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MetaCyc Enzyme: KASI

Gene: fabB Accession Numbers: EG10274 (MetaCyc), b2323, ECK2317

Synonyms: fabC, β-ketoacyl-ACP synthase I, 3-oxoacyl-ACP-synthase I, KASI

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of KASI = [FabB]2

Summary:
There are three β-ketoacyl-ACP synthases (KAS) in E. coli: KASI, KASII and KASIII, encoded by fabB, fabF and fabH, respectively. All three are genetically and biochemically distinct. Each of the three enzymes is capable of initiating fatty acid biosynthesis.

KASI differs from the others in that it alone is required for the elongation of short-chain unsaturated acyl-ACP. It can catalyze all the condensation reactions of long chain fatty acid synthesis except the elongation of pamitoleoyl-ACP, and is also capable of initiating fatty acid synthesis in the absence of acetyl-ACP primer by the utilization of a side reaction involving malonyl-ACP decarboxylase [Garwin80, Jackowski89, Magnuson93].

FabB, along with FabA, is a key enzyme in unsaturated fatty acid biosynthesis. Data suggest that FabB pulls fatty acid biosynthesis in the direction of unsaturated fatty acid formation [Heath96] (see pathway cis-dodecenoyl biosynthesis). The importance of FabB in catalyzing the elongation of cis3-decenoyl-[acp] produced by FabA has been demonstrated in in vivo experiments [Feng09].

The enzyme is also involved in the elongation of 3-ketoglutaryl-[acp]-methyl-ester to pimeloyl-[acp]-methyl-ester, part of the biotin biosynthesis pathway [Lin10].

Functional FabB is composed of two identical subunits. The apparent molecular masses of the native enzyme and the subunit were determined by sedimentation equilibrium and SDS-PAGE, respectively [Garwin80].

The β-ketoacyl-ACP synthase (KAS) enzymes of the bacterial type II fatty acid biosynthesis pathway are of interest as drug targets. The antibiotic thiolactomycin has been shown to be a slow onset inhibitor of both the E. coli FabB acyl-enzyme intermediate, and that of its ortholog KasA in Mycobacterium tuberculosis [Machutta10]. Genetic evidence also suggested that FabB is an in vivo target for this antibiotic [Jackowski02]. Derivatives of thiolactomycin have been computationally assessed for improved inhibition [Steinbrecher12].

Crystal structures for the enzyme [Olsen99, Zhang01, vonWettsteinKno06], the enzyme complexed with fatty acids [Olsen01, vonWettsteinKno06] or inhibitors [Price01a, Kim06], and mutant enzymes [vonWettsteinKno06] have been reported.

In metabolic engineering studies aimed at biofuel production, overexpression of the fatty acid elongation cycle enzymes has been used to increase long-chain fatty acid synthesis in E. coli [Lee13, Jeon12, Yu11, Cao10]. Inclusion of the regulatory transcription factor FadR enhanced production and produced largest transcriptional changes in fabB, fabF, and accA [Zhang12].

Reviews: [White05], and Cronan, J.E. and C.O. Rock (2008) "Biosynthesis of Membrane Lipids" EcoSal 3.6.4 [ECOSAL]

Locations: cytosol

Map Position: [2,438,407 <- 2,439,627]

Molecular Weight of Polypeptide: 42.613 kD (from nucleotide sequence), 43.0 kD (experimental) [Garwin80 ]

Molecular Weight of Multimer: 80.0 kD (experimental) [Garwin80]

pI: 5.59

Unification Links: ASAP:ABE-0007675 , CGSC:798 , DIP:DIP-29379N , EchoBASE:EB0270 , EcoGene:EG10274 , EcoliWiki:b2323 , Mint:MINT-1235843 , ModBase:P0A953 , OU-Microarray:b2323 , PortEco:fabB , PR:PRO_000022560 , Pride:P0A953 , Protein Model Portal:P0A953 , RefSeq:NP_416826 , RegulonDB:EG10274 , SMR:P0A953 , String:511145.b2323 , UniProt:P0A953

Relationship Links: InterPro:IN-FAMILY:IPR014030 , InterPro:IN-FAMILY:IPR014031 , InterPro:IN-FAMILY:IPR016038 , InterPro:IN-FAMILY:IPR016039 , InterPro:IN-FAMILY:IPR018201 , PDB:Structure:1DD8 , PDB:Structure:1EK4 , PDB:Structure:1F91 , PDB:Structure:1FJ4 , PDB:Structure:1FJ8 , PDB:Structure:1G5X , PDB:Structure:1H4F , PDB:Structure:2AQ7 , PDB:Structure:2AQB , PDB:Structure:2BUH , PDB:Structure:2BUI , PDB:Structure:2BYW , PDB:Structure:2BYX , PDB:Structure:2BYY , PDB:Structure:2BYZ , PDB:Structure:2BZ3 , PDB:Structure:2BZ4 , PDB:Structure:2VB7 , PDB:Structure:2VB8 , PDB:Structure:2VB9 , PDB:Structure:2VBA , Pfam:IN-FAMILY:PF00109 , Pfam:IN-FAMILY:PF02801 , Prosite:IN-FAMILY:PS00606

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006633 - fatty acid biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11, Feng09, Jackowski02]
GO:0008610 - lipid biosynthetic process Inferred from experiment [Feng09]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0004315 - 3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from experiment Inferred by computational analysis [GOA01a, Garwin80]
GO:0042803 - protein homodimerization activity Inferred from experiment [Garwin80]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016746 - transferase activity, transferring acyl groups Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]

MultiFun Terms: metabolism biosynthesis of building blocks fatty acids and phosphatidic acid

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: β-ketoacyl [acyl-carrier protein] synthase (KASI)

EC Number: 2.3.1.41

an acyl-[acyl-carrier protein] + a malonyl-[acp] + H+ <=> a 3-oxoacyl-[acp] + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 3-oxo-pimeloyl-[acp] methyl ester synthase (KASI)

EC Number: 2.3.1.41

a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ <=> a 3-oxo-pimeloyl-[acp] methyl ester + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: biotin biosynthesis I , 8-amino-7-oxononanoate biosynthesis I

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 3-oxo-cis-Δ7-tetradecenoyl-[acp] synthase (KASI)

EC Number: 2.3.1.41

a cis5-dodecenoyl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxo-cis7-tetradecenoyl-[acp] + a holo-[acyl-carrier protein] + CO2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of unsaturated fatty acids biosynthesis (E. coli) , superpathway of fatty acids biosynthesis (E. coli) , palmitoleate biosynthesis I

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 3-oxo-cis-Δ9-hexadecenoyl-[acp] synthase (KASI)

EC Number: 2.3.1.41

a cis7-tetradecenoyl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxo-cis9-hexadecenoyl-[acp] + a holo-[acyl-carrier protein] + CO2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of unsaturated fatty acids biosynthesis (E. coli) , superpathway of fatty acids biosynthesis (E. coli) , palmitoleate biosynthesis I

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: β-ketodecanoyl-[acp] synthase (KASI)

EC Number: 2.3.1.41

an octanoyl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxo-decanoyl-[acp] + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of fatty acids biosynthesis (E. coli) , palmitate biosynthesis II (bacteria and plants)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: β-ketododecanoyl-[acp] synthase (KASI)

EC Number: 2.3.1.41

a decanoyl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxo-dodecanoyl-[acp] + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of fatty acids biosynthesis (E. coli) , palmitate biosynthesis II (bacteria and plants)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: β-ketomeristoyl-[acp] synthase (KASI)

EC Number: 2.3.1.41

a dodecanoyl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxo-myristoyl-[acp] + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of fatty acids biosynthesis (E. coli) , palmitate biosynthesis II (bacteria and plants)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
E. coli FabB was shown to have an absolute requirement for an ACP substrate as the acyl donor, whereas variation in the acceptor carrier substrate had little impact on the kinetics of the reaction [Borgaro11].

Kinetic parameters for this reaction were reported as follows: varying lauroyl-[acp] (dodecanoyl-[acp]) with fixed malonyl-[acp] gave a Km of 3.2 ± 0.5 μM and a kcat of 3.4 ± 0.2 min-1; varying malonyl-[acp] with fixed lauroyl-[acp] gave a Km of 11.5 ± 2.2 μM and a kcat of 6.6 ± 0.5 min-1 [Borgaro11].

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
a dodecanoyl-[acp]
3.2
0.057
[Borgaro11]
a malonyl-[acp]
11.5
0.11
[Borgaro11]


Enzymatic reaction of: β-ketopalmityl-[acp] synthase (KASI)

EC Number: 2.3.1.41

a myristoyl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxo-palmitoyl-[acp] + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of fatty acids biosynthesis (E. coli) , palmitate biosynthesis II (bacteria and plants)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: β-ketohexanoyl-[acp] synthase (KASI)

EC Number: 2.3.1.41

a butyryl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxo-hexanoyl-[acp] + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of fatty acids biosynthesis (E. coli) , palmitate biosynthesis II (bacteria and plants)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: β-ketooctanoyl-[acp] synthase (KASI)

EC Number: 2.3.1.41

a hexanoyl-[acyl-carrier-protein] + a malonyl-[acp] + H+ <=> a 3-oxo-octanoyl-[acp] + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of fatty acids biosynthesis (E. coli) , palmitate biosynthesis II (bacteria and plants)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: β-keto-cis5-dodecenoyl-[acp] synthase (KASI)

Synonyms: 3-oxoacyl-ACP-synthase, 3-oxoacyl-[acyl-carrier-protein]-synthase, acyl-[acyl carrier protein]:malonyl-[acyl carrier protein] C-acyltransferase (decarboxylating)

a cis3-decenoyl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxo-cis5-dodecenoyl-[acp] + a holo-[acyl-carrier protein] + CO2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: superpathway of fatty acid biosynthesis I (E. coli) , superpathway of fatty acids biosynthesis (E. coli) , superpathway of unsaturated fatty acids biosynthesis (E. coli) , cis-dodecenoyl biosynthesis

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: acetoacetyl-[acp] synthase (KASI)

Synonyms: 3-oxoacyl-ACP-synthase, 3-oxoacyl-[acyl-carrier-protein]-synthase, acyl-[acyl carrier protein]:malonyl-[acyl carrier protein] C-acyltransferase (decarboxylating)

EC Number: 2.3.1.41

an acetyl-[acp] + a malonyl-[acp] + H+ <=> a holo-[acyl-carrier protein] + an acetoacetyl-[acp] + CO2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is irreversible in the direction shown.

In Pathways: superpathway of fatty acid biosynthesis I (E. coli) , superpathway of fatty acid biosynthesis initiation (E. coli) , fatty acid biosynthesis initiation III , fatty acid biosynthesis initiation II

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Inhibitors (Unknown Mechanism): thiolactomycin [Jackowski89] , iodoacetamide [Greenspan69, Comment 1] , cerulenin [Jackowski87, Comment 1]


Enzymatic reaction of: β-ketoacyl-ACP synthase (KASI)

Synonyms: 3-oxoacyl-ACP-synthase, 3-oxoacyl-[acyl-carrier-protein]-synthase, acyl-[acyl carrier protein]:malonyl-[acyl carrier protein] C-acyltransferase (decarboxylating)

EC Number: 2.3.1.41

a 2,3,4-saturated fatty acyl-[acp] + a malonyl-[acp] + H+ <=> a 3-oxoacyl-[acp] + CO2 + a holo-[acyl-carrier protein]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is irreversible in the direction shown.

In Pathways: superpathway of fatty acid biosynthesis I (E. coli) , fatty acid elongation -- saturated

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Inhibitors (Unknown Mechanism): a holo-[acyl-carrier protein] [McGuire01] , thiolactomycin [Jackowski89] , iodoacetamide [Greenspan69, Comment 1] , cerulenin [Jackowski87, Comment 1]


Enzymatic reaction of: malonyl-ACP decarboxylase (KASI)

EC Number: 2.3.1.-

a malonyl-[acp] + H+ <=> an acetyl-[acp] + CO2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: superpathway of fatty acid biosynthesis I (E. coli) , superpathway of fatty acid biosynthesis initiation (E. coli) , fatty acid biosynthesis initiation III

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
This is an alternate reaction catalyzed by the enzyme, namely malonyl-ACP decarboxylase. The only precursor required is malonyl-ACP. After decarboxylation with acetyl-ACP produced, the malonyl-ACP and acetyl-ACP are condensed using the other activity of the enzyme [Alberts72].


Sequence Features

Feature Class Location Citations Comment
Extrinsic-Sequence-Variant 4
[UniProt10a]
Alternate sequence: T; UniProt: (in strain: MA-1 / fabB3);
Extrinsic-Sequence-Variant 140
[UniProt10a]
Alternate sequence: F; UniProt: (in strain: K1060 / fabB5);
Active-Site 163
[UniProt10a]
Extrinsic-Sequence-Variant 299
[UniProt10a]
Alternate sequence: S; UniProt: (in strain: MA-1 / fabB3);
Extrinsic-Sequence-Variant 329
[UniProt10a]
Alternate sequence: V; UniProt: (in strain: M5 / fabB15);

History:
10/20/97 Gene b2323 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10274; confirmed by SwissProt match.


References

Alberts72: Alberts AW, Bell RM, Vagelos PR (1972). "Acyl carrier protein. XV. Studies of -ketoacyl-acyl carrier protein synthetase." J Biol Chem 247(10);3190-8. PMID: 5027749

Borgaro11: Borgaro JG, Chang A, Machutta CA, Zhang X, Tonge PJ (2011). "Substrate recognition by β-ketoacyl-ACP synthases." Biochemistry 50(49);10678-86. PMID: 22017312

Cao10: Cao Y, Yang J, Xian M, Xu X, Liu W (2010). "Increasing unsaturated fatty acid contents in Escherichia coli by coexpression of three different genes." Appl Microbiol Biotechnol 87(1);271-80. PMID: 20135119

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

ECOSAL: EcoSal "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

Feng09: Feng Y, Cronan JE (2009). "Escherichia coli unsaturated fatty acid synthesis: complex transcription of the fabA gene and in vivo identification of the essential reaction catalyzed by FabB." J Biol Chem 284(43);29526-35. PMID: 19679654

Garwin80: Garwin JL, Klages AL, Cronan JE (1980). "Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli." J Biol Chem 1980;255(24);11949-56. PMID: 7002930

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Greenspan69: Greenspan MD, Alberts AW, Vagelos PR (1969). "Acyl carrier protein. 13. Beta-ketoacyl acyl carrier protein synthetase from Escherichia coli." J Biol Chem 1969;244(23);6477-85. PMID: 4901371

Heath96: Heath RJ, Rock CO (1996). "Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis." J Biol Chem 1996;271(44);27795-801. PMID: 8910376

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jackowski02: Jackowski S, Zhang YM, Price AC, White SW, Rock CO (2002). "A missense mutation in the fabB (beta-ketoacyl-acyl carrier protein synthase I) gene confers tiolactomycin resistance to Escherichia coli." Antimicrob Agents Chemother 46(5);1246-52. PMID: 11959552

Jackowski87: Jackowski S, Rock CO (1987). "Acetoacetyl-acyl carrier protein synthase, a potential regulator of fatty acid biosynthesis in bacteria." J Biol Chem 1987;262(16);7927-31. PMID: 3294837

Jackowski89: Jackowski S, Murphy CM, Cronan JE, Rock CO (1989). "Acetoacetyl-acyl carrier protein synthase. A target for the antibiotic thiolactomycin." J Biol Chem 1989;264(13);7624-9. PMID: 2651445

Jeon12: Jeon E, Lee S, Han SO, Yoon YJ, Lee J (2012). "Improved production of long-chain fatty acid in Escherichia coli by an engineering elongation cycle during fatty acid synthesis (FAS) through genetic manipulation." J Microbiol Biotechnol 22(7);990-9. PMID: 22580319

Kim06: Kim P, Zhang YM, Shenoy G, Nguyen QA, Boshoff HI, Manjunatha UH, Goodwin MB, Lonsdale J, Price AC, Miller DJ, Duncan K, White SW, Rock CO, Barry CE, Dowd CS (2006). "Structure-activity relationships at the 5-position of thiolactomycin: an intact (5R)-isoprene unit is required for activity against the condensing enzymes from Mycobacterium tuberculosis and Escherichia coli." J Med Chem 49(1);159-71. PMID: 16392800

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Lee13: Lee S, Yoon YJ, Lee J (2013). "Enhancement of long-chain fatty acid production in Escherichia coli by coexpressing genes, including fabF, involved in the elongation cycle of fatty acid biosynthesis." Appl Biochem Biotechnol 169(2);462-76. PMID: 23225020

Lin10: Lin S, Hanson RE, Cronan JE (2010). "Biotin synthesis begins by hijacking the fatty acid synthetic pathway." Nat Chem Biol 6(9);682-8. PMID: 20693992

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Machutta10: Machutta CA, Bommineni GR, Luckner SR, Kapilashrami K, Ruzsicska B, Simmerling C, Kisker C, Tonge PJ (2010). "Slow onset inhibition of bacterial beta-ketoacyl-acyl carrier protein synthases by thiolactomycin." J Biol Chem 285(9);6161-9. PMID: 20018879

Magnuson93: Magnuson K, Jackowski S, Rock CO, Cronan JE (1993). "Regulation of fatty acid biosynthesis in Escherichia coli." Microbiol Rev 1993;57(3);522-42. PMID: 8246839

McGuire01: McGuire KA, Siggaard-Andersen M, Bangera MG, Olsen JG, von Wettstein-Knowles P (2001). "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." Biochemistry 40(33);9836-45. PMID: 11502177

Olsen01: Olsen JG, Kadziola A, von Wettstein-Knowles P, Siggaard-Andersen M, Larsen S (2001). "Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery." Structure 9(3);233-43. PMID: 11286890

Olsen99: Olsen JG, Kadziola A, von Wettstein-Knowles P, Siggaard-Andersen M, Lindquist Y, Larsen S (1999). "The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I." FEBS Lett 460(1);46-52. PMID: 10571059

Price01a: Price AC, Choi KH, Heath RJ, Li Z, White SW, Rock CO (2001). "Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism." J Biol Chem 276(9);6551-9. PMID: 11050088

Steinbrecher12: Steinbrecher T, Case DA, Labahn A (2012). "Free energy calculations on the binding of novel thiolactomycin derivatives to E. coli fatty acid synthase I." Bioorg Med Chem 20(11);3446-53. PMID: 22560835

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

vonWettsteinKno06: von Wettstein-Knowles P, Olsen JG, McGuire KA, Henriksen A (2006). "Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases." FEBS J 273(4);695-710. PMID: 16441657

White05: White SW, Zheng J, Zhang YM, Rock (2005). "The structural biology of type II fatty acid biosynthesis." Annu Rev Biochem 74;791-831. PMID: 15952903

Yu11: Yu X, Liu T, Zhu F, Khosla C (2011). "In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli." Proc Natl Acad Sci U S A 108(46);18643-8. PMID: 22042840

Zhang01: Zhang YM, Rao MS, Heath RJ, Price AC, Olson AJ, Rock CO, White SW (2001). "Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III." J Biol Chem 276(11);8231-8. PMID: 11078736

Zhang12: Zhang F, Ouellet M, Batth TS, Adams PD, Petzold CJ, Mukhopadhyay A, Keasling JD (2012). "Enhancing fatty acid production by the expression of the regulatory transcription factor FadR." Metab Eng 14(6);653-60. PMID: 23026122


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13B.