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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.
    View publication on PubMed
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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.