Beta-hydroxyacyl-acyl carrier protein dehydratase

From Proteopedia

Function

Beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase or 3-oxoacyl-ACP reductase (FabZ) catalyzes the dehydration of short and long chained β-hydroxyacyl-ACPs.

FabA exhibits broad overlapping activity to FabZ and is most active in dehydrating midlength chained β-hydroxyacyl-ACPs.
FabG or 3-ketoacyl-(acyl-carrier-protein) reductase or beta-ketoacyl carrier protein reductase is part of the fatty acid biosythesis elongation cycle. FabG reduces the β-keto acyl group of the elongating fatty acid^[1].

Structural highlights

The structure of FabA and FabZ shows a tunnel between the interfaces of the dimer. This tunnel accommodates the substrate. ^[2]

3D structures of β-hydroxyacyl-acyl carrier protein dehydratase

Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures

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Structure of FabZ (PDB code 1zhg).

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References

↑ Price AC, Zhang YM, Rock CO, White SW. Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis. Biochemistry. 2001 Oct 30;40(43):12772-81. PMID:11669613
↑ Swarnamukhi PL, Sharma SK, Bajaj P, Surolia N, Surolia A, Suguna K. Crystal structure of dimeric FabZ of Plasmodium falciparum reveals conformational switching to active hexamers by peptide flips. FEBS Lett. 2006 May 15;580(11):2653-60. Epub 2006 Apr 21. PMID:16643907 doi:10.1016/j.febslet.2006.04.014