Enzymes Involved in Fatty Acid and Polyketide Biosynthesis inStreptomyces glaucescens:  Role of FabH and FabD and Their Acyl Carrier Protein Specificity†

Biochemistry ◽  
2002 ◽  
Vol 41 (33) ◽  
pp. 10462-10471 ◽  
Author(s):  
Galina Florova ◽  
Galina Kazanina ◽  
Kevin A. Reynolds
Keyword(s):  
Fatty Acid ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Polyketide Biosynthesis ◽  
Protein Specificity

Structural Basis of Acyl-Carrier Protein Interactions in Fatty Acid and Polyketide Biosynthesis

2020 ◽  
pp. 61-122 ◽  
Author(s):  
Jeffrey T. Mindrebo ◽  
Ashay Patel ◽  
Laëtitia E. Misson ◽  
Woojoo E. Kim ◽  
Tony D. Davis ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Protein Interactions ◽  
Acyl Carrier Protein ◽  
Structural Basis ◽  
Carrier Protein ◽  
Polyketide Biosynthesis

The role of β-ketoacyl-acyl carrier protein synthase III in the condensation steps of fatty acid biosynthesis in sunflower

Planta ◽  
2010 ◽  
Vol 231 (6) ◽  
pp. 1277-1289 ◽  
Author(s):  
Damián González-Mellado ◽  
Penny von Wettstein-Knowles ◽  
Rafael Garcés ◽  
Enrique Martínez-Force
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Acid Biosynthesis

The Role of Tandem Acyl Carrier Protein Domains in Polyunsaturated Fatty Acid Biosynthesis

2008 ◽  
Vol 130 (20) ◽  
pp. 6336-6337 ◽  
Author(s):  
Hui Jiang ◽  
Ross Zirkle ◽  
James G. Metz ◽  
Lisa Braun ◽  
Leslie Richter ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Polyunsaturated Fatty Acid ◽  
Fatty Acid Biosynthesis ◽  
Acyl Carrier Protein ◽  
Protein Domains ◽  
Carrier Protein ◽  
Acid Biosynthesis

Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases

FEBS Journal ◽  
2006 ◽  
Vol 273 (4) ◽  
pp. 695-710 ◽  
Author(s):  
Penny von Wettstein-Knowles ◽  
Johan G. Olsen ◽  
Kirsten A. McGuire ◽  
Anette Henriksen
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Active Site ◽  
Acyl Carrier Protein ◽  
Acid Synthesis ◽  
Carrier Protein

scholarly journals Structural comparison of Acinetobacter baumannii β-ketoacyl-acyl carrier protein reductases in fatty acid and aryl polyene biosynthesis

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Woo Cheol Lee ◽  
Sungjae Choi ◽  
Ahjin Jang ◽  
Kkabi Son ◽  
Yangmee Kim
Keyword(s):  
Fatty Acid ◽  
Acinetobacter Baumannii ◽  
Gene Cluster ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Gene Clusters ◽  
Carrier Protein ◽  
Aryl Group ◽  
Visible Absorption

AbstractSome Gram-negative bacteria harbor lipids with aryl polyene (APE) moieties. Biosynthesis gene clusters (BGCs) for APE biosynthesis exhibit striking similarities with fatty acid synthase (FAS) genes. Despite their broad distribution among pathogenic and symbiotic bacteria, the detailed roles of the metabolic products of APE gene clusters are unclear. Here, we determined the crystal structures of the β-ketoacyl-acyl carrier protein (ACP) reductase ApeQ produced by an APE gene cluster from clinically isolated virulent Acinetobacter baumannii in two states (bound and unbound to NADPH). An in vitro visible absorption spectrum assay of the APE polyene moiety revealed that the β-ketoacyl-ACP reductase FabG from the A. baumannii FAS gene cluster cannot be substituted for ApeQ in APE biosynthesis. Comparison with the FabG structure exhibited distinct surface electrostatic potential profiles for ApeQ, suggesting a positively charged arginine patch as the cognate ACP-binding site. Binding modeling for the aryl group predicted that Leu185 (Phe183 in FabG) in ApeQ is responsible for 4-benzoyl moiety recognition. Isothermal titration and arginine patch mutagenesis experiments corroborated these results. These structure–function insights of a unique reductase in the APE BGC in comparison with FAS provide new directions for elucidating host–pathogen interaction mechanisms and novel antibiotics discovery.

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