BRENDA - Enzyme Database
show all sequences of 1.18.1.7

Salicylate 5-hydroxylase from Ralstonia sp. strain U2: a monooxygenase with close relationships to and shared electron transport proteins with naphthalene dioxygenase

Zhou, N.Y.; Al-Dulayymi, J.; Baird, M.S.; Williams, P.A.; J. Bacteriol. 184, 1547-1555 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli B L21(DE3)/pLysS cells
Ralstonia sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
reduced [2Fe-2S] ferredoxin + NAD+ + H+
Ralstonia sp.
-
oxidized [2Fe-2S] ferredoxin + NADH
-
-
?
reduced [2Fe-2S] ferredoxin + NAD+ + H+
Ralstonia sp. U2
-
oxidized [2Fe-2S] ferredoxin + NADH
-
-
?
reduced [2Fe-2S] ferredoxin + NADP+ + H+
Ralstonia sp.
-
oxidized [2Fe-2S] ferredoxin + NADPH
-
-
?
reduced [2Fe-2S] ferredoxin + NADP+ + H+
Ralstonia sp. U2
-
oxidized [2Fe-2S] ferredoxin + NADPH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ralstonia sp.
O52378
-
-
Ralstonia sp. U2
O52378
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
722507
Ralstonia sp.
oxidized [2Fe-2S] ferredoxin + NADH
-
-
-
?
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
722507
Ralstonia sp. U2
oxidized [2Fe-2S] ferredoxin + NADH
-
-
-
?
reduced [2Fe-2S] ferredoxin + NADP+ + H+
-
722507
Ralstonia sp.
oxidized [2Fe-2S] ferredoxin + NADPH
-
-
-
?
reduced [2Fe-2S] ferredoxin + NADP+ + H+
-
722507
Ralstonia sp. U2
oxidized [2Fe-2S] ferredoxin + NADPH
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Ralstonia sp.
NADP+
-
Ralstonia sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli B L21(DE3)/pLysS cells
Ralstonia sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Ralstonia sp.
NADP+
-
Ralstonia sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
reduced [2Fe-2S] ferredoxin + NAD+ + H+
Ralstonia sp.
-
oxidized [2Fe-2S] ferredoxin + NADH
-
-
?
reduced [2Fe-2S] ferredoxin + NAD+ + H+
Ralstonia sp. U2
-
oxidized [2Fe-2S] ferredoxin + NADH
-
-
?
reduced [2Fe-2S] ferredoxin + NADP+ + H+
Ralstonia sp.
-
oxidized [2Fe-2S] ferredoxin + NADPH
-
-
?
reduced [2Fe-2S] ferredoxin + NADP+ + H+
Ralstonia sp. U2
-
oxidized [2Fe-2S] ferredoxin + NADPH
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
722507
Ralstonia sp.
oxidized [2Fe-2S] ferredoxin + NADH
-
-
-
?
reduced [2Fe-2S] ferredoxin + NAD+ + H+
-
722507
Ralstonia sp. U2
oxidized [2Fe-2S] ferredoxin + NADH
-
-
-
?
reduced [2Fe-2S] ferredoxin + NADP+ + H+
-
722507
Ralstonia sp.
oxidized [2Fe-2S] ferredoxin + NADPH
-
-
-
?
reduced [2Fe-2S] ferredoxin + NADP+ + H+
-
722507
Ralstonia sp. U2
oxidized [2Fe-2S] ferredoxin + NADPH
-
-
-
?
General Information
General Information
Commentary
Organism
metabolism
ferredoxin reductase NagAa is required for salicylate transformation
Ralstonia sp.
General Information (protein specific)
General Information
Commentary
Organism
metabolism
ferredoxin reductase NagAa is required for salicylate transformation
Ralstonia sp.
Other publictions for EC 1.18.1.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745688
Peng
Metabolic engineering of Arab ...
Pseudomonas putida, Pseudomonas putida G7
Metab. Eng.
26
100-110
2014
-
-
1
-
-
-
-
-
-
-
-
2
-
11
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
722507
Zhou
Salicylate 5-hydroxylase from ...
Ralstonia sp., Ralstonia sp. U2
J. Bacteriol.
184
1547-1555
2002
-
-
1
-
-
-
-
-
-
-
-
4
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
437842
Haigler
Purification and properties of ...
Pseudomonas putida, Pseudomonas putida NCIB 9816
J. Bacteriol.
172
457-464
1990
-
-
-
-
-
-
5
-
-
1
3
-
-
3
-
-
1
-
-
-
1
1
10
1
-
-
1
-
-
-
-
2
-
1
1
-
-
-
2
-
-
-
1
5
-
-
-
1
3
-
-
-
-
1
-
-
1
1
10
1
-
-
1
-
-
-
-
1
-
-
-
-
-
-
722477
Haigler
Purification and properties of ...
Pseudomonas putida, Pseudomonas putida NCIB 9816
J. Bacteriol.
172
465-468
1990
-
-
-
-
-
-
-
-
-
1
1
-
-
3
-
-
1
-
-
-
4
-
4
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
4
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-