429097 |
| Journal | Structure |
| Year | 2002 |
| Volume | 10 |
| Pages | 1559-68 |
| Authors | Pan H, Tsai S, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM |
| Title | Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway. |
| Related PDB | 1mzj |
| Related UniProtKB | Q9F6D4 |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12502353 |
| Journal | J Med Chem |
| Year | 2003 |
| Volume | 46 |
| Pages | 5-8 |
| Authors | Daines RA, Pendrak I, Sham K, Van Aller GS, Konstantinidis AK, Lonsdale JT, Janson CA, Qiu X, Brandt M, Khandekar SS, Silverman C, Head MS |
| Title | First X-ray cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling. |
| Related PDB | 1mzs |
| Related UniProtKB | |
| [12] | |
| 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 | |
| [13] | |
| 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 | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 16040614 |
| Journal | J Biol Chem |
| Year | 2005 |
| Volume | 280 |
| Pages | 32539-47 |
| Authors | Brown AK, Sridharan S, Kremer L, Lindenberg S, Dover LG, Sacchettini JC, Besra GS |
| Title | Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. |
| Related PDB | 1m1m 2ahb 2aj9 |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15713483 |
| Journal | J Mol Biol |
| Year | 2005 |
| Volume | 346 |
| Pages | 1313-21 |
| Authors | Musayev F, Sachdeva S, Scarsdale JN, Reynolds KA, Wright HT |
| Title | Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A. |
| Related PDB | 1u6e 1u6s |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15987898 |
| Journal | Protein Sci |
| Year | 2005 |
| Volume | 14 |
| Pages | 2087-94 |
| Authors | Qiu X, Choudhry AE, Janson CA, Grooms M, Daines RA, Lonsdale JT, Khandekar SS |
| Title | Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus. |
| Related PDB | 1zow |
| Related UniProtKB | |
| [17] | |
| 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 | |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 17524982 |
| Journal | Chem Biol |
| Year | 2007 |
| Volume | 14 |
| Pages | 513-24 |
| Authors | Alhamadsheh MM, Musayev F, Komissarov AA, Sachdeva S, Wright HT, Scarsdale N, Florova G, Reynolds KA |
| Title | Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes. |
| Related PDB | 2eft 2gyo |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 18096200 |
| Journal | Bioorg Chem |
| Year | 2008 |
| Volume | 36 |
| Pages | 85-90 |
| Authors | Sachdeva S, Musayev F, Alhamadsheh MM, Neel Scarsdale J, Tonie Wright H, Reynolds KA |
| Title | Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 18420147 |
| Journal | Chem Biol |
| Year | 2008 |
| Volume | 15 |
| Pages | 402-12 |
| Authors | Sachdeva S, Musayev FN, Alhamadsheh MM, Scarsdale JN, Wright HT, Reynolds KA |
| Title | Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH. |
| Related PDB | 2qnz 2qny 2qnx 2qo0 2qo1 |
| Related UniProtKB | |
| [21] | |
| 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 | |
| [22] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 19665020 |
| Journal | FEBS Lett |
| Year | 2009 |
| Volume | 583 |
| Pages | 2939-46 |
| Authors | Gajiwala KS, Margosiak S, Lu J, Cortez J, Su Y, Nie Z, Appelt K |
| Title | Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme. |
| Related PDB | 3il3 3il4 3il5 3il6 3il7 3il9 |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to chalcone synthase family in thiolase superfamily (see [21]). According to the literature, According to the literature [2], (A) Transfer of acyl group from sulfur atom of acetyl-CoA to catalytic cysteine (see [9]): (A0) Asn274 (of 1hzp) modulate the pKa of His244, (A1) Glu140 (of 1hzp) acts as a general base to deprotonate the nucleophile, (A2) The activated thiol group of Cys112 makes a nucleophilic attack on the acetyl group of acetyl-CoA, (A3) His244 acts as a general acid to protonate the leaving sulfur atom of CoA, (B) Decarboxylation of malonyl-ACP (Elimination of carboxylate group from malonyl group) forming carbanion/enolate transition-state (I00134): (B0) Asn274 and His244 interact with the carbonyl oxygen of the second substrate, (B1) His244 may act as a general base to deprotonate the carboxylic group of malonyl-ACP, (C) Transfer of acetyl group from catalytic cysteine to carbanion on the transition-state (I00134): (C0) Asn274 and His244 stabilize the enol group of the transition-state (I00134). (C1) The carbanion makes a nucleophilic attack on the acetyl group of the acetyl intermediate (I00133), (C2) Glu140 may act as a general acid to protonate the leaving catalytic residue, |
| Created | Updated |
|---|---|
| 2009-11-26 | 2012-07-10 |