Residues in human arsenic (+3 oxidation state) methyltransferase forming potential hydrogen bond network around S-adenosylmethionine.
Residues Tyr59, Gly78, Ser79, Met103, Gln107, Ile136 and Glu137 in human arsenic (+3 oxidation state) methyltransferase (hAS3MT) were deduced to form a potential hydrogen bond network around S-adenosylmethionine (SAM) from the sequence alignment between Cyanidioschyzon merolae arsenite S-adenosylmet...
Saved in:
Main Authors: | Xiangli Li, Jing Cao, Shuping Wang, Zhirong Geng, Xiaoli Song, Xin Hu, Zhilin Wang |
---|---|
Format: | article |
Language: | EN |
Published: |
Public Library of Science (PLoS)
2013
|
Subjects: | |
Online Access: | https://doaj.org/article/5e68b321a1864b829103eae741e43277 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Development of a S-adenosylmethionine analog that intrudes the RNA-cap binding site of Zika methyltransferase
by: Rinku Jain, et al.
Published: (2017) -
Recurrent horizontal transfer of arsenite methyltransferase genes facilitated adaptation of life to arsenic
by: Song-Can Chen, et al.
Published: (2017) -
Structural evidence for inter-residue hydrogen bonding observed for cellobiose in aqueous solution.
by: William B O'Dell, et al.
Published: (2012) -
Halogen-bonded cocrystallization with phosphorus, arsenic and antimony acceptors
by: Katarina Lisac, et al.
Published: (2019) -
Effect of proline analogues on activity of human prolyl hydroxylase and the regulation of HIF signal transduction pathway.
by: Xiaoyan Ma, et al.
Published: (2014)