Nitrite inhibition of acyl transfer by coenzyme A via the formation of an S-nitrosothiol derivative

1984 ◽  
Vol 32 (5) ◽  
pp. 1057-1060 ◽  
Author(s):  
Shu I Tu ◽  
D. Michael Byler ◽  
James R. Cavanaugh
Keyword(s):  
Coenzyme A ◽  
Acyl Transfer ◽  
Nitrite Inhibition

scholarly journals Insight into Coenzyme A cofactor binding and the mechanism of acyl-transfer in an acylating aldehyde dehydrogenase from Clostridium phytofermentans

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Laura R. Tuck ◽  
Kirsten Altenbach ◽  
Thiau Fu Ang ◽  
Adam D. Crawshaw ◽  
Dominic J. Campopiano ◽  
...  
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Coenzyme A ◽  
Acyl Transfer ◽  
Cofactor Binding ◽  
Insight Into ◽  
Clostridium Phytofermentans

scholarly journals Structural basis for catalysis and substrate specificity of human ACAT1

2020 ◽  
Author(s):  
Hongwu Qian ◽  
Xin Zhao ◽  
Renhong Yan ◽  
Shuai Gao ◽  
Xue Sun ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Coenzyme A ◽  
Cholesterol Metabolism ◽  
Acyl Chain ◽  
Acyl Transfer ◽  
Structural Basis ◽  
Lateral Entry ◽  
Transmembrane Segments ◽  
Close Relationship ◽  
Acyl Coenzyme A

SummaryAcyl-coenzyme A: cholesterol acyltransferases (ACATs) catalyze acyl transfer from acyl-coenzyme A (CoA) to cholesterol to generate cholesteryl ester, which is the primary form for cellular storage and plasma transport of cholesterol. Because of their close relationship with cholesterol metabolism, ACATs represent potential drug target for the treatment of atherosclerosis and other cholesterol-related disorders. Here we present the cryo-EM structure of human ACAT1 at 3.3 Å resolution for dimer of dimers and 3.0 Å for a dimer. Each protomer consists of nine transmembrane segments that enclose a cytosolic (C) and a transmembrane (T) tunnel. The tunnels, each accommodating an elongated density, converge at the predicted catalytic site. Structure-guided mutational analyses suggest the cytosolic and lateral entry for acyl-CoA and cholesterol, respectively. Our structural, biochemical, and mass spectrometric characterizations reveal the catalytic mechanism and substrate preference for unsaturated acyl chain by ACAT1.

scholarly journals The terminal O-acetyltransferase involved in vindoline biosynthesis defines a new class of proteins responsible for coenzyme A-dependent acyl transfer

1998 ◽  
Vol 14 (6) ◽  
pp. 703-713 ◽  
Author(s):  
Benoit St-Pierre ◽  
Pierre Laflamme ◽  
Anne-Marie Alarco ◽  
Vincenzo D ◽  
e Luca
Keyword(s):  
Coenzyme A ◽  
Acyl Transfer ◽  
New Class

Palmitoyl coenzyme A

2015 ◽  
Author(s):  
LB Becnel ◽  
YF Darlington ◽  
S Orechsner ◽  
J Easton-Marks ◽  
CA Watkins ◽  
...  
Keyword(s):  
Coenzyme A
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