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1.4.3.19: glycine oxidase

This is an abbreviated version!
For detailed information about glycine oxidase, go to the full flat file.

Word Map on EC 1.4.3.19

Reaction

2-iminoacetate
+
H2O
=
glyoxylate
 +
NH3

Synonyms

BcGO, glycin oxidase, glycine:oxygen oxidoreductase (deaminating), GlyOX, GO, GOX, GoxA, GOXK, GoxR, LodA, PlGoxA, ThiO

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.19 glycine oxidase

Engineering

Engineering on EC 1.4.3.19 - glycine oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
D103Y/D121G/S122P/R238K/K367R/T368R
-
mutant displays increased activity towards glyphosate with dramatic loss of activity with glycine
D60G
the mutant shows activity with glycine and very low activity with glyphosate
F247P
inactive
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
S122P/H164R/Q346R/E357G/K367R/T368R
-
mutant displays increased activity towards glyphosate with dramatic loss of activity with glycine
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
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
L301V
improvement in residual activity after incubation of 60 min at 60°C to 12.9%
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
T42A
improvement in residual activity after incubation of 60 min at 60°C to 18.7%
T42A/C245S/L301V
improvement in residual activity after incubation of 60 min at 60°C to 74.0%. The mutant enzyme retains most of its enzymatic activity during storage for over a year at 4°C
T42S
improvement in residual activity after incubation of 60 min at 60°C to 31.5%
T42S/C245S/L301V
improvement in residual activity after incubation of 60 min at 60°C to 55.7%
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
-
L301V
-
improvement in residual activity after incubation of 60 min at 60°C to 12.9%
-
M49L
-
the mutant shows reduced catalytic efficiency with glycine compared to the wild type enzyme
-
T42A
-
improvement in residual activity after incubation of 60 min at 60°C to 18.7%
-
T42A/C245S/L301V
-
improvement in residual activity after incubation of 60 min at 60°C to 74.0%. The mutant enzyme retains most of its enzymatic activity during storage for over a year at 4°C
-
T42S
-
improvement in residual activity after incubation of 60 min at 60°C to 31.5%
-
T42S/C245S/L301V
-
improvement in residual activity after incubation of 60 min at 60°C to 55.7%
-
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