Literature summary for 1.13.11.15 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

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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	Brevibacterium fuscum
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	Arthrobacter globiformis

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular docking of metsulfuron-methyl and chlorsulfon	Brevibacterium fuscum
molecular docking of metsulfuron-methyl and chlorsulfon	Arthrobacter globiformis

Organism

Organism	UniProt	Comment	Textmining
Arthrobacter globiformis	Q44048	-	-
Brevibacterium fuscum	Q45135	-	-

Synonyms

Synonyms	Comment	Organism
MndD	-	Arthrobacter globiformis

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Release 2023.1 (January 2023)