Literature summary for 1.14.12.23 extracted from

Parales, J.; Parales, R.; Resnick, S.; Gibson, D.
Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the alpha-subunit of the oxygenase component (1998), J. Bacteriol., 180, 1194-1199.

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Protein Variants

Protein Variants	Comment	Organism
additional information	construction of hybrid dioxygenases with the genes encoding 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 and 2,4-dinitrotoluene dioxygenase from Burkholderia sp. strain DNT. The C-terminal region of the large subunit of the oxygenase component is responsible for the enzyme specificity differences observed between 2-nitrotoluene 2,3-dioxygenase and 2,4-dinitrotoluene dioxygenase	Pseudomonas sp.

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas sp.	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-nitrotoluene + NADH + O2	-	Pseudomonas sp.	3-methylcatechol + nitrite + NAD+	formation of 10 nmol 3-methylcatechol per mg protein plus 1.06 nmol 2-nitrobenzyl alcohol	?
3-nitrotoluene + NADH + O2	-	Pseudomonas sp.	4-methylcatechol + nitrite + NAD+	formation of 0.06 nmol 4-methylcatechol per mg protein plus 0.03 nmol 3-nitrobenzyl alcohol	?
additional information	no substrate: 2,4-dinitrotoluene	Pseudomonas sp.	?	-	?
naphthalene + O2	-	Pseudomonas sp.	cis-1,2-dihydroxy-1,2-dihydronaphthalene	formation of 0.75 nmol 3-methylcatechol per mg protein	?

Synonyms

Synonyms	Comment	Organism
2NTDO	-	Pseudomonas sp.

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Release 2023.1 (January 2023)