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Pathway Description
Fatty Acid Elongation (Saturated)
Escherichia coli O157:H7
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2024-12-20
Last Updated: 2025-06-03
The fatty acid elongation pathway shows an elongation cycle of an acyl-ACP chain by adding two carbons. Acetoacetyl-acp is produced from interaction of 3-oxoacyl-acp synthase 3 with malonyl-acp and Acetyl-CoA, and then Acetoacetyl-acp produce a 3-oxoacyl acp spontaneously. 3-oxoacyl acp will undergo the cycles of the elongation. The first step is converting the oxoacyl acp into a (3R) 3-hydroxyacyl(acp) through a 3-oxoacyl[acp] reductase.This second step converts the hydroxyacyl into a trans 2 enoyl acp through a protein complex conformed of a hydroxomyristoyl dehydratase and a hydroxydecanoyl dehydratase. The third step can be reached through two different reactions with a enoyl-acp reductase, involving NADPH or NADH. This leads to the production of a 2,3,4-saturated fatty acyl acp. For the final step the 2,3,4 fatty acyl acp is turned into a oxoacyl acp through a 3-oxoacyl acp synthase protein complex. The products of multiple of the elongation cycle are phospholipids, lipoproteins (saturated fatty acids), lauric and other fatty acid-containing compounds.
References
Fatty Acid Elongation (Saturated) References
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Pubmed: 3040739
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Pubmed: 3040734
Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. doi: 10.1093/dnares/4.2.91.
Pubmed: 9205837
Kondo H, Shiratsuchi K, Yoshimoto T, Masuda T, Kitazono A, Tsuru D, Anai M, Sekiguchi M, Tanabe T: Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9730-3. doi: 10.1073/pnas.88.21.9730.
Pubmed: 1682920
Li SJ, Cronan JE Jr: The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J Biol Chem. 1992 Jan 15;267(2):855-63.
Pubmed: 1370469
Muramatsu S, Mizuno T: Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli. Nucleic Acids Res. 1989 May 25;17(10):3982. doi: 10.1093/nar/17.10.3982.
Pubmed: 2660106
Alix JH: A rapid procedure for cloning genes from lambda libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome. DNA. 1989 Dec;8(10):779-89. doi: 10.1089/dna.1989.8.779.
Pubmed: 2575489
Magnuson K, Oh W, Larson TJ, Cronan JE Jr: Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli. FEBS Lett. 1992 Mar 16;299(3):262-6. doi: 10.1016/0014-5793(92)80128-4.
Pubmed: 1339356
Verwoert II, Verbree EC, van der Linden KH, Nijkamp HJ, Stuitje AR: Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase. J Bacteriol. 1992 May;174(9):2851-7. doi: 10.1128/jb.174.9.2851-2857.1992.
Pubmed: 1314802
Bouquin N, Tempete M, Holland IB, Seror SJ: Resistance to trifluoroperazine, a calmodulin inhibitor, maps to the fabD locus in Escherichia coli. Mol Gen Genet. 1995 Mar 10;246(5):628-37. doi: 10.1007/bf00298970.
Pubmed: 7700236
Tsay JT, Oh W, Larson TJ, Jackowski S, Rock CO: Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12. J Biol Chem. 1992 Apr 5;267(10):6807-14.
Pubmed: 1551888
Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. doi: 10.1038/msb4100049. Epub 2006 Feb 21.
Pubmed: 16738553
Lai CY, Cronan JE: Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium. J Bacteriol. 2004 Mar;186(6):1869-78. doi: 10.1128/jb.186.6.1869-1878.2004.
Pubmed: 14996818
Rawlings M, Cronan JE Jr: The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes. J Biol Chem. 1992 Mar 25;267(9):5751-4.
Pubmed: 1556094
Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. doi: 10.1093/dnares/3.3.137.
Pubmed: 8905232
Cronan JE Jr, Li WB, Coleman R, Narasimhan M, de Mendoza D, Schwab JM: Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase. J Biol Chem. 1988 Apr 5;263(10):4641-6.
Pubmed: 2832401
Henry MF, Cronan JE Jr: A new mechanism of transcriptional regulation: release of an activator triggered by small molecule binding. Cell. 1992 Aug 21;70(4):671-9. doi: 10.1016/0092-8674(92)90435-f.
Pubmed: 1505031
Coleman J, Raetz CR: First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene. J Bacteriol. 1988 Mar;170(3):1268-74. doi: 10.1128/jb.170.3.1268-1274.1988.
Pubmed: 3277952
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000819
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