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Literature summary extracted from

  • Parales, R.E.; Lee, K.; Resnick, S.M.; Jiang, H.; Lessner, D.J.; Gibson, D.T
    Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme (2000), J. Bacteriol., 182, 1641-1649.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.14.12.12 D362A mutation in alpha subunit of terminal dioxygenase ISPNAP, no activity with naphthalene, biphenyl and phenanthrene Pseudomonas sp.
1.14.12.12 F202L mutation in alpha subunit of terminal dioxygenase ISPNAP, no activity with naphthalene, biphenyl and phenanthrene Pseudomonas sp.
1.14.12.12 F202V mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 F352L mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type, major product of biphenyl oxidation: biphenyl-3,4-dihydrodiol instead of biphenyl-2,3-dihydrodiol Pseudomonas sp.
1.14.12.12 F352V mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type, product of biphenyl oxidation: 96% biphenyl-3,4-dihydrodiol instead of biphenyl-2,3-dihydrodiol Pseudomonas sp.
1.14.12.12 M366W mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 N201A mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene as wild-type, very weak activity with biphenyl Pseudomonas sp.
1.14.12.12 N201Q mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 N201S mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 T351N mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 T351R mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 T351S mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 V260A mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 V260L mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 V260N mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 W316A mutation in alpha subunit of terminal dioxygenase ISPNAP, similar activity with naphthalene, biphenyl and phenanthrene as wild-type Pseudomonas sp.
1.14.12.12 W358A mutation in alpha subunit of terminal dioxygenase ISPNAP, very low activity with naphthalene and biphenyl Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.12.12 Pseudomonas sp.
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strain NCIB 9816/11, naphthalene dihydrogenase mutant derived from strain NCIB 9816-4 oxidizing naphthalene to cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene
-