1.14.13.1: salicylate 1-monooxygenase This is an abbreviated version! For detailed information about salicylate 1-monooxygenase, go to the full flat file .
Reaction
salicylate +
NADH +
H+ +
O2 =
catechol +
NAD+ +
H2O +
CO2
Synonyms Efe-shyA, FAD/NADH-dependent SA 1-hydroxylase, FAD_binding_3 domain-containing protein, FGSG_03657, FgShy1, FgShyC, flavin-dependent monooxygenase salicylate hydroxylase, NahG, NahU, NRRL3_9723, oxygenase, salicylate 1-mono-, SA 1-decarboxylase/hydroxylase, SA 1-hydroxylase, SA hydroxylase, SA1H, SahA, salA, salcylic acid 1-hydroxylase, SALH, salicylate 1-hydroxylase, Salicylate 1-monooxygenase, salicylate hydroxylase, salicylate hydroxylase (decarboxylating), salicylate monooxygenase, salicylate, NADH: oxygen oxidoreductase, salicylate, NADH: oxygen oxidoreductase (1-hydroxylating, decarboxylating), salicylate-1-hydroxylase, salicylic acid hydroxylase, salicylic hydroxylase, SalOH, SHL, Shy1, ShyA, ShyC, SlSA 1H, SlSA1H, Solyc08g063130
ECTree
KM Value
KM Value on EC 1.14.13.1 - salicylate 1-monooxygenase
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0.004
1-hydroxy-2-naphthoate
-
-
0.028
2,3-Dihydroxybenzoate
0.143
2,4-dihydroxybenzoat
-
cosubstrate NADH
-
0.065
2,5-Dihydroxybenzoate
0.011
2,6-dihydroxybenzoate
0.0038
3-chlorosalicylate
pH not specified in the publication, 25°C
0.0127
3-methylsalicylate
pH not specified in the publication, 25°C
0.0042
4-(3-benzothiazol-2-yl-4-cyano-2-oxo-2H-chromen-7-yloxymethyl)-2-hydroxy-benzoic acid
-
pH 8.0, 37°C
0.0028
4-chlorosalicylate
pH not specified in the publication, 25°C
0.0158
4-methylsalicylate
pH not specified in the publication, 25°C
0.0006
5-chlorosalicylate
pH not specified in the publication, 25°C
0.0024
5-Methylsalicylate
pH not specified in the publication, 25°C
0.028
anthranilate
-
30°C, pH 7.0
0.087
Salicylaldehyde
-
-
0.0005 - 0.1388
salicylate
additional information
additional information
-
0.028
2,3-Dihydroxybenzoate
-
-
0.028
2,3-Dihydroxybenzoate
-
cosubstrate NADH
0.065
2,5-Dihydroxybenzoate
-
-
0.065
2,5-Dihydroxybenzoate
-
cosubstrate NADH
0.011
2,6-dihydroxybenzoate
-
-
0.011
2,6-dihydroxybenzoate
-
cosubstrate NADH
0.0026
NADH
-
-
0.0037
NADH
-
native enzyme
0.0158
NADH
pH not specified in the publication, 25°C
0.017
NADH
-
cosubstrate salicylate
0.02326
NADH
-
enzyme form NahG
0.044
NADH
-
cosubstrate p-aminosalicylate
0.049
NADH
-
modified enzyme
0.07974
NADH
-
enzyme form NahU
0.091
NADH
-
cosubstrate 2,3-dihydroxybenzoate
0.118
NADH
-
cosubstrate salicylaldehyde
0.14
NADH
-
cosubstrate 2,4-dihydroxybenzoate
0.23
NADH
-
cosubstrate 2,5-dihydroxybenzoate or 2,6-dihydroxybenzoate
0.1
NADPH
-
cosubstrate salicylate
0.1
NADPH
-
cosubstrates O2 and salicylate
0.034
o-Nitrophenol
-
-
0.034
o-Nitrophenol
-
cosubstrate NADH
0.13
O2
-
cosubstrate o-nitrophenol
0.196
O2
-
cosubstrates salicylate and NADH
0.015
p-Aminosalicylate
-
-
0.015
p-Aminosalicylate
-
cosubstrate NADH
0.0005
salicylate
-
enzyme form NahG
0.0011
salicylate
-
30°C, pH 7.0
0.0013
salicylate
-
at pH 7.5, temperature not specified in the publication
0.0016
salicylate
-
native enzyme
0.0016
salicylate
-
cosubstrate NADH
0.0016
salicylate
-
pH 8.0, 37°C
0.0018
salicylate
-
modified enzyme
0.0027
salicylate
-
cosubstrate NADH
0.0031
salicylate
-
at pH 7.5, temperature not specified in the publication
0.00494
salicylate
-
enzyme form NahU
0.0091
salicylate
recombinant enzyme, pH and temperature not specified in the publication
0.0096
salicylate
pH not specified in the publication, 25°C
0.1388
salicylate
-
pH 6.0, 45°C, recombinant enzyme
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
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FAD, salicylate and NADH, comparison of wild-type, recombinant and mutant enzyme
-
additional information
additional information
kinetic analysis, rate-limiting steps, detailed overview
-
additional information
additional information
-
the kinetic profile of ShyA, obtained while only varying the salicylic acid concentration at a constant 1 mM concentration of the second substrate (NADH), does not follow Michaelis-Menten kinetics. ShyA reveals a sigmoidal curve. This may be caused by inhibition or inactivation due to low salicylate concentrations and relatively high NADH concentrations
-