CATH Classification

CATH Clusters

Functional Family

Enzyme Information
3-hydroxyacyl-[acyl-carrier-protein] dehydratase.
based on mapping to UniProt P07149
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl- carrier protein] + H(2)O.
-!- 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 catalyzes EC -!- Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0). -!- FabZ, but not FabA, can also accept unsaturated substrates. -!- Formerly EC, EC and EC
[Acyl-carrier-protein] S-acetyltransferase.
based on mapping to UniProt P07149
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier- protein].
-!- Essential, along with EC, for the initiation of fatty-acid biosynthesis in bacteria. -!- The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide. -!- This is one of the activities associated with EC
Fatty-acyl-CoA synthase.
based on mapping to UniProt P07149
Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
-!- The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi- functional protein complex composed of two subunits. -!- One subunit catalyzes the reactions EC and EC, while the other subunit catalyzes the reactions of EC, EC, EC, EC and EC -!- The enzyme differs from the animal enzyme (EC 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.
Enoyl-[acyl-carrier-protein] reductase (NADH).
based on mapping to UniProt P07149
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH.
-!- The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. -!- The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
[Acyl-carrier-protein] S-malonyltransferase.
based on mapping to UniProt P07149
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein].
-!- Essential, along with EC, for the initiation of fatty-acid biosynthesis in bacteria. -!- Also provides the malonyl groups for polyketide biosynthesis. -!- The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. -!- In Mycobacterium tuberculosis, holo-ACP (the product of EC is the preferred substrate. -!- This enzyme also forms part of the multienzyme complexes EC and EC -!- Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase. -!- In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates. -!- The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
Oleoyl-[acyl-carrier-protein] hydrolase.
based on mapping to UniProt P07149
Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate.
-!- Acts on [acyl-carrier-protein] thioesters of fatty acids from C(12) to C(18), but the derivative of oleic acid is hydrolyzed much more rapidly than any other compound tested.

UniProtKB Entries (1)

Saccharomyces cerevisiae S288C
Fatty acid synthase subunit beta

PDB Structure

External Links
Primary Citation
Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase
Leibundgut, M., Jenni, S., Frick, C., Ban, N.