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EC Tree
IUBMB Comments This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.7, ferredoxin---NAD(P)+ reductase), an iron-sulfur oxygenase, and ferredoxin.
The enzyme appears in viruses and cellular organisms
Synonyms
nagG , NagGH,
nagH , S5H, SAL5H, SalABCD, SALD,
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SALD
enzyme complex component
nagG
-
-
-
-
NagGH
-
nagH
-
-
-
-
S5H
-
S5H
a three-component system consisting of NagGH (the oxygenase components), NagAa (ferredoxin reductase), and NagAb (ferredoxin)
S5H
a three-component system consisting of NagGH (the oxygenase components), NagAa (ferredoxin reductase), and NagAb (ferredoxin)
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SAL5H
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-
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salicylate + NADH + H+ + O2 = 2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
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salicylate,NADH:oxygen oxidoreductase (5-hydroxylating)
This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.7, ferredoxin---NAD(P)+ reductase), an iron-sulfur oxygenase, and ferredoxin.
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2,4-dihydroxybenzoate + NADH + H+ + O2
?
2,6-dihydroxybenzoate + NADH + H+ + O2
?
2-nitrophenol + NADH + H+ + O2
?
anthranilate + NADH + H+ + O2
5-hydroxyanthranilate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
additional information
?
-
2,4-dihydroxybenzoate + NADH + H+ + O2
?
-
-
-
?
2,4-dihydroxybenzoate + NADH + H+ + O2
?
-
-
-
?
2,6-dihydroxybenzoate + NADH + H+ + O2
?
-
-
-
?
2,6-dihydroxybenzoate + NADH + H+ + O2
?
-
-
-
?
2-nitrophenol + NADH + H+ + O2
?
-
-
-
?
2-nitrophenol + NADH + H+ + O2
?
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
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-
-
-
?
additional information
?
-
2-aminobenzoate might be a substrate for the enzyme
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-
?
additional information
?
-
no activity is detected against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate, and 2-hydroxyacetophenone
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-
?
additional information
?
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-
no activity is detected against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate, and 2-hydroxyacetophenone
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-
?
additional information
?
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no activity is detected against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate, and 2-hydroxyacetophenone
-
-
?
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salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
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additional information
SalABCD requires NAD(P)H as the cofactor instead of BH4
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NADH
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-
NADPH
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[2Fe-2S]-center
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[2Fe-2S]-center
contains a Rieske-type iron-sulfur center
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Iron
the enzyme contains one Rieske-type [2Fe-2S] cluster and 7.5 g iron per mol enzyme
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0.9398
2,6-dihydroxybenzoate
in 50 mM MES buffer (pH 6.4), at 22°C
0.3284
2-Nitrophenol
in 50 mM MES buffer (pH 6.4), at 22°C
0.05976
NADH
in 50 mM MES buffer (pH 6.4), at 22°C
0.05641
NADPH
in 50 mM MES buffer (pH 6.4), at 22°C
0.1071
salicylate
in 50 mM MES buffer (pH 6.4), at 22°C
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0.051
in 50 mM MES buffer, pH 6.4, at 30°C
107.1
after 124fold purification, in 50 mM MES buffer (pH 6.4), at 22°C
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-
UniProt
brenda
large oxygenase component and small oxagenase component
UniProt
brenda
large oxygenase component and small oxagenase component
UniProt
brenda
large oxygenase component and small oxagenase component
UniProt
brenda
large oxygenase component and small oxagenase component
UniProt
brenda
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brenda
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brenda
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physiological function
enzyme S5H hydroxylates salicylate into gentisate and is involved in the degradation of aromatic compounds. SalD is an essential component of the S5H complex
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20000
3 * 52000 + 3 * 20000, His6-tagged enzyme, SDS-PAGE
45000
-
4 * 45000, SDS-PAGE
48799
x * 48799 + x * 18800, calculated from amino acid sequence
51000
3 * 51000 + 3 * 18800, His6-tagged enzyme, calculated from amino acid sequence
52000
3 * 52000 + 3 * 20000, His6-tagged enzyme, SDS-PAGE
18800
3 * 51000 + 3 * 18800, His6-tagged enzyme, calculated from amino acid sequence
18800
x * 48799 + x * 18800, calculated from amino acid sequence
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?
x * 48799 + x * 18800, calculated from amino acid sequence
?
-
x * 48799 + x * 18800, calculated from amino acid sequence
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heterohexamer
3 * 51000 + 3 * 18800, His6-tagged enzyme, calculated from amino acid sequence
heterohexamer
3 * 52000 + 3 * 20000, His6-tagged enzyme, SDS-PAGE
heterohexamer
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3 * 51000 + 3 * 18800, His6-tagged enzyme, calculated from amino acid sequence
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heterohexamer
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3 * 52000 + 3 * 20000, His6-tagged enzyme, SDS-PAGE
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homotetramer
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4 * 45000, SDS-PAGE
homotetramer
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4 * 45000, SDS-PAGE
-
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additional information
precursor-directed biosynthesis of 5-hydroxytryptophan using metabolically engineered Escherichia coli and involving the salicylate 5-hydroxylase from Ralstonia eutropha strain H16
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the three-component Fe-S protein complex (NagAaGHAb) of the enzyme is purified by HisTrap column chromatography and Sephadex G-25 gel filtration
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enzyme S5H is encoded in the salABCD gene cluster, which locates on the chromosome rather than on a mobile plasmid, functional recombinant expression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)/pLysS cells
expressed in Escherichia coli DH5alpha cells
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Suemori, A.; Nakajima, K.; Kurane, R.; Nakamura, Y.
Physicochemical and immunochemical characterization of salicylate 5-hydroxylase, m-hydroxybenzoate 6-hydroxylase and p-hydroxybenzoate 3-hydroxylase from Rhodococcus erythropolis
Biotechnol. Lett.
17
1063-1068
1995
Rhodococcus erythropolis, Rhodococcus erythropolis S1
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brenda
Fang, T.; Zhou, N.Y.
Purification and characterization of salicylate 5-hydroxylase, a three-component monooxygenase from Ralstonia sp. strain U2
Appl. Microbiol. Biotechnol.
98
671-679
2014
Ralstonia sp. (O52379 and O52380), Ralstonia sp., Ralstonia sp. U2 (O52379 and O52380)
brenda
Fuenmayor, S.L.; Wild, M.; Boyes, A.L.; Williams, P.A.
A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2
J. Bacteriol.
180
2522-2530
1998
Pseudomonas sp. (O52379 and O52380), Pseudomonas sp., Pseudomonas sp. U2 (O52379 and O52380)
brenda
Zhou, N.Y.; Al-Dulayymi, J.; Baird, M.S.; Williams, P.A.
Salicylate 5-hydroxylase from Ralstonia sp. strain U2: a monooxygenase with close relationships to and shared electron transport proteins with naphthalene dioxygenase
J. Bacteriol.
184
1547-1555
2002
Ralstonia sp. (O52379 and O52380), Ralstonia sp., Ralstonia sp. U2 (O52379 and O52380)
brenda
Sun, X.; Lin, Y.; Yuan, Q.; Yan, Y.
Precursor-directed biosynthesis of 5-hydroxytryptophan using metabolically engineered E. coli
ACS Synth. Biol.
4
554-558
2015
Cupriavidus necator (Q0KB56)
brenda
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Enzyme Nomenclature
1.14.13.172 salicylate 5-hydroxylase
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