scholarly journals Detecting and Characterizing the Kinetic Activation of Thermal Networks in Proteins: Thermal Transfer from a Distal, Solvent-Exposed Loop to the Active Site in Soybean Lipoxygenase

2019 ◽  
Vol 123 (41) ◽  
pp. 8662-8674 ◽  
Author(s):  
Jan Paulo T. Zaragoza ◽  
Andy Nguy ◽  
Natalie Minnetian ◽  
Zhenyu Deng ◽  
Anthony T. Iavarone ◽  
...  
Biochemistry ◽  
2004 ◽  
Vol 43 (41) ◽  
pp. 13063-13071 ◽  
Author(s):  
Viola C. Ruddat ◽  
Rakesh Mogul ◽  
Ilya Chorny ◽  
Cameron Chen ◽  
Noah Perrin ◽  
...  

2010 ◽  
Vol 5 (1) ◽  
pp. 1934578X1000500 ◽  
Author(s):  
Isao Kubo ◽  
Tae Joung Ha ◽  
Kuniyoshi Shimizu

6-Pentadecanylsalicylic acid, referred to as anacardic acid (C15:0), was found to inhibit the linoleic acid peroxidation competitively catalyzed by soybean lipoxygenase-1 (EC 1.13.11.12, Type 1) with an IC50 of 14.3 μM (4.88 μg/mL). This inhibition is a reversible reaction without pro-oxidant effects. The inhibition kinetics analyzed by Dixon plots indicates that anacardic acid (C15:0) is a competitive inhibitor and the inhibition constant, KI, was established as 6.4 μM. The hydrophilic head (salicylic acid) portion first chelates the iron in the active site and then the hydrophobic tail portion begins reversibly interacting with the C-terminal domain where the iron is located. The inhibition of anacardic acid (C15:0) can be explained by a combination of iron ion-chelation and hydrophobic interaction abilities because of its specific structural feature.


Biochemistry ◽  
1992 ◽  
Vol 31 (33) ◽  
pp. 7700-7706 ◽  
Author(s):  
Sampath Ramachandran ◽  
Richard T. Carroll ◽  
William R. Dunham ◽  
Max O. Funk

Sign in / Sign up

Export Citation Format

Share Document