Molecular Basis of the Medium-Chain Fatty Acyl-CoA Dehydrogenase-Catalyzed "Oxidase" Reaction: pH-Dependent Distribution of Intermediary Enzyme Species during Catalysis

Biochemistry ◽  
1994 ◽  
Vol 33 (15) ◽  
pp. 4738-4744 ◽  
Author(s):  
Jeffrey K. Johnson ◽  
N. Ravi Kumar ◽  
D. K. Srivastava
2020 ◽  
pp. 89-114
Author(s):  
Maria Tsampika Manoli ◽  
Natalia Tarazona ◽  
Aranzazu Mato ◽  
Beatriz Maestro ◽  
Jesús M. Sanz ◽  
...  

2014 ◽  
Vol 16 (31) ◽  
pp. 16547-16562 ◽  
Author(s):  
M. Micaela Gonzalez ◽  
M. Paula Denofrio ◽  
Fernando S. García Einschlag ◽  
Carlos A. Franca ◽  
Reinaldo Pis Diez ◽  
...  

The nature of nucleotide and the pH modulate the type of complexes formed and the dynamic deactivation processes.


2012 ◽  
Vol 416 (2) ◽  
pp. 221-238 ◽  
Author(s):  
Aneesh Goyal ◽  
Priyanka Verma ◽  
Madhankumar Anandhakrishnan ◽  
Rajesh S. Gokhale ◽  
Rajan Sankaranarayanan

2013 ◽  
Vol 110 (40) ◽  
pp. 15973-15978 ◽  
Author(s):  
A. L. Garland ◽  
W. G. Walton ◽  
R. D. Coakley ◽  
C. D. Tan ◽  
R. C. Gilmore ◽  
...  

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Gajanan Shrikant Patil ◽  
Priyadarshan Kinatukara ◽  
Sudipta Mondal ◽  
Sakshi Shambhavi ◽  
Ketan D Patel ◽  
...  

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.


Enzyme ◽  
1987 ◽  
Vol 38 (1-4) ◽  
pp. 91-107 ◽  
Author(s):  
Kay Tanaka ◽  
Yasuyuki Ikeda ◽  
Yoichi Matsubara ◽  
David B. Hamyna

Lipids ◽  
1989 ◽  
Vol 24 (5) ◽  
pp. 383-388 ◽  
Author(s):  
José L. Periago ◽  
María L. Pita ◽  
María A. Sanchez del Castillo ◽  
Guillermo Caamaño ◽  
María D. Suárez

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