An acyltransferase domain of FK506 polyketide synthase recognizing both an acyl carrier protein and coenzyme A as acyl donors to transfer allylmalonyl and ethylmalonyl units

FEBS Journal ◽  
2015 ◽  
Vol 282 (13) ◽  
pp. 2527-2539 ◽  
Author(s):  
Hui Jiang ◽  
Yue-Yue Wang ◽  
Yuan-Yang Guo ◽  
Jie-Jie Shen ◽  
Xiao-Sheng Zhang ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Acyl Donors

scholarly journals Mutants of Escherichia coli with Temperature-sensitive Malonyl Coenzyme A-Acyl Carrier Protein Transacylase

1974 ◽  
Vol 249 (23) ◽  
pp. 7468-7475
Author(s):  
Mark E. Harder ◽  
Ruth C. Ladenson ◽  
Steven D. Schimmel ◽  
David F. Silbert
Keyword(s):  
Escherichia Coli ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Temperature Sensitive ◽  
Carrier Protein

scholarly journals Sticky swinging arm dynamics: studies of an acyl carrier protein domain from the mycolactone polyketide synthase

2016 ◽  
Vol 473 (8) ◽  
pp. 1097-1110 ◽  
Author(s):  
Steven Vance ◽  
Olga Tkachenko ◽  
Ben Thomas ◽  
Mona Bassuni ◽  
Hui Hong ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Acyl Carrier Protein ◽  
Protein Domain ◽  
Carrier Protein ◽  
Protein Surface ◽  
Prosthetic Group ◽  
Polyketide Biosynthesis ◽  
Covalently Linked

When covalently linked to an acyl carrier protein (ACP) and loaded with acyl substrate-mimics, some 4′-phosphopantetheine prosthetic group arms swing freely, whereas others stick to the protein surface, suggesting a possible mode of interaction with enzyme domains during polyketide biosynthesis.

scholarly journals Modular type I polyketide synthase acyl carrier protein domains share a common N-terminally extended fold

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Luisa Moretto ◽  
Rachel Heylen ◽  
Natalie Holroyd ◽  
Steven Vance ◽  
R. William Broadhurst
Keyword(s):  
Polyketide Synthase ◽  
Acyl Carrier Protein ◽  
Protein Domains ◽  
Carrier Protein ◽  
Type I

scholarly journals Active site labeling of fatty acid and polyketide acyl-carrier protein transacylases

2019 ◽  
Vol 17 (19) ◽  
pp. 4720-4724 ◽  
Author(s):  
Tony D. Davis ◽  
Jennifer M. Michaud ◽  
Michael D. Burkart
Keyword(s):  
Fatty Acid ◽  
Fluorescent Probe ◽  
Active Site ◽  
Polyketide Synthase ◽  
Acyl Carrier Protein ◽  
Site Directed Mutagenesis ◽  
Probe Design ◽  
Directed Mutagenesis ◽  
Carrier Protein

Fluorescent probe design and site-directed mutagenesis unveil new activity-based chemical reporters for fatty acid and polyketide synthase acyl-carrier protein transacylases.

Solution Structure of an Acyl Carrier Protein Domain from a Fungal Type I Polyketide Synthase,

Biochemistry ◽  
2010 ◽  
Vol 49 (10) ◽  
pp. 2186-2193 ◽  
Author(s):  
Pakorn Wattana-amorn ◽  
Christopher Williams ◽  
Eliza Płoskoń ◽  
Russell J. Cox ◽  
Thomas J. Simpson ◽  
...  
Keyword(s):  
Solution Structure ◽  
Polyketide Synthase ◽  
Acyl Carrier Protein ◽  
Protein Domain ◽  
Carrier Protein ◽  
Type I

An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein

ChemBioChem ◽  
2008 ◽  
Vol 9 (15) ◽  
pp. 2424-2432 ◽  
Author(s):  
Simon E. Evans ◽  
Christopher Williams ◽  
Christopher J. Arthur ◽  
Steven G. Burston ◽  
Thomas J. Simpson ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Acyl Carrier Protein ◽  
Carrier Protein

Molecular characterization of anEscherichia colimutant with a temperature-sensitive malonyl coenzyme A-acyl carrier protein transacylase

FEBS Letters ◽  
1994 ◽  
Vol 348 (3) ◽  
pp. 311-316 ◽  
Author(s):  
Ira I.G.S. Verwoert ◽  
Etienne F. Verhagen ◽  
Karin H. van der Linden ◽  
Elizabeth C. Verbree ◽  
H.John J. Nijkamp ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Temperature Sensitive ◽  
Carrier Protein

scholarly journals A universal pocket in Fatty acyl-AMP ligases ensures redirection of fatty acid pool away from Coenzyme A-based activation

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Gajanan Shrikant Patil ◽  
Priyadarshan Kinatukara ◽  
Sudipta Mondal ◽  
Sakshi Shambhavi ◽  
Ketan D Patel ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Binding Sites ◽  
Molecular Basis ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Fatty Acyl ◽  
Carrier Protein ◽  
Binding Pockets ◽  
Fatty Acid Pool ◽  
Do So

Fatty acyl-AMP ligases (FAALs) channelize fatty acids towards biosynthesis of virulent lipids in mycobacteria and other pharmaceutically or ecologically important polyketides and lipopeptides in other microbes. They do so by bypassing the ubiquitous coenzyme A-dependent activation and rely on the acyl carrier protein-tethered 4'-phosphopantetheine (holo-ACP). The molecular basis of how FAALs strictly reject chemically identical and abundant acceptors like coenzyme A (CoA) and accept holo-ACP unlike other members of the ANL superfamily remains elusive. We show FAALs have plugged the promiscuous canonical CoA-binding pockets and utilize highly selective alternative binding sites. These alternative pockets can distinguish adenosine 3', 5'-bisphosphate-containing CoA from holo-ACP and thus FAALs can distinguish between CoA and holo-ACP. These exclusive features helped identify the omnipresence of FAAL-like proteins and their emergence in plants, fungi, and animals with unconventional domain organisations. The universal distribution of FAALs suggests they are parallelly evolved with FACLs for ensuring a CoA-independent activation and redirection of fatty acids towards lipidic metabolites.

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