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Escherichia coli K-12 substr. MG1655 Enzyme: 3-oxoacyl-[acyl-carrier-protein] reductase



Gene: fabG Accession Numbers: EG11318 (EcoCyc), b1093, ECK1079

Synonyms: 3-oxoacyl-[acyl-carrier-protein] reductase FabG

Regulation Summary Diagram: ?

Subunit composition of 3-oxoacyl-[acyl-carrier-protein] reductase = [FabG]4
         3-oxoacyl-[acyl-carrier-protein] reductase subunit = FabG

Summary:
3-oxoacyl-[acyl-carrier-protein] reductase (3-oxoacyl-[ACP] reductase) encoded by gene fabG catalyzes the NADPH-dependent reduction of 3-oxoacyl-[ACP] intermediates (β-ketoacyl-[ACP] intermediates) to (3R)-3-hydroxyacyl-[ACP] intermediates in the prokaryotic fatty acid biosynthesis pathway. It functions in every cycle of fatty acid elongation (see pathway fatty acid elongation -- saturated) and in the synthesis of unsaturated fatty acids (see superpathway of fatty acid biosynthesis I (E. coli)). It is also involved in the biotin biosynthesis pathway (see pathway biotin biosynthesis I) [Lin10]. The enzyme is a member of the short-chain dehydrogenase/reductase (SDR) family [Oppermann03].

In early work, the enzyme was purified from E. coli extracts (although the strain used was not reported). It showed a marked preference for ACP derivatives over CoA derivatives as substrates and produced the D(-) isomer of the 3-hydroxyacyl-[ACP] product. It was specific for NADPH, but was nonspecific for the carbon chain length of the β-ketoacyl group. It utilized both saturated and unsaturated substrates [Toomey66]. FabG has also been shown to function in an in vitro reconstruction of fatty acid biosynthesis using purified components [Heath95, Heath96a, Zhang03a] and a steady state kinetic analysis of a reconstituted system has been performed [Yu11].

Site-directed mutagenesis studies and enzymatic analysis probed the residues on FabG required for high affinity binding to the ACP. NMR spectroscopy was also used to identify the ACP residues contributing to formation of the FabG-[ACP] complex [Zhang03a]. The crystal structure of wild-type, uncomplexed FabG has been determined at 2.60 Å resolution. The enzyme was shown to be a homotetramer [Price01a]. The crystal structures of wild-type FabG and a Y151F mutant, both complexed with NADP(H), have been determined at 2.05 Å resolution. Each monomer in the complex bound one molecule of NADP+ and the asymmetric unit contained eight Ca2+. The data suggested that important conformational changes accompany NADPH binding and that an allosteric mechanism is utilized [Price04].

The fabG gene is cotranscribed with acpP [Rawlings92]. It is an essential gene in E. coli [Zhang98c]. Conditionally lethal, temperature-sensitive mutants of FabG have been isolated. At the nonpermissive temperature fatty acid synthesis was inhibited, butyryl-ACP accumulated, and longer chain acyl-ACP intermediates were greatly decreased [Lai04].

In metabolic engineering studies, coexpression of E. coli fabG with polyhydroxyalkanoate (PHA) synthesis genes enhanced the production of PHAs in recombinant E. coli strains [Nomura08, Nomura05]. Improved production of long-chain fatty acids for biofuel in E. coli K-12 MG1655 was achieved by overexpressing the fabG along with other genes of the elongation cycle [Jeon12, Lee13, Jung13]. The enzyme is also of interest as an antimicrobial drug target [Kristan09, Campbell01, Heath01].

Reviews: [White05, Magnuson93, Campbell01, Heath01]

Gene Citations: [Podkovyrov95, Zhang96b, Podkovyrov96]

Locations: cytosol

Map Position: [1,149,893 -> 1,150,627] (24.78 centisomes)
Length: 735 bp / 244 aa

Molecular Weight of Polypeptide: 25.56 kD (from nucleotide sequence)

pI: 7.38

Unification Links: ASAP:ABE-0003700 , DIP:DIP-31869N , EchoBASE:EB1294 , EcoGene:EG11318 , EcoliWiki:b1093 , Mint:MINT-1232516 , ModBase:P0AEK2 , OU-Microarray:b1093 , PortEco:fabG , PR:PRO_000022563 , Pride:P0AEK2 , Protein Model Portal:P0AEK2 , RefSeq:NP_415611 , RegulonDB:EG11318 , SMR:P0AEK2 , String:511145.b1093 , Swiss-Model:P0AEK2 , UniProt:P0AEK2

Relationship Links: InterPro:IN-FAMILY:IPR002198 , InterPro:IN-FAMILY:IPR002347 , InterPro:IN-FAMILY:IPR011284 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR020904 , PDB:Structure:1I01 , PDB:Structure:1Q7B , PDB:Structure:1Q7C , Pfam:IN-FAMILY:PF00106 , Prints:IN-FAMILY:PR00080 , Prints:IN-FAMILY:PR00081 , Prosite:IN-FAMILY:PS00061

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006633 - fatty acid biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA01a, Lai04]
GO:0008610 - lipid biosynthetic process Inferred from experiment [Lai04]
GO:0009102 - biotin biosynthetic process Inferred from experiment [Lin10]
GO:0030497 - fatty acid elongation Inferred from experiment [Lai04]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0004316 - 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Zhang03a, Lai04]
GO:0042802 - identical protein binding Inferred from experiment [Price01a]
GO:0050661 - NADP binding Inferred from experiment [Price04]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051287 - NAD binding Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]

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

Essentiality data for fabG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Created 03-Apr-2013 by Fulcher C , SRI International
Last-Curated ? 03-Apr-2013 by Fulcher C , SRI International


Enzymatic reaction of: 3-oxoacyl-[ACP] reductase (3-oxoacyl-[acyl-carrier-protein] reductase)

Synonyms: 3-oxoacyl-[acyl-carrier-protein] reductase, 3-ketoacyl-ACP reductase, β-ketoacyl-ACP reductase, 3-ketoacyl-acyl carrier protein reductase, (3R)-3-hydroxyacyl-[ACP]:NADP+ oxidoreductase, β-ketoacyl-acyl carrier protein reductase

EC Number: 1.1.1.100

a 3-oxoacyl-[acp] + NADPH + H+ <=> a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+

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 physiologically favored in the direction shown.

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


Enzymatic reaction of: 3-oxo-cis5-dodecenoyl-[acp] reductase (3-oxoacyl-[acyl-carrier-protein] reductase)

EC Number: 1.1.1.100

a 3-oxo-cis5-dodecenoyl-[acp] + NADPH + H+ <=> a 3R-hydroxy cis Δ5-dodecenoyl-[acp] + NADP+

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 physiologically favored in the direction shown.

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


Enzymatic reaction of: 3-oxo-cis7-tetradecenoyl-[acp] reductase (3-oxoacyl-[acyl-carrier-protein] reductase)

EC Number: 1.1.1.100

a 3-oxo-cis7-tetradecenoyl-[acp] + NADPH + H+ <=> a 3R-hydroxy cis Δ7-tetradecenoyl-[acp] + NADP+

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 physiologically favored in the direction shown.

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

Summary:
The participation of FabG in the biosynthesis of unsaturated fatty acids was demonstrated in elongation assays in which reaction mixtures contained FadD, FabB, FabG, NADDPH, NADH, ACP, radiolabeled malonyl-CoA, and either 14:0-ACP or 14:1(Δ7)-ACP. The corresponding radiolabeled β-hydroxyacyl-ACP thioesters were formed [Heath96a].


Enzymatic reaction of: 3-oxo-cis9-hexadecenoyl-[acp] reductase (3-oxoacyl-[acyl-carrier-protein] reductase)

EC Number: 1.1.1.100

a 3-oxo-cis9-hexadecenoyl-[acp] + NADPH + H+ <=> a 3R-hydroxy cis Δ9-hexadecenoyl-[acp] + NADP+

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 physiologically favored in the direction shown.

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


Enzymatic reaction of: 3-oxo-pimeloyl-[acp] methyl ester reductase (3-oxoacyl-[acyl-carrier-protein] reductase)

EC Number: 1.1.1.100

a 3-oxo-pimeloyl-[acp] methyl ester + NADPH + H+ <=> a 3R-hydroxypimeloyl-[acp] methyl ester + NADP+

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 physiologically favored in the direction shown.

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


Enzymatic reaction of: 3-oxo-glutaryl-[acp] methyl ester reductase (3-oxoacyl-[acyl-carrier-protein] reductase)

EC Number: 1.1.1.100

a 3-oxo-glutaryl-[acp] methyl ester + NADPH + H+ <=> a 3R-hydroxyglutaryl-[acp] methyl ester + NADP+

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 physiologically favored in the direction shown.

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


Enzymatic reaction of: acetoacetyl-[acp] reductase (3-oxoacyl-[acyl-carrier-protein] reductase)

EC Number: 1.1.1.100

an acetoacetyl-[acp] + NADPH + H+ <=> a (R)-3-hydroxybutanoyl-[acp] + NADP+

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 physiologically favored in the direction shown.

Alternative Substrates for an acetoacetyl-[acp]: acetoacetyl-CoA [Zhang03a ] , ethyl-acetoacetate [Sun08 ]

In Pathways: palmitate biosynthesis II (bacteria and plants)

Summary:
FabG activity was assayed using an ACP-dependent gel reconstitution assay that measured the formation of β-hydroxybutyryl-ACP ((R)-3-hydroxybutanoyl-[acp]). The reaction mixture included ACP, malonyl-CoA, radiolabeled acetyl-CoA, NADPH, purified FabD, purified FabH, and purified FabG. The substrate was generated using FabD to to transfer the malonyl group from CoA to ACP, and FabH to condense acetyl-CoA and malonyl-ACP to produce β-ketobutyryl-ACP (acetoacetyl-ACP) [Zhang03a].

FabG was also able to utilize β-ketobutyryl-CoA (acetoacetyl-CoA) as substrate in an ACP-independent spectrophotometric assay that measures the disappearance of NADPH. However, the enzyme was less active than with its normal substrate β-ketobutyryl-ACP (acetoacetyl-ACP). Inhibition by free ACP was demonstrated using this assay [Zhang03a, Zhang04]. Using acetoacetyl-CoA as substrate, several cinnamic acid esters were found to inhibit the enzyme [Kristan09].

An in vitro assay was developed using ethyl acetoacetate as an alternative substrate and its kinetics were characterized [Sun08]. Using this substrate, trans-5-O-caffeoyl-D-quinate (chlorogenic acid) was shown to be a competitive inhibitor with respect to NADPH [Li06].

Inhibitors (Unknown Mechanism): (-)-epigallocatechin 3-gallate [Li06a] , Ca2+ [Price04] , Mg2+ [Price04] , trans-5-O-caffeoyl-D-quinate [Li06]


Sequence Features

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 12 -> 15
[UniProt11a]
UniProt: NADP.
Sequence-Conflict 30
[Rawlings92, UniProt10a]
Alternate sequence: A → G; UniProt: (in Ref. 1; AAA23739);
Amino-Acid-Sites-That-Bind 37
[UniProt11a]
UniProt: NADP.
Sequence-Conflict 43
[Rawlings92, UniProt11a]
Alternate sequence: Q → R; UniProt: (in Ref. 1; AAA23739).
Metal-Binding-Site 50
[UniProt11a]
UniProt: Calcium 1; via carbonyl oxygen; shared with dimeric partner.
Metal-Binding-Site 53
[UniProt11a]
UniProt: Calcium 1; via carbonyl oxygen; shared with dimeric partner.
Nucleotide-Phosphate-Binding-Region 59 -> 60
[UniProt11a]
UniProt: NADP.
Amino-Acid-Sites-That-Bind 86
[UniProt11a]
UniProt: NADP; via carbonyl oxygen.
Amino-Acid-Sites-That-Bind 138
[UniProt10]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 145
[UniProt11a]
UniProt: Calcium 2.
Mutagenesis-Variant 151
[Price04, UniProt11]
Alternate sequence: Y → F; UniProt: Defect in the affinity for NADPH.
Nucleotide-Phosphate-Binding-Region 151 -> 155
[UniProt11a]
UniProt: NADP.
Active-Site 151
[UniProt10]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 154
[Lai04, UniProt11]
Alternate sequence: A → T; UniProt: Decreases in the thermolability of the reductase; when associated with K- 233.
Mutagenesis-Variant 155
[Price04, UniProt11]
Alternate sequence: K → A; UniProt: Defect in the affinity for NADPH.
Amino-Acid-Sites-That-Bind 184
[UniProt11a]
UniProt: NADP; via amide nitrogen and carbonyl oxygen.
Mutagenesis-Variant 233
[Lai04, UniProt11]
Alternate sequence: E → K; UniProt: Decreases in the thermolability of the reductase; when associated with T- 154.
Metal-Binding-Site 233
[UniProt11a]
UniProt: Calcium 3; shared with dimeric partner.
Metal-Binding-Site 234
[UniProt11a]
UniProt: Calcium 3; via carbonyl oxygen; shared with dimeric partner.


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
1/26/1998 (pkarp) Merged genes G7999/fabG and EG11318/fabG


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Campbell01: Campbell JW, Cronan JE (2001). "Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery." Annu Rev Microbiol 55;305-32. PMID: 11544358

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

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Heath01: Heath RJ, White SW, Rock CO (2001). "Lipid biosynthesis as a target for antibacterial agents." Prog Lipid Res 40(6);467-97. PMID: 11591436

Heath95: Heath RJ, Rock CO (1995). "Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli." J Biol Chem 270(44);26538-42. PMID: 7592873

Heath96a: 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

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

Jung13: Jung Y, Lee S, Lee J (2013). "Correlations Between FAS Elongation Cycle Genes Expression and Fatty Acid Production for Improvement of Long-Chain Fatty Acids in Escherichia coli." Appl Biochem Biotechnol 169(5);1606-19. PMID: 23322253

Kristan09: Kristan K, Bratkovic T, Sova M, Gobec S, Prezelj A, Urleb U (2009). "Novel inhibitors of beta-ketoacyl-ACP reductase from Escherichia coli." Chem Biol Interact 178(1-3);310-6. PMID: 18977209

Lai04: Lai CY, Cronan JE (2004). "Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium." J Bacteriol 186(6);1869-78. PMID: 14996818

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

Li06: Li BH, Ma XF, Wu XD, Tian WX (2006). "Inhibitory activity of chlorogenic acid on enzymes involved in the fatty acid synthesis in animals and bacteria." IUBMB Life 58(1);39-46. PMID: 16540431

Li06a: Li BH, Zhang R, Du YT, Sun YH, Tian WX (2006). "Inactivation mechanism of the beta-ketoacyl-[acyl carrier protein] reductase of bacterial type-II fatty acid synthase by epigallocatechin gallate." Biochem Cell Biol 84(5);755-62. PMID: 17167539

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

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

Nomura05: Nomura CT, Taguchi K, Gan Z, Kuwabara K, Tanaka T, Takase K, Doi Y (2005). "Expression of 3-ketoacyl-acyl carrier protein reductase (fabG) genes enhances production of polyhydroxyalkanoate copolymer from glucose in recombinant Escherichia coli JM109." Appl Environ Microbiol 71(8);4297-306. PMID: 16085817

Nomura08: Nomura CT, Tanaka T, Eguen TE, Appah AS, Matsumoto K, Taguchi S, Ortiz CL, Doi Y (2008). "FabG mediates polyhydroxyalkanoate production from both related and nonrelated carbon sources in recombinant Escherichia coli LS5218." Biotechnol Prog 24(2);342-51. PMID: 18215055

Oppermann03: Oppermann U, Filling C, Hult M, Shafqat N, Wu X, Lindh M, Shafqat J, Nordling E, Kallberg Y, Persson B, Jornvall H (2003). "Short-chain dehydrogenases/reductases (SDR): the 2002 update." Chem Biol Interact 143-144;247-53. PMID: 12604210

Podkovyrov95: Podkovyrov S, Larson TJ (1995). "Lipid biosynthetic genes and a ribosomal protein gene are cotranscribed." FEBS Lett 368(3);429-31. PMID: 7635191

Podkovyrov96: Podkovyrov SM, Larson TJ (1996). "Identification of promoter and stringent regulation of transcription of the fabH, fabD and fabG genes encoding fatty acid biosynthetic enzymes of Escherichia coli." Nucleic Acids Res 1996;24(9);1747-52. PMID: 8649995

Price01a: Price AC, Zhang YM, Rock CO, White SW (2001). "Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis." Biochemistry 40(43);12772-81. PMID: 11669613

Price04: Price AC, Zhang YM, Rock CO, White SW (2004). "Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG." Structure 12(3);417-28. PMID: 15016358

Rawlings92: Rawlings M, Cronan JE (1992). "The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes." J Biol Chem 1992;267(9);5751-4. PMID: 1556094

Sun08: Sun YH, Cheng Q, Tian WX, Wu XD (2008). "A substitutive substrate for measurements of beta-ketoacyl reductases in two fatty acid synthase systems." J Biochem Biophys Methods 70(6);850-6. PMID: 18201766

Toomey66: Toomey RE, Wakil SJ (1966). "Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli." Biochim Biophys Acta 116(2);189-97. PMID: 4381013

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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

UniProt11: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

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

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

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

Zhang03a: Zhang YM, Wu B, Zheng J, Rock CO (2003). "Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction." J Biol Chem 278(52);52935-43. PMID: 14527946

Zhang04: Zhang YM, Rock CO (2004). "Evaluation of epigallocatechin gallate and related plant polyphenols as inhibitors of the FabG and FabI reductases of bacterial type II fatty-acid synthase." J Biol Chem 279(30);30994-1001. PMID: 15133034

Zhang96b: Zhang Y, Cronan JE (1996). "Polar allele duplication for transcriptional analysis of consecutive essential genes: application to a cluster of Escherichia coli fatty acid biosynthetic genes." J Bacteriol 1996;178(12);3614-20. PMID: 8655562

Zhang98c: Zhang Y, Cronan JE (1998). "Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster." J Bacteriol 180(13);3295-303. PMID: 9642179

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

My13: My L, Rekoske B, Lemke JJ, Viala JP, Gourse RL, Bouveret E (2013). "Transcription of the Escherichia coli Fatty Acid Synthesis Operon fabHDG Is Directly Activated by FadR and Inhibited by ppGpp." J Bacteriol 195(16);3784-95. PMID: 23772072

Tanaka89: Tanaka Y, Tsujimura A, Fujita N, Isono S, Isono K (1989). "Cloning and analysis of an Escherichia coli operon containing the rpmF gene for ribosomal protein L32 and the gene for a 30-kilodalton protein." J Bacteriol 1989;171(10);5707-12. PMID: 2477362

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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
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