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Escherichia coli K-12 substr. MG1655 Protein Class: a palmitoyl-[acp]

Synonyms: a palmitoyl-[acyl-carrier-protein], 18:0-ACP

Superclasses: a modified protein an acyl-protein thioester an acyl-[acyl-carrier protein] a 2,3,4-saturated fatty acyl-[acp]
a modified protein an acyl-protein thioester an acyl-[acyl-carrier protein] a long-chain acyl-[acp]
a modified protein an acyl-protein thioester an acyl-[acyl-carrier protein] a saturated acyl-[acp]

Summary:
Palmitate (palmitic acid) is one of the most common saturated fatty acids found in animals and plants.

The compound was discovered by Edmond Frémy in 1840 in saponified palm oil, of which it is a major component, and was named "palmitique".

It is the first fatty acid produced during lipogenesis (fatty acid synthesis). In cells palmitate is usually found in the form of palmitoyl-[acp], palmitoyl-CoA or incorporated into lipids.

a palmitoyl-[acp] compound structure

SMILES: CCCCCCCCCCCCCCCC(SCCNC(=O)CCNC(C(O)C(C)(C)COP(=O)([O-])OCC(N[an apo-[acyl-carrier protein]])C(=O)[an apo-[acyl-carrier protein]])=O)=O

Unification Links: IAF1260:1437566

Reactions known to consume the compound:

palmitate biosynthesis II (bacteria and plants) :
a palmitoyl-[acp] + H2O → palmitate + a holo-[acyl-carrier protein] + H+

Not in pathways:
1-palmitoylglycerol 3-phosphate + a palmitoyl-[acp] → dipalmitoyl phosphatidate + a holo-[acyl-carrier protein]

fatty acid elongation -- saturated :
a malonyl-[acp] + a 2,3,4-saturated fatty acyl-[acp] + H+ → a holo-[acyl-carrier protein] + a 3-oxoacyl-[acp] + CO2

CDP-diacylglycerol biosynthesis II :
a 1-acyl-sn-glycerol 3-phosphate + an acyl-[acyl-carrier protein] → a 1,2-diacyl-sn-glycerol 3-phosphate + a holo-[acyl-carrier protein]
sn-glycerol 3-phosphate + an acyl-[acyl-carrier protein] → a 1-acyl-sn-glycerol 3-phosphate + a holo-[acyl-carrier protein]

Reactions known to produce the compound:

palmitate biosynthesis II (bacteria and plants) :
a palmitoyl-[acp] + NAD+ ← a trans hexadecenoyl-[acp] + NADH + H+

fatty acid elongation -- saturated :
a 2,3,4-saturated fatty acyl-[acp] + NAD+ ← a trans-2-enoyl-[acyl-carrier protein] + NADH + H+
a 2,3,4-saturated fatty acyl-[acp] + NADP+ ← a trans-2-enoyl-[acyl-carrier protein] + NADPH + H+

Not in pathways:
ATP + a holo-[acyl-carrier protein] + a fatty acid → AMP + a 2,3,4-saturated fatty acyl-[acp] + diphosphate

Reactions known to both consume and produce the compound:

Not in pathways:
an acyl-[acyl-carrier protein] + a 2-acyl-1-lyso-phosphatidylethanolamine ↔ a holo-[acyl-carrier protein] + an L-1-phosphatidylethanolamine

In Reactions of unknown directionality:

Not in pathways:
a 2,3,4-saturated 2-lysophosphatidate + a 2,3,4-saturated fatty acyl-[acp] = a 2,3,4-saturated L-phosphatidate + a holo-[acyl-carrier protein]

Not in pathways:
an acyl-[acyl-carrier protein] + NAD+ = a trans-2-enoyl-[acyl-carrier protein] + NADH + H+
an acyl-[acyl-carrier protein] + a malonyl-[acp] + H+ = a 3-oxoacyl-[acp] + CO2 + a holo-[acyl-carrier protein]

Enzymes inhibited by a palmitoyl-[acp], sorted by the type of inhibition, are:

Inhibitor (Competitive) of: β-ketoacyl-ACP synthase [Comment 1]

Inhibitor (Mechanism unknown) of: acetyl-CoA carboxyltransferase [Davis01] , 2,3,4-saturated fatty acyl-[acp]:NAD+ oxidoreductase [Heath95, Comment 2]

Inhibitor (Other types) of: β-ketoacyl-ACP synthase [Heath96, Comment 3]

This compound has been characterized as an alternative substrate of the following enzymes: acyl-CoA:sn-glycerol-3-phosphate 1-O-acyltransferase , acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase


References

Davis01: Davis MS, Cronan, Jr. JE (2001). "Inhibition of Escherichia coli acetyl coenzyme A carboxylase by acyl-acyl carrier protein." J Bacteriol. 183(4):1499-503. PMID: 11157970

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

Heath96: Heath RJ, Rock CO (1996). "Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli." J Biol Chem 1996;271(18);10996-1000. PMID: 8631920

Heath96a: Heath RJ, Rock CO (1996). "Regulation of fatty acid elongation and initiation by acyl-acyl carrier protein in Escherichia coli." J Biol Chem 1996;271(4);1833-6. PMID: 8567624


Report Errors or Provide Feedback
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 19.0 on Fri Sep 4, 2015, biocyc12.