Beta-hydroxyacyl-acyl carrier protein dehydratase

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spinqualitylabelsall models Structure of FabZ (PDB code 1zhg). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase (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 is part of the fatty acid biosythesis elongation cycle. FabG reduces the β-keto acyl group of the elongating fatty acid[1]. Structural highlights . This tunnel accommodates the substrate. [2]

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

Updated on 28-March-2018

References

1. ↑ 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
2. ↑ 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