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Information on EC 1.4.3.19 - glycine oxidase
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1.4.3.19 glycine oxidaseIUBMB Comments
A flavoenzyme containing non-covalently bound FAD. The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-alpha-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine. It differs from EC 1.4.3.3, D-amino-acid oxidase, due to its activity on sarcosine and D-pipecolate. The intermediate 2-iminoacetate is used directly by EC 2.8.1.10, thiazole synthase.
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Word Map
- 1.4.3.19
-
d-amino
- sarcosine
- flavoproteins
- fad
- flavin
- glyphosate
-
tryptophylquinone
-
flavoenzyme
-
deamination
- d-proline
-
homotetrameric
- glyoxylate
- luteoviolacea
-
protein-derived
-
pseudoalteromonas
- d-alanine
-
fad-dependent
-
fad-binding
-
thios
-
quinoprotein
-
site-saturation
- 5-enolpyruvylshikimate-3-phosphate
-
rosetta
-
fad-containing
-
half-reaction
- ttq
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
glycin oxidase, glycine:oxygen oxidoreductase (deaminating), GO, GOX, GoxA, GOXK, GoxR, LodA, ThiO, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycine:oxygen oxidoreductase (deaminating)
GO
-
-
-
-
GOX
GoxA
GoxR
LodA
ThiO
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-iminoacetate + H2O = glyoxylate + NH3
(1b)
-
-
-
glycine + O2 = 2-iminoacetate + H2O2
(1a)
-
-
-
glycine + H2O + O2 = glyoxylate + NH3 + H2O2
ternary complex sequential mechanism
-
glycine + H2O + O2 = glyoxylate + NH3 + H2O2
overall reaction
-
-
-
glycine + H2O + O2 = glyoxylate + NH3 + H2O2
reaction mechanism involving an FADH2-imino acid complex, overview
-
glycine + H2O + O2 = glyoxylate + NH3 + H2O2
reaction mechanism involving an FADH2-imino acid complex, overview
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
glycine:oxygen oxidoreductase (deaminating)
A flavoenzyme containing non-covalently bound FAD. The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-alpha-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine. It differs from EC 1.4.3.3, D-amino-acid oxidase, due to its activity on sarcosine and D-pipecolate. The intermediate 2-iminoacetate is used directly by EC 2.8.1.10, thiazole synthase.
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CAS REGISTRY NUMBER
COMMENTARY
39307-16-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-aminobutanoate + H2O + O2
? + H2O2
30% 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-Pro + H2O + O2
? + H2O2
-
about 120% of the activity with sarcosine
-
-
?
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
-
-
?
glyphosate + H2O + O2
? + H2O2
110% of the activity with sarcosine
-
-
?
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
-
-
?
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
pyruvate + NH3 + H2O2
-
7.4% of the activity with sarcosine
-
-
?
D-Ala + H2O + O2
pyruvate + NH3 + H2O2
-
about 115% of the activity with sarcosine
-
-
?
D-alanine + H2O + O2
?
10% activity compared to glycine
-
-
?
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-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-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
-
-
-
-
?
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
-
15.1% of the activity with sarcosine
-
-
?
D-Pro + H2O + O2
? + NH3 + H2O2
110% of the activity with sarcosine
-
-
?
D-proline + H2O + O2
?
-
0.3% 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
-
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
85% of the activity with sarcosine
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
100% activity
-
-
?
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
-
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
? + H2O2
90% of the activity with sarcosine
-
-
?
glyphosate + H2O + O2
?
the wild type enzyme shows very low activity with glyphosate
-
-
?
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
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
-
-
?
sarcosine + H2O + O2
?
-
0.1% activity compared to glycine
-
-
?
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
?
-
-
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 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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclopropylglycine + H2O + O2
?
enzyme is required for the biosynthesis of the thiazole moiety of thiamine diphosphate
-
-
?
glycine ethyl ester + H2O + O2
?
-
30.7% activity compared to glycine
-
-
?
N-ethylglycine + H2O + O2
?
-
0.3% activity compared to glycine
-
-
?
D-4-hydroxyphenylglycine + H2O + O2
?
-
0.6% activity compared to glycine
-
-
?
D-4-hydroxyphenylglycine + H2O + O2
?
-
0.6% activity compared to glycine
-
-
?
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-proline + H2O + O2
?
-
0.3% activity compared to glycine
-
-
?
glycine + H2O + O2
glyoxylate + NH3 + H2O2
-
100% activity
-
-
?
sarcosine + H2O + O2
?
-
0.1% activity compared to glycine
-
-
?
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
?
-
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
tight binding of coenzyme to the protein moiety, addition of exogenous FAD or FMN to the assay mixture does not increase enzyme activity
FAD
the isolated apoprotein species is present in solution as a monomer which rapidly recovers its tertiary structure and converts into the tetrameric holoenzyme following incubation with free FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no enhancement of enzyme activity in the presence of metal cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
there is a sharp decrease in activity when 1 mM Co2+ is added to the reaction assay
diethylether
73% residual activity after 30 min incubation at 30% (v/v)
ethyl acetate
19% residual activity after 30 min incubation at 30% (v/v)
N,N-Dimethyl formamide
17% residual activity after 30 min incubation at 30% (v/v)
Zn2+
there is a sharp decrease in activity when 1 mM Zn2+ is added to the reaction assay
additional information
not inhibited by glycine, sarcosine, and glycine ethyl ester
-
additional information
-
not inhibited by glycine, sarcosine, and glycine ethyl ester
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
34.65
D-alanine
wild type enzyme, at pH 7.5, temperature not specified in the publication
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
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
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
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
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
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
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
0.4
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
0.6
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
0.79
glycine
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
0.826
glycine
-
mutant enzyme F237A, at 30°C, pH not specified in the publication
0.95
glycine
mutant enzyme N336H, at pH 7.5, temperature not specified in the publication
1.04
glycine
wild type enzyme, at pH 7.5, temperature not specified in the publication
1.41
glycine
mutant enzyme N336A, at pH 7.5, temperature not specified in the publication
2.25
glycine
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
3.03
glycine
-
mutant enzyme F237Y, at 30°C, pH not specified in the publication
39
glycine
-
wild type enzyme, at 30°C, pH not specified in the publication
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
80.43
glycine
mutant enzyme G51R/G60S/D121G/S122P/H164Y/M267T, at pH 8.5 and 60°C
101.8
glycine
mutant enzyme BG51R/G60S/I198V/E357G, 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
0.52
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
0.6
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
1.8
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
0.53
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
1.37
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
2.77
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
10.44
glyphosate
mutant enzyme N336R, at pH 7.5, temperature not specified in the publication
22.45
glyphosate
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
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
84.79
glyphosate
wild type enzyme, at pH 7.5, temperature not specified in the publication
96.73
glyphosate
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
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
0.5
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
0.416
O2
-
mutant enzyme F237A, at 30°C, pH not specified in the publication
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
0.45
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
0.51
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
0.6
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
1.51
sarcosine
wild type enzyme, at pH 7.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1.08
D-alanine
-
apparent value for mutant enzyme H244Q, at 25°C and pH 8.5
0.38
D-proline
-
apparent value for mutant enzyme M261Y, at 25°C and pH 8.5
0.62
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
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
0.038
glycine
mutant enzyme G51R/D60G/T118A/K133R/I284L, at pH 8.5 and 60°C
0.09
glycine
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
0.169
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
0.37
glycine
mutant enzyme N336H, at pH 7.5, temperature not specified in the publication
0.52
glycine
mutant enzyme N336A, at pH 7.5, temperature not specified in the publication
0.67
glycine
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
0.71
glycine
wild type enzyme, at pH 7.5, temperature not specified in the publication
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
0.069
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
0.121
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
0.87
glyphosate
wild type enzyme, at pH 7.5, temperature not specified in the publication
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
0.73
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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
D-alanine
wild type enzyme, at pH 7.5, temperature not specified in the publication
0.045
glycine
mutant enzyme N336R, at pH 7.5, temperature not specified in the publication
0.3
glycine
mutant enzyme N336G, at pH 7.5, temperature not specified in the publication
0.32
glycine
mutant enzyme N336K, at pH 7.5, temperature not specified in the publication
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
0.68
glycine
wild type enzyme, at pH 7.5, temperature not specified in the publication
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1000
after 68.6fold purification, when D-alanine is used as a substrate, at pH 8.0 and 37°C
11.85
14
cell free extract, when glycine is used as a substrate, at pH 8.0 and 37°C
960
after 68.6fold purification, when glycine is used as a substrate, at pH 8.0 and 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
about 75% activity at pH 7.0, more than 50% activity is retained between pH 7.5 and 8.5, about 60% activity at pH 9.0. The enzyme activity decreases sharply below pH 7.0 and above pH 9.0. There is a negligible amount of activity at pH below 5.0 and above 10.0
8 - 11
-
pH 8.0: about 55% of maximal activity, pH 11.0: about 55% of maximal activity, reaction with sarcosine
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
60
additional information
-
increase in activity with no evidence for any plateau or decrease up to 60°C, reaction with sarcosine
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 60
-
increase in activity with no evidence for any plateau or decrease up to 60°C, reaction with sarcosine
40 - 55
the enzyme exhibits almost 80% of its activity at temperatures 40 and 55°C. The activity sharply decreases above 55°C
60
-
activation during the first 15 min, with slow decrease thereafter
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (3963 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
172000
40000
40762
-
x * 40763, recombinant enzyme, mass spectrometry, x * 40762, sequence calculation
40763
-
x * 40763, recombinant enzyme, mass spectrometry, x * 40762, sequence calculation
42000
43000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
monomer
tetramer
additional information
?
-
x * 40763, recombinant enzyme, mass spectrometry, x * 40762, sequence calculation
?
-
x * 40763, recombinant enzyme, mass spectrometry, x * 40762, sequence calculation
-
additional information
the isolated apoprotein of glycine oxidase shows high protein fluorescence, high exposure of hydrophobic surfaces, and low temperature stability as compared to the holoenzyme
additional information
-
the isolated apoprotein of glycine oxidase shows high protein fluorescence, high exposure of hydrophobic surfaces, and low temperature stability as compared to the holoenzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
H244A
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
H244N
H244Q
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
M261H
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
M261Y
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
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
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
-
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
-
a great decrease in stability is only produced at pH values below pH 4.0, shows good stability between pH 6.0 and 9.0
689934
6 - 11
the enzyme remains stable between pH 6.0 and 11.0 after 6 h incubation
743639
6.5 - 10
the tetrameric oligomeric state of the holoenzyme is not affected within this range
696494
6.5 - 9.5
8 - 10
the enzyme is most stable in the pH range from 8.0 to 10.0 upon incubation at 25°C for 1 h
743136
6.5 - 9.5
the tetrameric state of the enzyme is not affected by pH in the pH range 6.5-9.5
656226
6.5 - 9.5
the incubation of both enzymes for 1 h shows highest stability between pH 6.5 and pH 9.5, the mutant enzyme is also stable at pH below pH 6.5 retaining about 70% of its initial activity, this stability at a lower pH is in contrast to the sharp decrease in pH-stability showed by wild type GOX which retains only about 37% of the initial activity
687878
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 50
the enzyme remains stable between 0 and 50°C after 6 h incubation
34.7
melting temperature, mutant G51R/A54R, determined by following protein and flavin fluorescence
41.3
melting temperature, mutant G51R, determined by following protein and flavin fluorescence
44.8
melting temperature, mutant A54R, determined by following protein and flavin fluorescence
45
45.3
melting temperature, mutant G51S/A54R, determined by following protein and flavin fluorescence
45.7
melting temperature, mutant G51S/A54R/H244A, determined by following protein and flavin fluorescence
56.9
60 - 80
at 60°C, the I15V mutant shows a similar profile than the wild type enzyme but with lower residual activity after 20 min, at 65°C the mutant goes through activation (160%) during the first 15 min, the activity then falls with a time-dependent trend and reaches a half-life value similar to the wild type enzyme, at higher temperatures (70-80°C) the activity decreases rapidly in both cases, but with half-life value higher for I15V mutant than for wild type enzyme
95
-
heat treatment of the protein at 95°C for 5 min results in the release of the FAD cofactor
56.9
melting temperature, wild-type, determined by following protein and flavin fluorescence
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
tetrameric enzyme is strongly resistant to proteolysis, only the N-terminus is sensitive to proteases
thiocyanate, up to 1 mM, decreases stability of the tetrameric enzyme in solution
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 75 mM sodium diphosphate buffer pH 8.5 containing 10% glycerol, several months, no loss of activity
-80°C, 75 mM sodium diphosphate, pH 8.5, 10% glycerol, stable for months
-
-80°C, pH 7.5, both glycine oxidase and His-tagged glycine oxidase are stable for months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
100 kDa ultrafiltration, HisTrap FF Ni2+-chelating affinity column chromatography, and phenyl-Sepharose FF hydrophobic column chromatography
ammonium sulfate precipitation, Resource Q column chromatography and Resource ISO column chromatography
His-Trap column chromatography, and Superdex 200 gel filtration
HiTrap FF chelating affinity column chromatography and phenyl-Sepharose FF hydrophobic column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the glycine oxidase gene from Bacillus subtilis ATCC 6633 into the Rosetta Escherichia coli strain which contains the pRARE plasmid, inserting of the gene into the pET28a expression vector
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells
expressed in Escherichia coli Rosetta (DE3) cells Rosetta under the strong inducible T7 promotor of the pET28a vector
-
expression in Escherichia coli
production of a recombinant plasmid, pT7-GO by insertion of the DNA encoding for glycine oxidase into the multiple cloning site of the expression vector pT7.7. The pT7-glycine oxidase encodes a fully active fusion protein with six additional residues at the N-terminus of glycine oxidase. In BL21(DE3)pLysS Escherichia coli cells, and under optimal isopropyl thio-beta-D-galactoside induction conditions, soluble and active chimeric glycine oxidase is expressed up to 1.14 U per mg of cell. An N-terminally His-tagged glycine oxidase is also successfully expressed in Escherichia coli as a soluble protein and a fully active holoenzyme
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the isolated apoprotein species is present in solution as a monomer which rapidly recovers its tertiary structure and converts into the tetrameric holoenzyme following incubation with free FAD. The reconstitution process follows a particular two-stage process, the spectral properties of the reconstituted holoenzyme are virtually indistinguishable from those observed with native glycine oxidase, while the activity is only recovered to about 50%. The urea-induced unfolding process of glycine oxidase can be considered as a two-step process. Only a single transition at 4.5 M urea concentration is observed for the apoprotein form. The chemical denaturation of glycine oxidase holoenzyme is partially reversible
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nishiya, Y.; Imanaka, T.
Purification and characterization of a novel glycine oxidase from Bacillus subtilis
FEBS Lett.
438
263-266
1998
Bacillus subtilis
brenda
Molla, G.; Motteran, L.; Job, V.; Pilone, M.S.; Pollegioni, L.
Kinetic mechanisms of glycine oxidase from Bacillus subtilis
Eur. J. Biochem.
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
2971-2981
2003
Bacillus subtilis (O31616), Bacillus subtilis
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.
269
1456-1463
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
J. Biol. Chem.
279
29718-29727
2004
Bacillus subtilis (O31616), Bacillus subtilis
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)
Biotechnol. Prog.
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
J. Biotechnol.
133
1-8
2008
Bacillus subtilis (O31616), Bacillus subtilis
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 (O31616), Bacillus subtilis
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 (O31616), Bacillus subtilis
brenda
Pedotti, M.; Rosini, E.; Molla, G.; Moschetti, T.; Savino, C.; Vallone, B.; Pollegioni, L.
Glyphosate resistance by engineering the flavoenzyme glycine oxidase
J. Biol. Chem.
284
36415-36423
2009
Bacillus subtilis (O31616), Bacillus subtilis
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
Biologia
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
Anal. Chem.
86
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
Electron. J. Biotechnol.
22
26-30
2016
Bacillus cereus (L7T8Y9), Bacillus cereus HYC-7 (L7T8Y9)
-
brenda
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
Enzyme Microb. Technol.
85
12-18
2016
Bacillus licheniformis (S5FMM4), Bacillus licheniformis, Bacillus licheniformis J33-8 (S5FMM4)
brenda
Rosini, E.; Piubelli, L.; Molla, G.; Frattini, L.; Valentino, M.; Varriale, A.; DAuria, S.; Pollegioni, L.
Novel biosensors based on optimized glycine oxidase
FEBS J.
281
3460-3472
2014
Bacillus subtilis (O31616), Bacillus subtilis, Bacillus subtilis 168 (O31616)
brenda
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
Int. J. Biol. Macromol.
79
965-970
2015
Bacillus cereus (L7T8Y9)
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
J. Biol. Chem.
291
23199-23207
2016
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
J. Biotechnol.
184
201-208
2014
Bacillus subtilis (O31616), Bacillus subtilis, Bacillus subtilis 168 (O31616)
brenda
Equar, M.Y.; Tani, Y.; Mihara, H.
Purification and properties of glycine oxidase from Pseudomonas putida KT2440
J. Nutr. Sci. Vitaminol.
61
506-510
2015
Pseudomonas putida (Q88Q83), Pseudomonas putida, 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
PLoS ONE
8
e79175
2013
Bacillus cereus (L7T8Y9), Bacillus cereus
brenda
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