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2-iminoacetate + H2O
glyoxylate + NH3
cephalosporin C + H2O + O2
?
cyclopropylglycine + H2O + O2
?
D-2-aminobutyrate + H2O + O2
2-oxobutyrate + H2O2
-
as active as sarcosine
-
-
?
D-2-aminobutyrate + H2O + O2
? + NH3 + H2O2
-
2.2% of the activity with sarcosine
-
-
?
D-4-hydroxyphenylglycine + H2O + O2
?
D-Ala + H2O + O2
? + NH3 + H2O2
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
D-aminobutanoate + H2O + O2
? + H2O2
-
30% of the activity with sarcosine
-
-
?
D-Arg + H2O + O2
? + H2O2
-
about 35% of the activity with sarcosine
-
-
?
D-glutamate + H2O + O2
?
-
0.2% activity compared to glycine
-
-
?
D-His + H2O + O2
? + H2O2
-
about 25% of the activity with sarcosine
-
-
?
D-Ile + H2O + O2
3-methyl-2-oxopentanoate + H2O2
-
about 30% of the activity with sarcosine
-
-
?
D-Leu + H2O + O2
4-methyl-2-oxopentanoate + H2O2
-
about 35% of the activity with sarcosine
-
-
?
D-lysine + H2O + O2
?
-
0.2% activity compared to glycine
-
-
?
D-methionine + H2O + O2
4-(methylsulfanyl)-2-oxobutanoic acid + NH3 + H2O2
D-methionine + H2O + O2
?
-
-
-
-
?
D-norvaline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
D-pipecolate + H2O + O2
?
D-pipecolate + H2O + O2
? + H2O2
D-Pro + H2O + O2
? + H2O2
-
about 120% of the activity with sarcosine
-
-
?
D-Pro + H2O + O2
? + NH3 + H2O2
D-Val + H2O + O2
3-methyl-2-oxobutanoate + H2O2
-
about 35% of the activity with sarcosine
-
-
?
D-Val + H2O + O2
? + NH3 + H2O2
-
4.8% of the activity with sarcosine
-
-
?
D-valine + H2O + O2
3-methyl-2-oxobutanoic acid + NH3 + H2O2
glycine + H2O + O2
glyoxylate + NH3 + H2O2
glycine + O2
2-iminoacetate + H2O2
glycine + O2 + H2O
glyoxylate + H2O2 + NH3
glycine ethyl ester + H2O + O2
?
glycine-ethyl-ester + H2O + O2
?
glycine-ethyl-ester + H2O + O2
? + H2O2
glycylglycine + H2O + O2
?
3% activity compared to glycine
-
-
?
glyphosate + H2O + O2
? + H2O2
-
110% of the activity with sarcosine
-
-
?
glyphosate + H2O + O2
glyoxylate + aminomethylphosphonic acid + NH3 + H2O2
N-ethylglycine + H2O + O2
?
N-ethylglycine + H2O + O2
glyoxylate + ethylamine + H2O2
N-ethylglycine + H2O + O2
glyoxylate + NH3 + H2O2
N-methyl-D-Ala + H2O + O2
? + H2O2
-
75% of the activity with sarcosine
-
-
?
N-methyl-D-Ala + H2O + O2
? + NH3 + H2O2
-
16.9% of the activity with sarcosine
-
-
-
N-methyl-D-Ala + H2O + O2
pyruvate + methylamine + H2O2
-
about 110% of the activity with sarcosine
-
-
?
sarcosine + H2O + O2
glyoxylate + methylamine + H2O2
additional information
?
-
2-iminoacetate + H2O

glyoxylate + NH3
-
-
-
-
?
2-iminoacetate + H2O
glyoxylate + NH3
-
-
-
-
?
2-iminoacetate + H2O
glyoxylate + NH3
-
-
-
-
?
2-iminoacetate + H2O
glyoxylate + NH3
-
-
-
?
2-iminoacetate + H2O
glyoxylate + NH3
-
-
-
-
?
cephalosporin C + H2O + O2

?
-
-
-
-
?
cephalosporin C + H2O + O2
?
-
-
-
-
?
cyclopropylglycine + H2O + O2

?
-
-
-
?
cyclopropylglycine + H2O + O2
?
enzyme is required for the biosynthesis of the thiazole moiety of thiamine diphosphate
-
-
?
D-4-hydroxyphenylglycine + H2O + O2

?
-
0.6% activity compared to glycine
-
-
?
D-4-hydroxyphenylglycine + H2O + O2
?
-
0.6% activity compared to glycine
-
-
?
D-Ala + H2O + O2

? + NH3 + H2O2
-
40% of the activity with sarcosine
-
-
?
D-Ala + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
D-Ala + H2O + O2

pyruvate + NH3 + H2O2
-
7.4% of the activity with sarcosine
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
no activity with D-Ala
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
about 115% of the activity with sarcosine
-
-
?
D-alanine + H2O + O2

?
-
-
-
?
D-alanine + H2O + O2
?
-
-
-
?
D-alanine + H2O + O2
?
10% activity compared to glycine
-
-
?
D-alanine + H2O + O2
?
10% activity compared to glycine
-
-
?
D-alanine + H2O + O2

pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
-
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
0.2% activity compared to glycine
-
-
?
D-alanine + H2O + O2
pyruvate + NH3 + H2O2
-
0.2% activity compared to glycine
-
-
?
D-arginine + H2O + O2

?
-
-
-
-
?
D-arginine + H2O + O2
?
-
-
-
-
?
D-aspartate + H2O + O2

?
-
-
-
-
?
D-aspartate + H2O + O2
?
-
-
-
-
?
D-methionine + H2O + O2

4-(methylsulfanyl)-2-oxobutanoic acid + NH3 + H2O2
-
25% of the activity with sarcosine
-
-
?
D-methionine + H2O + O2
4-(methylsulfanyl)-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-methionine + H2O + O2
4-(methylsulfanyl)-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-norvaline + H2O + O2

2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-norvaline + H2O + O2
2-oxopentanoic acid + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2

phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
D-pipecolate + H2O + O2

?
-
-
-
-
?
D-pipecolate + H2O + O2
?
-
-
-
-
?
D-pipecolate + H2O + O2
?
-
-
-
-
?
D-pipecolate + H2O + O2

? + H2O2
-
about 85% of the activity with sarcosine
-
-
?
D-pipecolate + H2O + O2
? + H2O2
-
70% of the activity with sarcosine
-
-
?
D-Pro + H2O + O2

? + NH3 + H2O2
-
-
-
-
?
D-Pro + H2O + O2
? + NH3 + H2O2
-
15.1% of the activity with sarcosine
-
-
?
D-Pro + H2O + O2
? + NH3 + H2O2
-
110% of the activity with sarcosine
-
-
?
D-Pro + H2O + O2
? + NH3 + H2O2
-
-
-
-
?
D-proline + H2O + O2

?
-
-
-
-
?
D-proline + H2O + O2
?
-
-
-
-
?
D-proline + H2O + O2
?
-
0.3% activity compared to glycine
-
-
?
D-proline + H2O + O2
?
-
0.3% activity compared to glycine
-
-
?
D-proline + H2O + O2
?
25% activity compared to glycine
-
-
?
D-proline + H2O + O2
?
25% activity compared to glycine
-
-
?
D-valine + H2O + O2

3-methyl-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
D-valine + H2O + O2
3-methyl-2-oxobutanoic acid + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2

glyoxylate + NH3 + H2O2
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
r
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
free glycine oxidase forms the anionic red semiquinone upon photoreduction.This species is thermodynamically stable, as indicated by the large separation of the two single-electron reduction potentials of DeltaE 290 mV. The first potential is pH-independent, while the second is dependent. The midpoint reduction potential exhibits a 23.4 mV/pH unit slope, which is consistent with an overall two-electrons/one-proton transfer in the reduction to yield anionic reduced flavin. In the presence of glycolate and at pH 7.5 the potential for the semiquinone-reduced enzyme couple is shifted positively by about 160 mV, this favors a two-electron transfer compared to the free enzyme. Binding of glycolate and sulfite is also affected by pH
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
77.4% of the activity with sarcosine
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
as active as sarcosine
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
85% of the activity with sarcosine
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
r
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
100% activity
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
100% activity
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
?
glycine + O2

2-iminoacetate + H2O2
-
-
-
-
?
glycine + O2
2-iminoacetate + H2O2
-
-
-
?
glycine + O2
2-iminoacetate + H2O2
-
-
-
?
glycine + O2
2-iminoacetate + H2O2
-
-
-
-
?
glycine + O2
2-iminoacetate + H2O2
-
-
-
-
?
glycine + O2
2-iminoacetate + H2O2
-
-
-
?
glycine + O2
2-iminoacetate + H2O2
-
-
-
-
?
glycine + O2 + H2O

glyoxylate + H2O2 + NH3
-
-
-
-
?
glycine + O2 + H2O
glyoxylate + H2O2 + NH3
-
using samples of [2-RS-3H2,2-14C]-, [2-R-3H,2-14C]-, and [2-S-3H,2-14C]glycine, HSi is removed in the overall process. Incubation of the enzyme with [2-RS-3H2,2-14C]glycine under anaerobic conditions, when only the reducing half of the reaction can occur, leads to the recovery of 98.5% of the original glycine, which has the same 3H:14C ratio as the starting substrate. Isotope effects, overview
-
-
?
glycine + O2 + H2O
glyoxylate + H2O2 + NH3
-
-
-
-
?
glycine + O2 + H2O
glyoxylate + H2O2 + NH3
-
using samples of [2-RS-3H2,2-14C]-, [2-R-3H,2-14C]-, and [2-S-3H,2-14C]glycine, HSi is removed in the overall process. Incubation of the enzyme with [2-RS-3H2,2-14C]glycine under anaerobic conditions, when only the reducing half of the reaction can occur, leads to the recovery of 98.5% of the original glycine, which has the same 3H:14C ratio as the starting substrate. Isotope effects, overview
-
-
?
glycine ethyl ester + H2O + O2

?
-
30.7% activity compared to glycine
-
-
?
glycine ethyl ester + H2O + O2
?
5% activity compared to glycine
-
-
?
glycine ethyl ester + H2O + O2
?
5% activity compared to glycine
-
-
?
glycine-ethyl-ester + H2O + O2

?
-
-
-
-
?
glycine-ethyl-ester + H2O + O2
?
-
-
-
-
?
glycine-ethyl-ester + H2O + O2

? + H2O2
-
90% of the activity with sarcosine
-
-
?
glycine-ethyl-ester + H2O + O2
? + H2O2
-
-
-
-
?
glyphosate + H2O + O2

?
-
-
-
?
glyphosate + H2O + O2
?
-
the wild type enzyme shows very low activity with glyphosate
-
-
?
glyphosate + H2O + O2
?
-
-
-
?
glyphosate + H2O + O2
?
-
-
-
?
glyphosate + H2O + O2
?
-
-
-
?
glyphosate + H2O + O2

glyoxylate + aminomethylphosphonic acid + NH3 + H2O2
-
-
-
-
?
glyphosate + H2O + O2
glyoxylate + aminomethylphosphonic acid + NH3 + H2O2
-
-
-
-
?
N-ethylglycine + H2O + O2

?
-
0.3% activity compared to glycine
-
-
?
N-ethylglycine + H2O + O2
?
40% activity compared to glycine
-
-
?
N-ethylglycine + H2O + O2

glyoxylate + ethylamine + H2O2
-
-
-
-
?
N-ethylglycine + H2O + O2
glyoxylate + ethylamine + H2O2
-
about 65% of the activity with sarcosine
-
-
?
N-ethylglycine + H2O + O2
glyoxylate + ethylamine + H2O2
-
120% of the activity with sarcosine
-
-
?
N-ethylglycine + H2O + O2
glyoxylate + ethylamine + H2O2
-
-
-
-
?
N-ethylglycine + H2O + O2

glyoxylate + NH3 + H2O2
-
85.3% of the activity with sarcosine
-
-
?
N-ethylglycine + H2O + O2
glyoxylate + NH3 + H2O2
-
-
-
-
?
sarcosine + H2O + O2

?
-
-
-
?
sarcosine + H2O + O2
?
-
-
-
?
sarcosine + H2O + O2
?
-
0.1% activity compared to glycine
-
-
?
sarcosine + H2O + O2
?
-
0.1% activity compared to glycine
-
-
?
sarcosine + H2O + O2
?
-
-
-
?
sarcosine + H2O + O2
?
-
-
-
?
sarcosine + H2O + O2

glyoxylate + methylamine + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glyoxylate + methylamine + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glyoxylate + methylamine + H2O2
-
-
-
?
sarcosine + H2O + O2
glyoxylate + methylamine + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glyoxylate + methylamine + H2O2
-
-
-
-
?
additional information

?
-
-
glycine oxidase is converted to a two-electron reduced form upon anaerobic reduction with the individual substrates and its reductive half-reaction is reversible
-
-
-
additional information
?
-
-
a general catabolic role of the enzyme on primary or secondary amines is excluded, because the expression of glycine oxidase is not inducible by Gly, sarcosine, or D-Ala as carbon or nitrogen source
-
-
-
additional information
?
-
-
the enzyme is strictly stereospecific as it only catalyzes the oxidation of the D-isomer
-
-
-
additional information
?
-
no activity with L-alanine
-
-
-
additional information
?
-
no activity with L-alanine
-
-
-
additional information
?
-
-
no activity with butilamine, benzilamine, D-histidine, D-leucine, L-proline, D-tryptophan, and D-tyrosine
-
-
-
additional information
?
-
-
substrate preference for amines of small size, like glycine, sarcosine, N-ethyl-glycine, and glycine-ethylester
-
-
-
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1.17
cyclopropylglycine
-
-
221.8 - 2000
D-pipecolate
0.29 - 1.8
glycine-ethyl-ester
0.71 - 2.8
N-ethyl-glycine
0.22 - 7.68
N-ethylglycine
4 - 10
D-alanine

-
apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
20.6
D-alanine
-
in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C
20.6
D-alanine
-
pH 8.5, 37°C
34.65
D-alanine
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
121.9
D-alanine
-
M261Y mutant
155.6
D-alanine
-
M261H mutant
217
D-alanine
-
mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
315
D-alanine
-
M261 wild type
315
D-alanine
-
wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
350
D-alanine
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
420
D-alanine
-
apparent value for mutant enzyme H244N, at 25°C and pH 8.5
490
D-alanine
-
apparent value for wild type enzyme, at 25°C and pH 8.5
530
D-alanine
-
apparent value for mutant enzyme H244F, at 25°C and pH 8.5
2000
D-alanine
-
Km above 2000 mM, apparent value for mutant enzyme M261H, at 25°C and pH 8.5
221.8
D-pipecolate

-
in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C
221.8
D-pipecolate
-
pH 8.5, 37°C
290
D-pipecolate
-
mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
2000
D-pipecolate
-
wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
46
D-Pro

-
-
2.06
D-proline

-
M261Y mutant
3.91
D-proline
-
M261H mutant
7.9
D-proline
-
mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
8.9
D-proline
-
M261 wild type
8.9
D-proline
-
wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
9.3
D-proline
-
in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C
9.3
D-proline
-
pH 8.5, 37°C
17
D-proline
-
apparent value for wild type enzyme, at 25°C and pH 8.5
26
D-proline
-
apparent value for mutant enzyme H244F, at 25°C and pH 8.5; apparent value for mutant enzyme H244N, at 25°C and pH 8.5
27
D-proline
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
31.7
D-proline
at pH 8.5 and 40°C
280
D-proline
-
apparent value for mutant enzyme M261H, at 25°C and pH 8.5
285
D-proline
-
apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
0.99
Gly

-
-
0.14
glycine

-
mutant enzyme H244K, at pH 8.5 and 25°C
0.18
glycine
-
M261Y mutant
0.24
glycine
-
mutant enzyme H244R, at pH 8.5 and 25°C
0.25
glycine
-
in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C
0.25
glycine
-
pH 8.5, 37°C
0.3
glycine
-
mutant enzyme H244K/M261R, at pH 8.5 and 25°C
0.31
glycine
-
mutant enzyme M49I, at pH 8.5 and 25°C
0.37
glycine
at pH 8.0 and 50°C
0.4
glycine
-
mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
0.53
glycine
-
mutant enzyme N336R, at pH 7.5, temperature not specified in the publication
0.56
glycine
-
M261 wild type
0.6
glycine
-
apparent value for mutant enzyme H244F, at 25°C and pH 8.5
0.6
glycine
-
wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
0.7
glycine
-
apparent value for wild type enzyme, at 25°C and pH 8.5
0.7
glycine
-
wild-type, pH 8.5, 25°C
0.7
glycine
-
wild type enzyme, at pH 8.5 and 25°C
0.79
glycine
-
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
0.8
glycine
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
0.826
glycine
-
mutant enzyme F237A, at 30°C, pH not specified in the publication
0.9
glycine
-
mutant enzyme H244Q, at pH 8.5 and 25°C
0.95
glycine
-
mutant enzyme N336H, at pH 7.5, temperature not specified in the publication
0.97
glycine
-
M261H mutant
0.99
glycine
-
mutant enzyme D60G, at pH 8.5 and 60°C
1.04
glycine
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
1.04
glycine
-
wild type enzyme, at pH 8.5 and 60°C
1.35
glycine
-
mutant enzyme M49L, at pH 8.5 and 25°C
1.41
glycine
-
mutant enzyme N336A, at pH 7.5, temperature not specified in the publication
1.47
glycine
-
mutant enzyme M49T, at pH 8.5 and 25°C
1.5
glycine
-
mutant H244A, pH 8.5, 25°C
1.5
glycine
-
mutant enzyme H244A, at pH 8.5 and 25°C; mutant enzyme M261I, at pH 8.5 and 25°C
1.9
glycine
-
apparent value for mutant enzyme H244N, at 25°C and pH 8.5
1.9
glycine
-
mutant enzyme H244N, at pH 8.5 and 25°C
2.25
glycine
-
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
2.43
glycine
at pH 8.5 and 40°C
3.03
glycine
-
mutant enzyme F237Y, at 30°C, pH not specified in the publication
3.5
glycine
-
mutant enzyme M261R, at pH 8.5 and 25°C
3.8
glycine
-
pH 8.5, 25°C
5.4
glycine
-
pH 7.5, 25°C; pH 9.0, 25°C
5.6
glycine
-
pH 7.0, 25°C
8.33
glycine
-
pH and temperature not specified in the publication
9.2
glycine
-
pH 6.5, 25°C
10
glycine
-
mutant enzyme A54E, at pH 8.5 and 25°C
14.6
glycine
-
mutant enzyme G51Q, at pH 8.5 and 25°C
14.7
glycine
-
pH 9.5, 25°C
17.2
glycine
-
mutant enzyme Y246W, at pH 8.5 and 25°C
18
glycine
-
apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
18.8
glycine
-
mutant enzyme M49L/A54R/H244K, at pH 8.5 and 25°C
28
glycine
-
apparent value for mutant enzyme M261H, at 25°C and pH 8.5
28
glycine
-
mutant A54R, pH 8.5, 25°C
28
glycine
-
mutant enzyme A54R, at pH 8.5 and 25°C
35
glycine
-
mutant G51S/A54R, pH 8.5, 25°C
35.7
glycine
-
mutant enzyme G51H, at pH 8.5 and 25°C
38
glycine
-
mutant Y241H, pH 8.5, 25°C
39
glycine
-
wild type enzyme, at 30°C, pH not specified in the publication
40.1
glycine
-
mutant enzyme A54R/H244K, at pH 8.5 and 25°C
41.55
glycine
-
mutant enzyme G51R/G60S/T118A/K133R/I198V/V262I/I284L/L307S/E357G, at pH 8.5 and 60°C
41.64
glycine
-
mutant enzyme G51R/D60G/T118A/K133R/I284L, at pH 8.5 and 60°C
45.9
glycine
-
mutant enzyme A54R/H244K/M261R, at pH 8.5 and 25°C
53
glycine
-
mutant G51R, pH 8.5, 25°C
54.6
glycine
-
mutant enzyme G51R, at pH 8.5 and 60°C
58.5
glycine
-
mutant enzyme G51R/D60G, at pH 8.5 and 60°C
59
glycine
-
mutant G51R/A54R, pH 8.5, 25°C
80.43
glycine
-
mutant enzyme G51R/G60S/D121G/S122P/H164Y/M267T, at pH 8.5 and 60°C
92.5
glycine
-
mutant enzyme G51R/D60G/T118A/K133R, at pH 8.5 and 60°C
101.8
glycine
-
mutant enzyme BG51R/G60S/I198V/E357G, at pH 8.5 and 60°C
105
glycine
-
mutant G51S/A54R/H244A, pH 8.5, 25°C
105.6
glycine
-
mutant enzyme G51R/D60G/K133R/V262I, at pH 8.5 and 60°C
134.4
glycine
-
mutant enzyme BG51R/G60S/S210P/M267T, at pH 8.5 and 60°C
138.1
glycine
-
mutant enzyme G51R/G60S/K133R/S210P/R250G/V262I, at pH 8.5 and 60°C
0.29
glycine-ethyl-ester

-
M261Y mutant
0.52
glycine-ethyl-ester
-
in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C
0.52
glycine-ethyl-ester
-
pH 8.5, 37°C
0.6
glycine-ethyl-ester
-
mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
1.57
glycine-ethyl-ester
-
M261H mutant
1.78
glycine-ethyl-ester
-
M261 wild type
1.8
glycine-ethyl-ester
-
wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
0.5
glyphosate

-
mutant G51S/A54R/H244A, pH 8.5, 25°C
0.53
glyphosate
-
mutant enzyme G51R/G60S/T118A/K133R/I198V/V262I/I284L/L307S/E357G, at pH 8.5 and 60°C
0.57
glyphosate
-
mutant enzyme G51R/D60G/T118A/K133R/I284L, at pH 8.5 and 60°C
1
glyphosate
-
mutant G51R/A54R, pH 8.5, 25°C
1.3
glyphosate
-
mutant G51S/A54R, pH 8.5, 25°C
1.37
glyphosate
-
mutant enzyme G51R/G60S/D121G/S122P/H164Y/M267T, at pH 8.5 and 60°C
1.69
glyphosate
-
mutant enzyme G51R/G60S/K133R/S210P/R250G/V262I, at pH 8.5 and 60°C
2.17
glyphosate
-
mutant enzyme G51R/D60G/T118A/K133R, at pH 8.5 and 60°C
2.45
glyphosate
-
mutant enzyme G51R/D60G, at pH 8.5 and 60°C
2.77
glyphosate
-
mutant enzyme G51R/D60G/K133R/V262I, at pH 8.5 and 60°C
3.8
glyphosate
-
mutant enzyme BG51R/G60S/I198V/E357G, at pH 8.5 and 60°C
4.37
glyphosate
-
mutant enzyme BG51R/G60S/S210P/M267T, at pH 8.5 and 60°C
4.4
glyphosate
-
mutant A54R, pH 8.5, 25°C
6.5
glyphosate
-
mutant G51R, pH 8.5, 25°C
8.29
glyphosate
-
mutant enzyme G51R, at pH 8.5 and 60°C
10.44
glyphosate
-
mutant enzyme N336R, at pH 7.5, temperature not specified in the publication
18.88
glyphosate
-
mutant enzyme D60G, at pH 8.5 and 60°C
22.45
glyphosate
-
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
41
glyphosate
-
mutant Y241H, pH 8.5, 25°C
42.31
glyphosate
-
mutant enzyme N336H, at pH 7.5, temperature not specified in the publication
68.36
glyphosate
-
mutant enzyme N336A, at pH 7.5, temperature not specified in the publication
78
glyphosate
-
mutant H244A, pH 8.5, 25°C
84.79
glyphosate
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
84.79
glyphosate
-
wild type enzyme, at pH 8.5 and 60°C
87
glyphosate
-
wild-type, pH 8.5, 25°C
96.73
glyphosate
-
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
0.71
N-ethyl-glycine

-
M261Y mutant
2.07
N-ethyl-glycine
-
M261H mutant
2.8
N-ethyl-glycine
-
M261 wild type
0.22
N-ethylglycine

-
in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C
0.22
N-ethylglycine
-
pH 8.5, 37°C
0.5
N-ethylglycine
-
mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
2.8
N-ethylglycine
-
wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
7.68
N-ethylglycine
at pH 8.5 and 40°C
0.15
O2

-
pH 6.5, 25°C; pH 9.0, 25°C
0.38
O2
-
reaction with Gly
0.416
O2
-
mutant enzyme F237A, at 30°C, pH not specified in the publication
0.42
O2
-
reaction with sarcosine
0.44
O2
-
reaction with D-Pro
2.27
O2
-
mutant enzyme F237Y, at 30°C, pH not specified in the publication
2.6
O2
-
wild type enzyme, at 30°C, pH not specified in the publication
0.22
sarcosine

-
-
0.23
sarcosine
-
M261Y mutant
0.45
sarcosine
-
in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C
0.45
sarcosine
-
pH 8.5, 37°C
0.51
sarcosine
-
mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
0.57
sarcosine
-
M261 wild type
0.58
sarcosine
-
M261H mutant
0.6
sarcosine
-
wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C
0.7
sarcosine
-
apparent value for wild type enzyme, at 25°C and pH 8.5
0.7
sarcosine
-
wild type enzyme, at pH 8.5 and 25°C
1.4
sarcosine
-
apparent value for mutant enzyme H244F, at 25°C and pH 8.5
1.51
sarcosine
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
2.1
sarcosine
-
apparent value for mutant enzyme H244N, at 25°C and pH 8.5
2.8
sarcosine
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
4.86
sarcosine
at pH 8.5 and 40°C
11
sarcosine
-
apparent value for mutant enzyme M261H, at 25°C and pH 8.5; apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.14
cyclopropylglycine
-
-
0.4
D-Ala

-
-
0.33
D-alanine

-
kcat above 0.33 1/s, apparent value for mutant enzyme M261H, at 25°C and pH 8.5
0.47
D-alanine
-
apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
0.75
D-alanine
-
apparent value for mutant enzyme H244N, at 25°C and pH 8.5
0.81
D-alanine
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
0.92
D-alanine
-
apparent value for wild type enzyme, at 25°C and pH 8.5
1.08
D-alanine
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
1.5
D-alanine
-
apparent value for mutant enzyme H244F, at 25°C and pH 8.5
1.3
D-Pro

-
-
0.3
D-proline

-
apparent value for mutant enzyme H244N, at 25°C and pH 8.5
0.38
D-proline
-
apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
0.5
D-proline
-
apparent value for wild type enzyme, at 25°C and pH 8.5
0.62
D-proline
-
apparent value for mutant enzyme M261H, at 25°C and pH 8.5
1.23
D-proline
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
1.35
D-proline
-
apparent value for mutant enzyme H244F, at 25°C and pH 8.5
1.2
Gly

-
-
0.007
glycine

-
mutant enzyme G51R/D60G, at pH 8.5 and 60°C
0.019
glycine
-
mutant enzyme G51R, at pH 8.5 and 60°C
0.0225
glycine
-
mutant enzyme G51R/D60G/T118A/K133R, at pH 8.5 and 60°C
0.024
glycine
-
mutant enzyme N336R, at pH 7.5, temperature not specified in the publication
0.031
glycine
-
mutant enzyme G51R/D60G/K133R/V262I, at pH 8.5 and 60°C
0.038
glycine
-
mutant enzyme G51R/D60G/T118A/K133R/I284L, at pH 8.5 and 60°C
0.04
glycine
-
mutant enzyme M49T, at pH 8.5 and 25°C
0.076
glycine
-
mutant enzyme D60G, at pH 8.5 and 60°C
0.09
glycine
-
mutant enzyme BG51R/G60S/S210P/M267T, at pH 8.5 and 60°C; mutant enzyme G51R/G60S/T118A/K133R/I198V/V262I/I284L/L307S/E357G, at pH 8.5 and 60°C
0.095
glycine
-
mutant enzyme G51R/G60S/D121G/S122P/H164Y/M267T, at pH 8.5 and 60°C
0.14
glycine
-
wild type enzyme, at pH 8.5 and 60°C
0.169
glycine
-
mutant enzyme G51R/G60S/K133R/S210P/R250G/V262I, at pH 8.5 and 60°C
0.217
glycine
-
mutant enzyme BG51R/G60S/I198V/E357G, at pH 8.5 and 60°C
0.25
glycine
-
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
0.3
glycine
-
apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
0.35
glycine
-
mutant G51R, pH 8.5, 25°C
0.35
glycine
-
mutant enzyme A54E, at pH 8.5 and 25°C
0.36
glycine
-
mutant enzyme M49I, at pH 8.5 and 25°C
0.37
glycine
-
mutant enzyme N336H, at pH 7.5, temperature not specified in the publication
0.43
glycine
-
mutant enzyme M49L, at pH 8.5 and 25°C
0.52
glycine
-
mutant enzyme N336A, at pH 7.5, temperature not specified in the publication
0.55
glycine
-
apparent value for mutant enzyme M261H, at 25°C and pH 8.5
0.6
glycine
-
apparent value for wild type enzyme, at 25°C and pH 8.5
0.6
glycine
-
wild-type, pH 8.5, 25°C
0.6
glycine
-
mutant enzyme M49L/A54R/H244K, at pH 8.5 and 25°C; wild type enzyme, at pH 8.5 and 25°C
0.63
glycine
-
mutant H244A, pH 8.5, 25°C
0.63
glycine
-
mutant enzyme H244A, at pH 8.5 and 25°C
0.64
glycine
-
mutant enzyme M261I, at pH 8.5 and 25°C
0.67
glycine
-
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
0.7
glycine
-
mutant G51R/A54R, pH 8.5, 25°C
0.71
glycine
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
0.74
glycine
-
mutant enzyme G51Q, at pH 8.5 and 25°C
0.77
glycine
-
mutant enzyme G51H, at pH 8.5 and 25°C
0.78
glycine
-
apparent value for mutant enzyme H244F, at 25°C and pH 8.5
0.9
glycine
-
pH 6.5, 25°C
0.91
glycine
-
mutant G51S/A54R, pH 8.5, 25°C; mutant Y241H, pH 8.5, 25°C
1
glycine
-
mutant enzyme M261R, at pH 8.5 and 25°C
1.2
glycine
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
1.2
glycine
-
mutant A54R, pH 8.5, 25°C
1.2
glycine
-
mutant enzyme A54R, at pH 8.5 and 25°C; mutant enzyme H244K/M261R, at pH 8.5 and 25°C
1.21
glycine
-
mutant enzyme H244Q, at pH 8.5 and 25°C; mutant enzyme Y246W, at pH 8.5 and 25°C
1.3
glycine
-
apparent value for mutant enzyme H244N, at 25°C and pH 8.5
1.3
glycine
-
mutant enzyme H244N, at pH 8.5 and 25°C
1.35
glycine
-
mutant enzyme H244K, at pH 8.5 and 25°C
1.49
glycine
-
mutant enzyme H244R, at pH 8.5 and 25°C
1.5
glycine
-
mutant G51S/A54R/H244A, pH 8.5, 25°C
1.61
glycine
-
mutant enzyme A54R/H244K/M261R, at pH 8.5 and 25°C
2.4
glycine
-
pH 7.0, 25°C
3.2
glycine
-
mutant enzyme A54R/H244K, at pH 8.5 and 25°C
3.6
glycine
-
pH 8.0, 25°C
4.1
glycine
-
pH 9.0, 25°C
39
glycine
-
wild type enzyme, at 30°C, pH not specified in the publication
0.021
glyphosate

-
mutant enzyme N336R, at pH 7.5, temperature not specified in the publication
0.046
glyphosate
-
mutant enzyme G51R/D60G, at pH 8.5 and 60°C
0.049
glyphosate
-
mutant enzyme G51R, at pH 8.5 and 60°C
0.069
glyphosate
-
mutant enzyme G51R/D60G/T118A/K133R, at pH 8.5 and 60°C
0.077
glyphosate
-
mutant enzyme G51R/D60G/T118A/K133R/I284L, at pH 8.5 and 60°C
0.095
glyphosate
-
wild type enzyme, at pH 8.5 and 60°C
0.12
glyphosate
-
mutant enzyme D60G, at pH 8.5 and 60°C
0.121
glyphosate
-
mutant enzyme BG51R/G60S/S210P/M267T, at pH 8.5 and 60°C
0.19
glyphosate
-
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
0.195
glyphosate
-
mutant enzyme G51R/G60S/T118A/K133R/I198V/V262I/I284L/L307S/E357G, at pH 8.5 and 60°C
0.2165
glyphosate
-
mutant enzyme G51R/G60S/D121G/S122P/H164Y/M267T, at pH 8.5 and 60°C
0.22
glyphosate
-
mutant enzyme G51R/G60S/K133R/S210P/R250G/V262I, at pH 8.5 and 60°C
0.23
glyphosate
-
mutant enzyme N336H, at pH 7.5, temperature not specified in the publication
0.513
glyphosate
-
mutant enzyme BG51R/G60S/I198V/E357G, at pH 8.5 and 60°C
0.62
glyphosate
-
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
0.67
glyphosate
-
mutant enzyme N336A, at pH 7.5, temperature not specified in the publication
0.7
glyphosate
-
mutant G51R/A54R, pH 8.5, 25°C
0.77
glyphosate
-
mutant H244A, pH 8.5, 25°C
0.87
glyphosate
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
0.91
glyphosate
-
wild-type, pH 8.5, 25°C
1.05
glyphosate
-
mutant G51S/A54R/H244A, pH 8.5, 25°C; mutant G51S/A54R, pH 8.5, 25°C
1.3
glyphosate
-
mutant Y241H, pH 8.5, 25°C
1.5
glyphosate
-
mutant A54R, pH 8.5, 25°C
1.8
glyphosate
-
mutant G51R, pH 8.5, 25°C
64
glyphosate
-
mutant enzyme G51R/D60G/K133R/V262I, at pH 8.5 and 60°C
0.6
O2

-
mutant enzyme F237A, at 30°C, pH not specified in the publication
15
O2
-
mutant enzyme F237Y, at 30°C, pH not specified in the publication
93
O2
-
wild type enzyme, at 30°C, pH not specified in the publication
0.47
sarcosine

-
apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
0.6
sarcosine
-
apparent value for wild type enzyme, at 25°C and pH 8.5
0.6
sarcosine
-
wild type enzyme, at pH 8.5 and 25°C
0.73
sarcosine
-
apparent value for mutant enzyme M261H, at 25°C and pH 8.5
0.98
sarcosine
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
1.08
sarcosine
-
apparent value for mutant enzyme H244F, at 25°C and pH 8.5
1.12
sarcosine
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
1.33
sarcosine
-
apparent value for mutant enzyme H244N, at 25°C and pH 8.5
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0.023
D-alanine
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
0.02
glycine

-
mutant enzyme G51H, at pH 8.5 and 25°C
0.03
glycine
-
mutant enzyme M49L/A54R/H244K, at pH 8.5 and 25°C; mutant enzyme M49T, at pH 8.5 and 25°C
0.04
glycine
-
mutant enzyme A54E, at pH 8.5 and 25°C; mutant enzyme A54R, at pH 8.5 and 25°C; mutant enzyme A54R/H244K/M261R, at pH 8.5 and 25°C
0.045
glycine
-
mutant enzyme N336R, at pH 7.5, temperature not specified in the publication
0.05
glycine
-
mutant enzyme G51Q, at pH 8.5 and 25°C
0.07
glycine
-
mutant enzyme Y246W, at pH 8.5 and 25°C
0.11
glycine
-
mutant enzyme A54R/H244K, at pH 8.5 and 25°C
0.3
glycine
-
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
0.3
glycine
-
mutant enzyme M261R, at pH 8.5 and 25°C
0.32
glycine
-
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
0.32
glycine
-
mutant enzyme M49L, at pH 8.5 and 25°C
0.37
glycine
-
mutant enzyme N336A, at pH 7.5, temperature not specified in the publication
0.39
glycine
-
mutant enzyme N336H, at pH 7.5, temperature not specified in the publication
0.42
glycine
-
mutant enzyme H244A, at pH 8.5 and 25°C
0.43
glycine
-
mutant enzyme M261I, at pH 8.5 and 25°C
0.68
glycine
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
0.68
glycine
-
mutant enzyme H244N, at pH 8.5 and 25°C
0.86
glycine
-
wild type enzyme, at pH 8.5 and 25°C
1.17
glycine
-
mutant enzyme M49I, at pH 8.5 and 25°C
1.34
glycine
-
mutant enzyme H244Q, at pH 8.5 and 25°C
4
glycine
-
mutant enzyme H244K/M261R, at pH 8.5 and 25°C
6.22
glycine
-
mutant enzyme H244R, at pH 8.5 and 25°C
9.65
glycine
-
mutant enzyme H244K, at pH 8.5 and 25°C
0.002
glyphosate

-
mutant enzyme N336R, at pH 7.5, temperature not specified in the publication
0.0054
glyphosate
-
mutant enzyme N336H, at pH 7.5, temperature not specified in the publication
0.0064
glyphosate
-
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
0.0084
glyphosate
-
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
0.0098
glyphosate
-
mutant enzyme N336A, at pH 7.5, temperature not specified in the publication
0.01
glyphosate
-
wild type enzyme, at pH 7.5, temperature not specified in the publication
1
O2

-
mutant enzyme F237A, at 30°C, pH not specified in the publication
6.6
O2
-
mutant enzyme F237Y, at 30°C, pH not specified in the publication
36
O2
-
wild type enzyme, at 30°C, pH not specified in the publication
0.65
sarcosine

-
wild type enzyme, at pH 7.5, temperature not specified in the publication
0.86
sarcosine
-
wild type enzyme, at pH 8.5 and 25°C
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BG51R/G60S/I198V/E357G
-
the mutant shows no activity with glycine and high activity with glyphosate
BG51R/G60S/S210P/M267T
-
the mutant shows no activity with glycine and activity with glyphosate
D60G
-
the mutant shows activity with glycine and very low activity with glyphosate
G51R
-
the mutant shows no activity with glycine and very low activity with glyphosate
G51R/D60G
-
the mutant shows no activity with glycine and activity with glyphosate
G51R/D60G/K133R/V262I
-
the mutant shows no activity with glycine and activity with glyphosate
G51R/D60G/T118A/K133R
-
the mutant shows no activity with glycine and activity with glyphosate
G51R/D60G/T118A/K133R/I284L
-
the mutant shows no activity with glycine and very high activity with glyphosate
G51R/G60S/D121G/S122P/H164Y/M267T
-
the mutant shows no activity with glycine and high activity with glyphosate
G51R/G60S/K133R/S210P/R250G/V262I
-
the mutant shows no activity with glycine and high activity with glyphosate
G51R/G60S/T118A/K133R/I198V/V262I/I284L/L307S/E357G
-
the mutant shows no activity with glycine and high activity with glyphosate
N336A
-
the mutant shows increased substrate affinity compared to the wild type enzyme
N336G
-
the mutant shows increased substrate affinity compared to the wild type enzyme
N336H
-
the mutant shows increased substrate affinity compared to the wild type enzyme
N336K
-
the mutant shows increased substrate affinity compared to the wild type enzyme
N336R
-
the mutant shows increased substrate affinity compared to the wild type enzyme
N336A
-
the mutant shows increased substrate affinity compared to the wild type enzyme
-
N336G
-
the mutant shows increased substrate affinity compared to the wild type enzyme
-
N336H
-
the mutant shows increased substrate affinity compared to the wild type enzyme
-
N336K
-
the mutant shows increased substrate affinity compared to the wild type enzyme
-
N336R
-
the mutant shows increased substrate affinity compared to the wild type enzyme
-
A45H/G300C
-
monomeric in solution. Upon incubation of apoprotein with FAD, neither FAD binding nor enzymatic activity is observed. Slow elimination of urea from partially unfolded mutant in presence of a large excess of FAD and 30% glyccerol does not produce the holoenzyme
A54E
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
A54R/H244K
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
A54R/H244K/M261R
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
agriculture
-
expression of an evolved engineered variant of glycine oxidase leads to glyphosate resistance in alfalfa
G300C
-
upon incubation of apoprotein with FAD, neither FAD binding nor enzymatic activity is observed. Slow elimination of urea from partially unfolded mutant in presence of a large excess of FAD and 30% glycerol does not produce the holoenzyme
G51H
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
G51Q
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
G51R
-
4000fold increase in the specificity constant for substrate glyphosate
G51R/A54R
-
5800fold increase in the specificity constant for substrate glyphosate
G51S/A54R
-
3100fold increase in the specificity constant for substrate glyphosate
G51S/A54R/H244A
-
210fold increase in catalytic activity and 15000fold increase in the specificity constant for substrate glyphosate. The alpha2-alpha3-loop assumes a different conformation, residue R54 may be the key residue in stabilizing glyphosate binding
H244F
-
shows increased kcat value for glycine compared to the wild type enzyme, the mutation does not affect the expression of glycine oxidase and the physicochemical properties of bound FAD
H244K
-
the mutant shows increased catalytic efficiency with glycine compared to the wild type enzyme
H244K/M261R
-
the variant shows a 5.4fold increase in maximal activity on glycine compared to the wild type enzyme
H244R
-
the mutant shows increased catalytic efficiency with glycine compared to the wild type enzyme
I15V
-
the mutant exhibits a 7fold higher specific activity compared to the wild type enzyme
M261I
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
M261R
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
M49I
-
the mutant shows increased catalytic efficiency with glycine compared to the wild type enzyme
M49L
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
M49L/A54R/H244K
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
M49T
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
Y241H
-
100fold increase in the specificity constant for substrate glyphosate
Y246W
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
A54R
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
-
agriculture
-
expression of an evolved engineered variant of glycine oxidase leads to glyphosate resistance in alfalfa
-
H244A
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
-
H244N
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
-
H244Q
-
the mutant shows increased catalytic efficiency with glycine compared to the wild type enzyme
-
M49L
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
-
F237A
-
the mutant shows stronlgy reduced catalytic efficiency compared to the wild type enzyme
F237Y
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A54R

-
20fold increase in Km for glyphosate
A54R
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
H244A

-
2fold increase in expression yield
H244A
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
H244N

-
shows increased kcat value for glycine compared to the wild type enzyme, the mutation does not affect the expression of glycine oxidase and the physicochemical properties of bound FAD
H244N
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
H244Q

-
shows increased kcat value compared to the wild type enzyme, the mutation does not affect the expression of glycine oxidase and the physicochemical properties of bound FAD
H244Q
-
the mutant shows increased catalytic efficiency with glycine compared to the wild type enzyme
M261H

-
decreased in Km compared with the wild type
M261H
-
shows decreased kcat value for glycine compared to the wild type enzyme, the mutation does not affect the expression of glycine oxidase and the physicochemical properties of bound FAD
M261Y

-
decreased in Km compared with the wild type
M261Y
-
shows decreased kcat value for glycine compared to the wild type enzyme, the mutation does not affect the expression of glycine oxidase and the physicochemical properties of bound FAD
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Nishiya, Y.; Imanaka, T.
Purification and characterization of a novel glycine oxidase from Bacillus subtilis
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438
263-266
1998
Bacillus subtilis
brenda
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Kinetic mechanisms of glycine oxidase from Bacillus subtilis
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270
1474-1482
2003
Bacillus subtilis
brenda
Settembre, E.C.; Dorrestein, P.C.; Park, J.H.; Augustine, A.M.; Begley, T.P.; Ealick, S.E.
Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis
Biochemistry
42
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2003
Bacillus subtilis, Bacillus subtilis (O31616)
brenda
Job, V.; Molla, G.; Pilone, M.S.; Pollegioni, L.
Overexpression of a recombinant wild-type anf His-tagged Bacillus subtilis glycine oxidase in Escherichia coli
Eur. J. Biochem.
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2002
Bacillus subtilis
brenda
Mörtl, M.; Diedrichs, K.; Welte, W.; Molla, G.; Motteran, L.; Andriolo, G.; Pilone, M.S.; Pollegioni, L.
Structure-function correlation in glycine oxidase from Bacillus subtilis
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279
29718-29727
2004
Bacillus subtilis, Bacillus subtilis (O31616)
brenda
Martinez-Martinez, I.; Navarro-Fernandez, J.; Lozada-Ramirez, J.D.; Garcia-Carmona, F.; Sanchez-Ferrer, A.
Maximization of production of his-tagged glycine oxidase and its M261 mutant proteins
Biotechnol. Prog.
22
647-652
2006
Bacillus subtilis
brenda
Boselli, A.; Rosini, E.; Marcone, G.L.; Sacchi, S.; Motteran, L.; Pilone, M.S.; Pollegioni, L.; Molla, G.
Glycine oxidase from Bacillus subtilis: role of histidine 244 and methionine 261
Biochimie
89
1372-1380
2007
Bacillus subtilis
brenda
Martinez-Martinez, I.; Kaiser, C.; Rohde, A.; Ellert, A.; Garcia-Carmona, F.; Sanchez-Ferrer, A.; Luttmann, R.
High-level production of Bacillus subtilis glycine oxidase by fed-batch cultivation of recombinant Escherichia coli Rosetta (DE3)
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23
645-651
2007
Bacillus subtilis
brenda
Martinez-Martinez, I.; Navarro-Fernandez, J.; Garcia-Carmona, F.; Sanchez-Ferrer, A.
Implication of a mutation in the flavin binding site on the specific activity and substrate specificity of glycine oxidase from Bacillus subtilis produced by directed evolution
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133
1-8
2008
Bacillus subtilis, Bacillus subtilis (O31616)
brenda
Martinez-Martinez, I.; Navarro-Fernandez, J.; Garcia-Carmona, F.; Takami, H.; Sanchez-Ferrer, A.
Characterization and structural modeling of a novel thermostable glycine oxidase from Geobacillus kaustophilus HTA426
Proteins
70
1429-1441
2008
Geobacillus kaustophilus
brenda
Caldinelli, L.; Pedotti, M.; Motteran, L.; Molla, G.; Pollegioni, L.
FAD binding in glycine oxidase from Bacillus subtilis
Biochimie
91
1499-1508
2009
Bacillus subtilis, Bacillus subtilis (O31616)
brenda
Pedotti, M.; Ghisla, S.; Motteran, L.; Molla, G.; Pollegioni, L.
Catalytic and redox properties of glycine oxidase from Bacillus subtilis
Biochimie
91
604-612
2009
Bacillus subtilis, Bacillus subtilis (O31616)
brenda
Pedotti, M.; Rosini, E.; Molla, G.; Moschetti, T.; Savino, C.; Vallone, B.; Pollegioni, L.
Glyphosate resistance by engineering the flavoenzyme glycine oxidase
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284
36415-36423
2009
Bacillus subtilis, Bacillus subtilis (O31616)
brenda
Martinez-Martinez, I.; Navarro-Fernandez, J.; Garcia-Carmona, F.; Takami, H.; Sanchez-Ferrer, A.
Characterization and structural modeling of a novel thermostable glycine oxidase from Geobacillus kaustophilus HTA426
Proteins Struct. Funct. Bioinform.
70
1429-1441
2008
Geobacillus kaustophilus HTA426
brenda
Jamil, F.; Afza Gardner, Q.T.; Bashir, Q.; Rashid, N.; Akhtar, M.
Mechanistic and stereochemical studies of glycine oxidase from Bacillus subtilis strain R5
Biochemistry
49
7377-7383
2010
Bacillus subtilis, Bacillus subtilis R5
brenda
Jamil, F.; Rashid, N.; Gardner, Q.; Akhtar, M.
Gene cloning and characterization of glycine oxidase from newly isolated Bacillus subtilis strain R5
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66
1-7
2011
Bacillus subtilis (D7UTZ8), Bacillus subtilis R5 (D7UTZ8)
-
brenda
Campillo-Brocal, J.C.; Lucas-Elio, P.; Sanchez-Amat, A.
Identification in Marinomonas mediterranea of a novel quinoprotein with glycine oxidase activity
Microbiologyopen
2
684-694
2013
Marinomonas mediterranea, Marinomonas mediterranea MMB-1
brenda
Weiss, M.S.; Pavlidis, I.V.; Vickers, C.; Hoehne, M.; Bornscheuer, U.T.
Glycine oxidase based high-throughput solid-phase assay for substrate profiling and directed evolution of (R)- and (S)-selective amine transaminases
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11847-11853
2014
Geobacillus kaustophilus (Q5L2C2)
brenda
Wu, G.; Zhan, T.; Guo, Y.; Kumar, A.; Liu, Z.
Asn336 is involved in the substrate affinity of glycine oxidase from Bacillus cereus
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22
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-
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Zhang, K.; Guo, Y.; Yao, P.; Lin, Y.; Kumar, A.; Liu, Z.; Wu, G.; Zhang, L.
Characterization and directed evolution of BliGO, a novel glycine oxidase from Bacillus licheniformis
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85
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Bacillus licheniformis, Bacillus licheniformis (S5FMM4), Bacillus licheniformis J33-8 (S5FMM4)
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Rosini, E.; Piubelli, L.; Molla, G.; Frattini, L.; Valentino, M.; Varriale, A.; DAuria, S.; Pollegioni, L.
Novel biosensors based on optimized glycine oxidase
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Bacillus subtilis 168 (O31616), Bacillus subtilis, Bacillus subtilis (O31616)
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Yao, P.; Lin, Y.; Wu, G.; Lu, Y.; Zhan, T.; Kumar, A.; Zhang, L.; Liu, Z.
Improvement of glycine oxidase by DNA shuffling, and site-saturation mutagenesis of F247 residue
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79
965-970
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brenda
Sehanobish, E.; Williamson, H.R.; Davidson, V.L.
Roles of conserved residues of the glycine oxidase GoxA in controlling activity, cooperativity, subunit composition, and cysteine tryptophylquinone biosynthesis
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291
23199-23207
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Marinomonas mediterranea
brenda
Nicolia, A.; Ferradini, N.; Molla, G.; Biagetti, E.; Pollegioni, L.; Veronesi, F.; Rosellini, D.
Expression of an evolved engineered variant of a bacterial glycine oxidase leads to glyphosate resistance in alfalfa
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2014
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Purification and properties of glycine oxidase from Pseudomonas putida KT2440
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Pseudomonas putida, Pseudomonas putida (Q88Q83), Pseudomonas putida KT 2240 (Q88Q83)
brenda
Zhan, T.; Zhang, K.; Chen, Y.; Lin, Y.; Wu, G.; Zhang, L.; Yao, P.; Shao, Z.; Liu, Z.
Improving glyphosate oxidation activity of glycine oxidase from Bacillus cereus by directed evolution
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8
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Bacillus cereus, Bacillus cereus (L7T8Y9)
brenda