scholarly journals Characterization of protein‐ligand binding interactions of enoyl‐ACP reductase ( FabI ) by native MS reveals allosteric effects of coenzymes and the inhibitor triclosan

2021 ◽  
Author(s):  
P. Matthew Joyner ◽  
Denise P. Tran ◽  
Muhammad A. Zenaidee ◽  
Joseph A. Loo
Keyword(s):  
Ligand Binding ◽  
Binding Interactions ◽  
Native Ms ◽  
Enoyl Acp Reductase

Characterization of the r-state insulin hexamer and its derivatives. The hexamer is stabilized by heterotropic ligand binding interactions

Biochemistry ◽  
1991 ◽  
Vol 30 (27) ◽  
pp. 6636-6645 ◽  
Author(s):  
Mark L. Brader ◽  
Niels C. Kaarsholm ◽  
Robert W. K. Lee ◽  
Michael F. Dunn
Keyword(s):  
Ligand Binding ◽  
Binding Interactions

scholarly journals Characterization of protein-ligand binding interactions of enoyl-ACP reductase (FabI) by native MS reveals allosteric effects of coenzymes and the inhibitor triclosan

2019 ◽  
Author(s):  
P. Matthew Joyner ◽  
Denise P. Tran ◽  
Muhammad A. Zenaidee ◽  
Joseph A. Loo
Keyword(s):  
Fatty Acid Synthase ◽  
Antibacterial Drug ◽  
Allosteric Effect ◽  
The Past ◽  
Protein Ligand Interactions ◽  
Native Ms ◽  
Ligand Interactions ◽  
Enoyl Acp Reductase ◽  
The Subject

AbstractThe enzyme enoyl-ACP reductase (also called FabI in bacteria) is an essential member of the fatty acid synthase II pathway in plants and bacteria. This enzyme is the target of the antibacterial drug triclosan and has been the subject of extensive studies for the past 20 years. Despite the large number of reports describing the biochemistry of this enzyme, there have been no studies that provided direct observation of the protein and its various ligands. Here we describe the use of native MS to characterize the protein-ligand interactions of FabI with its coenzymes NAD+ and NADH and with the inhibitor triclosan. Measurements of the gas-phase affinities of the enzyme for these ligands yielded values that are in close agreement with solution-phase affinity measurements. Additionally, FabI is a homotetramer and we were able to measure the affinity of each subunit for each coenzyme, which revealed that both coenzymes exhibit a positive homotropic allosteric effect. An allosteric effect was also observed in association with the inhibitor triclosan. These observations provide new insights into this well-studied enzyme and suggest that there may still be gaps in the existing mechanistic models that explain FabI inhibition.

scholarly journals Characterization of protein–ligand interactions by SABRE

2021 ◽  
Author(s):  
Ratnamala Mandal ◽  
Pierce Pham ◽  
Christian Hilty
Keyword(s):  
Ligand Binding ◽  
Polarization Transfer ◽  
Binding Interactions ◽  
Protein Ligand Interactions ◽  
Ligand Interactions

Protein–ligand binding interactions are characterized by the para-H2 based hyperpolarization technique SABRE and flow-NMR. Binding to the protein is identified by R2 change of a ligand first interacting with the Ir polarization transfer catalyst.

scholarly journals Odorant-binding protein. Characterization of ligand binding.

1990 ◽  
Vol 265 (11) ◽  
pp. 6118-6125
Author(s):  
J Pevsner ◽  
V Hou ◽  
A M Snowman ◽  
S H Snyder
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Protein Characterization ◽  
Odorant Binding Protein ◽  
Odorant Binding

Characterization of Determinants of Ligand Binding to the Nicotinic Acid Receptor GPR109A (HM74A/PUMA-G)

2005 ◽  
Vol 68 (5) ◽  
pp. 1271-1280 ◽  
Author(s):  
Sorin Tunaru ◽  
Jens Lättig ◽  
Jukka Kero ◽  
Gerd Krause ◽  
Stefan Offermanns
Keyword(s):  
Ligand Binding ◽  
Nicotinic Acid ◽  
Acid Receptor

Characterization of labeled reagents in ligand-binding assays by a surface plasmon resonance biosensor

Bioanalysis ◽  
2017 ◽  
Vol 9 (2) ◽  
pp. 193-207 ◽  
Author(s):  
Jia Duo ◽  
JoAnne Bruno ◽  
Steven Piccoli ◽  
Binodh DeSilva ◽  
Yan J Zhang
Keyword(s):  
Surface Plasmon Resonance ◽  
Ligand Binding ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Assays ◽  
Surface Plasmon Resonance Biosensor
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