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Literature summary extracted from

  • Ferraroni, M.; Steimer, L.; Matera, I.; Buerger, S.; Scozzafava, A.; Stolz, A.; Briganti, F.
    The generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutations of salicylate 1,2-dioxygenase - rational design of mutants and the crystal structures of the A85H and W104Y variants (2012), J. Struct. Biol., 180, 563-571.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.38 expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Pseudaminobacter salicylatoxidans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.38 mutant A85H and W104Y variants and mutant W104Y with gentiate, sitting drop vapor diffusion method, 4°C, mixing of 0.001 ml of protein solution with 0.0008 ml of crystallization solution containing 8% PEG10000 and 0.1 M Tris-HCl pH 8.0, with 0.0002 ml of a 0.1 M calcium chloride solution, crystals quality is also improved using seeding techniques, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution Pseudaminobacter salicylatoxidans

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.38 A85H site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate than the wild-type enzyme and no more activity with gentisate. substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected. Pseudaminobacter salicylatoxidans
1.13.11.38 L38Q site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate than the wild-type enzyme Pseudaminobacter salicylatoxidans
1.13.11.38 additional information generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutation M46V of salicylate 1,2-dioxygenase, rational design of mutants, structure comparisons, overview Pseudaminobacter salicylatoxidans
1.13.11.38 W104Y site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows increased catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate and to the wild-type enzyme. W104Y SDO mutant exhibits reduced reaction rates for all substrates Pseudaminobacter salicylatoxidans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.38 0.046
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant M46V Pseudaminobacter salicylatoxidans
1.13.11.38 0.08
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant A85H Pseudaminobacter salicylatoxidans
1.13.11.38 0.08
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant L38Q Pseudaminobacter salicylatoxidans
1.13.11.38 0.14
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, wild-type enzyme Pseudaminobacter salicylatoxidans
1.13.11.38 0.144
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant W104Y Pseudaminobacter salicylatoxidans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.38 Fe2+ salicylate 1,2-dioxygenase is an iron (II) class III ring cleaving dioxygenase Pseudaminobacter salicylatoxidans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.38 1-hydroxy-2-naphthoate + O2 Pseudaminobacter salicylatoxidans
-
 (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
 ?
1.13.11.38 1-hydroxy-2-naphthoate + O2 Pseudaminobacter salicylatoxidans BN12
-
 (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.38 Pseudaminobacter salicylatoxidans
-
-
-
1.13.11.38 Pseudaminobacter salicylatoxidans BN12
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.38 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Pseudaminobacter salicylatoxidans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.38 1-hydroxy-2-naphthoate + O2
-
 Pseudaminobacter salicylatoxidans (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
 ?
1.13.11.38 1-hydroxy-2-naphthoate + O2
-
 Pseudaminobacter salicylatoxidans BN12 (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.38 1-hydroxy-2-naphthoate 1,2-dioxygenase
-
 Pseudaminobacter salicylatoxidans
1.13.11.38 1H2NDO
-
 Pseudaminobacter salicylatoxidans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.38 2.2
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant L38Q Pseudaminobacter salicylatoxidans
1.13.11.38 3.31
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant A85H Pseudaminobacter salicylatoxidans
1.13.11.38 4.6
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant W104Y Pseudaminobacter salicylatoxidans
1.13.11.38 17
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant M46V Pseudaminobacter salicylatoxidans
1.13.11.38 24
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, wild-type enzyme Pseudaminobacter salicylatoxidans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.38 8
-
 assay at Pseudaminobacter salicylatoxidans

General Information

EC Number General Information Comment Organism
1.13.11.38 additional information salicylate 1,2-dioxygenase shares with 1-hydroxy-2-naphthoate dioxygenase its unique ability to oxidatively cleave monohydroxylated aromatic compounds. Nevertheless salicylate 1,2-dioxygenase is more versatile with respect to 1-hydroxy-2-naphthoate dioxygenase and other known gentisate dioxygenases because it cleaves not only gentisate and1-hydroxy-2-naphthoate but also salicylate and substituted salicylates, cf. EC 1.13.11.4 Pseudaminobacter salicylatoxidans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.13.11.38 27.5
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant L38Q Pseudaminobacter salicylatoxidans
1.13.11.38 32
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant W104Y Pseudaminobacter salicylatoxidans
1.13.11.38 41.4
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant A85H Pseudaminobacter salicylatoxidans
1.13.11.38 171
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, wild-type enzyme Pseudaminobacter salicylatoxidans
1.13.11.38 369.6
-
 1-hydroxy-2-naphthoate pH 8.0, temperature not specified in the publication, mutant M46V Pseudaminobacter salicylatoxidans