Literature summary for 1.13.11.2 extracted from
Bauri, S.; Sen, M.; Das, R.; Mondal, S.
In-silico investigation of the efficiency of microbial dioxygenases in degradation of sulfonylurea group herbicides (2022), Bioremediat. J., 26, 76-87 .
No PubMed abstract available
Application
Application |
Comment |
Organism |
degradation |
comparison of binding sites and affinities using substrates chlorsulfon and metsulfuron-methyl. Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum and Arthrobacter globiformis are more effective in binding than catechol 2,3-dioxygenase from Pseudomonas putida. B. fuscum and A. globiformis have more potential than P. putida to remediate chlorsulfuron and metsulfuronmethyl |
Pseudomonas putida |
Crystallization (Commentary)
Crystallization (Comment) |
Organism |
molecular docking of metsulfuron-methyl and chlorsulfon |
Pseudomonas putida |
Organism
Organism |
UniProt |
Comment |
Textmining |
Pseudomonas putida |
Q44048 |
- |
- |
Synonyms
Synonyms |
Comment |
Organism |
XylE |
- |
Pseudomonas putida |