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Pathway · 3 proteins

Fatty acid biosynthesis

Proteins of this group that KEGG places on its “Fatty acid biosynthesis” map for Aquifex aeolicus.

How it works

This map shows how fatty acids are built two carbons at a time on the acyl carrier protein, and how they are activated for use. The proteins here load malonyl groups onto the carrier, reduce the growing chain, and attach coenzyme A to fatty acids.

Grouped by KEGG pathway map. The explanation above is the atlas’s own; the map itself covers more organisms than Aquifex.

Its proteins

ProteinECReaction (UniProt)Metal or clusterAmino acidsCertainty
3-oxoacyl-[acyl-carrier-protein] reductase FabG1.1.1.100a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + NADPH + H(+)—248Step named
Malonyl CoA-acyl carrier protein transacylase2.3.1.39holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA—326Step named
Long-chain-fatty-acid CoA ligase—a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate—823Step named

Also part of this pathway

These proteins are described under another pathway, but also take part here.

ProteinECReaction (UniProt)Metal or clusterAmino acidsCertainty
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaHome: Lipid and cofactor connections2.1.3.15N(6)-carboxybiotinyl-L-lysyl-[protein] + acetyl-CoA = N(6)-biotinyl-L-lysyl-[protein] + malonyl-CoA—323Step named
Biotin carboxyl carrier protein of acetyl-CoA carboxylaseHome: Lipid and cofactor connections———154Step named
Biotin carboxylaseHome: Lipid and cofactor connections6.3.4.14N(6)-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP = N(6)-carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H(+)—444Step named
Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaHome: Lipid and cofactor connections2.1.3.15N(6)-carboxybiotinyl-L-lysyl-[protein] + acetyl-CoA = N(6)-biotinyl-L-lysyl-[protein] + malonyl-CoAZn(2+)276Step named
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZHome: Fatty-acid elongation4.2.1.59a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O—150Step named
Beta-ketoacyl-[acyl-carrier-protein] synthase IIIHome: Fatty-acid elongation2.3.1.180malonyl-[ACP] + acetyl-CoA + H(+) = 3-oxobutanoyl-[ACP] + CO2 + CoA—309Step named
Enoyl-[acyl-carrier-protein] reductase [NADH] FabIHome: Fatty-acid elongation1.3.1.9a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + NADH + H(+)—270Step named
3-oxoacyl-[acyl-carrier-protein] synthase 2Home: Fatty-acid elongation2.3.1.179(9Z)-hexadecenoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxo-(11Z)-octadecenoyl-[ACP] + holo-[ACP] + CO2—415Step named

Origins

Could fatty acids long enough to make a membrane have formed before cells?

How it was discovered

  1. late 1950sSalih Wakil finds that malonyl-CoA is the building unit of fatty acids, after Feodor Lynen had shown the central role of acetyl-CoA.Zubay, Origins of Life on Earth and in the Cosmos, p. 336
Naturalistic proposal

The Murchison meteorite contains a series of monocarboxylic acids from formic acid up to the 12-carbon dodecanoic acid, and Deamer counts these among possible membrane-forming compounds.

Design analysis

Deamer also notes that chains shorter than 14 carbons cannot assemble into stable membranes; membrane fatty acids are typically 14 to 18 carbons long. Straight-chain fatty acids have not been convincingly made under simulated prebiotic conditions.

In the cell, eight enzyme-catalysed reactions turn acetyl-CoA into a fatty acid, and the first one spends ATP to supply the energy for the rest.

From the books: Deamer, Assembling Life, pp. 35 and 56; Garrett & Grisham, Biochemistry, p. 665; Zubay, Origins of Life on Earth and in the Cosmos, p. 336.

The wider question for this part of the cell: origins for building and maintaining the membrane.

Sources

Other pathways in this group: Glycerolipid assembly · Lipid A and outer envelope · Fatty-acid elongation · Substrate recognition · Terpenoid backbone biosynthesis · Lipopolysaccharide biosynthesis · Biosynthesis of various nucleotide sugars · Not yet placed in a pathway