Intra-subunit residue interactions from the protein surface to the active site of glutathione S-transferase AdGSTD3-3 impact on structure and enzyme properties
Structural residues are one of the major factors that modulate the catalytic specificity as well as having a role in stability of the glutathione S-transferases (GST). To understand how residues remote from the active site can affect enzymatic properties, four mutants, His144Ala, Val147Leu, Val147Al...
Saved in:
Main Authors: | Jeerang Wongtrakul, Issara Sramala, La Aied Prapanthadara, Albert J. Ketterman |
---|---|
Format: | Journal |
Published: |
2018
|
Subjects: | |
Online Access: | https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=13444270611&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/62061 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Chiang Mai University |
Similar Items
-
Intra-subunit residue interactions from the protein surface to the active site of glutathione S-transferase AdGSTD3-3 impact on structure and enzyme properties
by: Jeerang Wongtrakul, et al.
Published: (2018) -
Non-active site residues Cys69 and Asp150 affected the enzymatic properties of glutathione S-transferase AdGSTD3-3
by: Jeerang Wongtrakul, et al.
Published: (2018) -
Molecular cloning and expression of several new anopheles cracens epsilon class glutathione transferases
by: Jeerang Wongtrakul, et al.
Published: (2018) -
Molecular cloning and expression of several new anopheles cracens epsilon class glutathione transferases
by: Jeerang Wongtrakul, et al.
Published: (2018) -
Molecular cloning and expression of several new anopheles cracens epsilon class glutathione transferases
by: Jeerang Wongtrakul, et al.
Published: (2018)