3-Aryl-4-hydroxyquinolin-2(1H)-one derivatives as type I fatty acid synthase inhibitors

2006 ◽  
Vol 16 (17) ◽  
pp. 4620-4623 ◽  
Author(s):  
Alexey Rivkin ◽  
Yoona R. Kim ◽  
Mark T. Goulet ◽  
Nathan Bays ◽  
Armetta D. Hill ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Type I

scholarly journals Production of long chain alcohols and alkanes upon coexpression of an acyl-ACP reductase and aldehyde-deformylating oxygenase with a bacterial type-I fatty acid synthase in E. coli

2015 ◽  
Vol 11 (9) ◽  
pp. 2464-2472 ◽  
Author(s):  
Dan Coursolle ◽  
Jiazhang Lian ◽  
John Shanklin ◽  
Huimin Zhao
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Type I ◽  
E Coli ◽  
Bacterial Type ◽  
Long Chain

An orthogonal type I FAS was introduced into E. coli to increase the production of long chain alcohols and alkanes.

scholarly journals Type I fatty acid synthase trapped in the octanoyl‐bound state

2020 ◽  
Vol 29 (2) ◽  
pp. 589-605 ◽  
Author(s):  
Alexander Rittner ◽  
Karthik S. Paithankar ◽  
Aaron Himmler ◽  
Martin Grininger
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Bound State ◽  
Type I

Structural Similarities between 6-Methylsalicylic Acid Synthase fromPenicillium patulumand Vertebrate Type I Fatty Acid Synthase:  Evidence from Thiol Modification Studies†

Biochemistry ◽  
1996 ◽  
Vol 35 (38) ◽  
pp. 12267-12274 ◽  
Author(s):  
Christopher J. Child ◽  
Jonathan B. Spencer ◽  
Pamela Bhogal ◽  
Peter M. Shoolingin-Jordan
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Type I ◽  
Methylsalicylic Acid Synthase

Molecular analysis of a Type I fatty acid synthase in Cryptosporidium parvum

2000 ◽  
Vol 105 (2) ◽  
pp. 253-260 ◽  
Author(s):  
Guan Zhu ◽  
Mary J Marchewka ◽  
Keith M Woods ◽  
Steve J Upton ◽  
Janet S Keithly
Keyword(s):  
Fatty Acid ◽  
Molecular Analysis ◽  
Cryptosporidium Parvum ◽  
Fatty Acid Synthase ◽  
Type I

scholarly journals A Mammalian Type I Fatty Acid Synthase Acyl Carrier Protein Domain Does Not Sequester Acyl Chains

2007 ◽  
Vol 283 (1) ◽  
pp. 518-528 ◽  
Author(s):  
Eliza Ploskoń ◽  
Christopher J. Arthur ◽  
Simon E. Evans ◽  
Christopher Williams ◽  
John Crosby ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Protein Domain ◽  
Carrier Protein ◽  
Type I ◽  
Acyl Chains

ChemInform Abstract: Discovery of BI 99179, a Potent and Selective Inhibitor of Type I Fatty Acid Synthase with Central Exposure.

ChemInform ◽  
2012 ◽  
Vol 43 (8) ◽  
pp. no-no
Author(s):  
Joerg T. Kley ◽  
Juergen Mack ◽  
Bradford Hamilton ◽  
Stefan Scheuerer ◽  
Norbert Redemann
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Selective Inhibitor ◽  
Type I

Acyl carrier protein: structure–function relationships in a conserved multifunctional protein family

2007 ◽  
Vol 85 (6) ◽  
pp. 649-662 ◽  
Author(s):  
David M. Byers ◽  
Huansheng Gong
Keyword(s):  
Fatty Acid ◽  
Active Sites ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Divalent Cations ◽  
Structural Features ◽  
Carrier Protein ◽  
Type I ◽  
Prosthetic Group

Acyl carrier protein (ACP) is a universal and highly conserved carrier of acyl intermediates during fatty acid synthesis. In yeast and mammals, ACP exists as a separate domain within a large multifunctional fatty acid synthase polyprotein (type I FAS), whereas it is a small monomeric protein in bacteria and plastids (type II FAS). Bacterial ACPs are also acyl donors for synthesis of a variety of products, including endotoxin and acylated homoserine lactones involved in quorum sensing; the distinct and essential nature of these processes in growth and pathogenesis make ACP-dependent enzymes attractive antimicrobial drug targets. Additionally, ACP homologues are key components in the production of secondary metabolites such as polyketides and nonribosomal peptides. Many ACPs exhibit characteristic structural features of natively unfolded proteins in vitro, with a dynamic and flexible conformation dominated by 3 parallel α helices that enclose the thioester-linked acyl group attached to a phosphopantetheine prosthetic group. ACP conformation may also be influenced by divalent cations and interaction with partner enzymes through its “recognition” helix II, properties that are key to its ability to alternately sequester acyl groups and deliver them to the active sites of ACP-dependent enzymes. This review highlights recent progress in defining how the structural features of ACP are related to its multiple carrier roles in fatty acid metabolism.

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