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Escherichia coli K-12 substr. MG1655 Reaction: 2.3.1.85/2.3.1.86/4.2.1.59

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 2.3.1.85 , 2.3.1.86 , 4.2.1.59

Enzymes and Genes:
3-hydroxydecanoyl-[acp] dehydrase : fabA
3-hydroxy-acyl-[acyl-carrier-protein] dehydratase : fabZ

In Pathway: palmitate biosynthesis II (bacteria and plants)

Supersedes EC numbers: 4.2.1.58, 4.2.1.60, 4.2.1.61

Note that this reaction equation differs from the official Enzyme Commission reaction equations for this EC number.

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

Mass balance status: Balanced.

Direct generic reaction:
a (3R)-3-hydroxyacyl-[acyl-carrier protein] → a trans-2-enoyl-[acyl-carrier protein] + H2O (2.3.1.85/2.3.1.86/4.2.1.59)

Enzyme Commission Primary Name for 2.3.1.85: fatty-acid synthase

Enzyme Commission Synonyms for 2.3.1.85: FASN (gene name)

Enzyme Commission Primary Name for 2.3.1.86: fatty-acyl-CoA synthase

Enzyme Commission Synonyms for 2.3.1.86: yeast fatty acid synthase, FAS1 (gene name), FAS2 (gene name)

Enzyme Commission Primary Name for 4.2.1.59: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase

Enzyme Commission Synonyms for 4.2.1.59: fabZ (gene name), fabA (gene name), D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase, D-3-hydroxyoctanoyl-acyl carrier protein dehydratase, β-hydroxyoctanoyl-acyl carrier protein dehydrase, β-hydroxyoctanoyl thioester dehydratase, β-hydroxyoctanoyl-ACP-dehydrase, (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase, (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase (oct-2-enoyl-[acyl-carrier protein]-forming), 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase

Enzyme Commission Summary for 2.3.1.85:
The animal enzyme is a multi-functional protein catalysing the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase, EC 4.2.1.59, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 3.1.2.14, oleoyl-[acyl-carrier-protein] hydrolase. cf. EC 2.3.1.86, fatty-acyl-CoA synthase.

Enzyme Commission Summary for 2.3.1.86:
The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits.One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.

Enzyme Commission Summary for 4.2.1.59:
This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. The enzyme uses fatty acyl thioesters of ACP in vivo. Different forms of the enzyme may have preferences for substrates with different chain length. For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyses EC 5.3.3.14, trans-2-decenoyl-[acyl-carrier protein] isomerase. Despite the differences both forms can catalyse all steps leading to the synthesis of palmitate (C16:0). FabZ, but not FabA, can also accept unsaturated substrates [Heath96a].

Citations: [Stoops79, Wakil83, Schweizer73, Tehlivets07, Mizugaki68, Sharma90, Mohan94]

Relationship Links: BRENDA:EC:2.3.1.85 , BRENDA:EC:2.3.1.86 , BRENDA:EC:4.2.1.59 , ENZYME:EC:2.3.1.85 , ENZYME:EC:2.3.1.86 , ENZYME:EC:4.2.1.59 , IUBMB-ExplorEnz:EC:2.3.1.85 , IUBMB-ExplorEnz:EC:2.3.1.86 , IUBMB-ExplorEnz:EC:4.2.1.59


References

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

Mizugaki68: Mizugaki M, Swindell AC, Wakil SJ (1968). "Intermediate- and long-chain beta-hydroxyacyl-ACP dehydrases from E. coli fatty acid synthetase." Biochem Biophys Res Commun 33(3);520-7. PMID: 4881058

Mohan94: Mohan S, Kelly TM, Eveland SS, Raetz CR, Anderson MS (1994). "An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis." J Biol Chem 1994;269(52);32896-903. PMID: 7806516

Schweizer73: Schweizer E, Kniep B, Castorph H, Holzner U (1973). "Pantetheine-free mutants of the yeast fatty-acid-synthetase complex." Eur J Biochem 39(2);353-62. PMID: 4590449

Sharma90: Sharma A, Henderson BS, Schwab JM, Smith JL (1990). "Crystallization and preliminary X-ray analysis of beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli." J Biol Chem 1990;265(9);5110-2. PMID: 2180957

Stoops79: Stoops JK, Ross P, Arslanian MJ, Aune KC, Wakil SJ, Oliver RM (1979). "Physicochemical studies of the rat liver and adipose fatty acid synthetases." J Biol Chem 254(15);7418-26. PMID: 457689

Tehlivets07: Tehlivets O, Scheuringer K, Kohlwein SD (2007). "Fatty acid synthesis and elongation in yeast." Biochim Biophys Acta 1771(3);255-70. PMID: 16950653

Wakil83: Wakil SJ, Stoops JK, Joshi VC (1983). "Fatty acid synthesis and its regulation." Annu Rev Biochem 52;537-79. PMID: 6137188


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, BIOCYC13A.