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glycine + 3-hydroxypyruvate
glyoxylate + L-serine
-
-
-
r
glycine + pyruvate
glyoxylate + L-alanine
-
-
-
r
L-alanine + 2-oxomalonate
pyruvate + 2-aminomalonate
-
-
-
?
L-alanine + 3-hydroxypyruvate
pyruvate + L-serine
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
L-asparagine + hydroxypyruvate
2-oxosuccinamate + L-serine
-
20% of L-serine transamination activity
-
?
L-asparagine + pyruvate
2-oxosuccinamate + L-alanine
-
-
-
r
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
L-serine + 2-oxomalonate
3-hydroxypyruvate + 2-aminomalonate
L-serine + 2-oxosuccinamate
3-hydroxypyruvate + L-asparagine
-
poor substrate
-
?
L-serine + 3-hydroxypyruvate
3-hydroxypyruvate + L-serine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
L-serine + hydroxypyruvate
3-hydroxypyruvate + L-serine
-
poor substrate
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
55% of the activity with L-serine and glyoxylate
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
20% of L-serine transamination activity
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
poor substrate
-
?
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
-
-
-
r
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
-
-
-
?
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
-
transamination at 38% the rate of L-serine
-
r
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
-
-
-
?
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
-
20% of L-serine transamination actiivty
-
r
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxomalonate
3-hydroxypyruvate + 2-aminomalonate
-
-
-
?
L-serine + 2-oxomalonate
3-hydroxypyruvate + 2-aminomalonate
-
-
-
?
L-serine + 2-oxomalonate
3-hydroxypyruvate + 2-aminomalonate
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
reaction in photorespiratory glycolate pathway
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
reduced activity in vivo results in the accumulation of serine and to a smaller extend, of glycine, indicating that the flux through the photorespiratory pathway is restricted
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
highly specific
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
no activity with Phe, Arg, Val, Trp, Thr, Met
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
nearly irreversible, trace amounts of L-serine
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
no activity with D-serine
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
no or trace activity with oxaloacetate, 2-oxoglutarate
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
no activity with Ala, Glu, Gln, His, oxamate, 2-oxo-n-butanoate, 3-methyl-2-oxo-butanoate, 2-methyl-DL-serine, L-serine-O-sulfate, DL-serine hydroxamate, O-phospho-L-serine
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
plays essential role in methanol assimilation through serine pathway
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
part of the C-1 assimilation pathway
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
reverse reaction at 4-11% the rate of forward reaction
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
preferred substrates
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
preferred substrates
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
involved in glycine metabolism
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
no activity with Phe, Arg, Val, Trp, Thr, Met
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
reverse reaction at 4-11% the rate of forward reaction
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
preferred substrates
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
no or trace activity with oxaloacetate, 2-oxoglutarate
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
no activity with Tyr, Ile, Pro, Cys, Leu, Asp
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
equilibrium towards glycine production
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
reverse reaction at 4-11% the rate of forward reaction
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
physiologically irreversible
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
-
-
r
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
6% of glyoxylate transamination activity
-
r
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
8% of glyoxylate transamination activity
-
r
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
equilibrium towards alanine production
-
r
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
8% of glyoxylate transamination activity
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
poor substrate, 10% of glyoxylate transamination activity
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-alanine + glyoxylate
pyruvate + glycine
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
L-serine + 3-hydroxypyruvate
3-hydroxypyruvate + L-serine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
reaction of alanine-glyoxylate aminotransferase (AGAT), EC 2.6.1.44
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + 2-oxoglutarate
3-hydroxypyruvate + L-glutamate
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
reaction in photorespiratory glycolate pathway
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
reduced activity in vivo results in the accumulation of serine and to a smaller extend, of glycine, indicating that the flux through the photorespiratory pathway is restricted
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
plays essential role in methanol assimilation through serine pathway
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
part of the C-1 assimilation pathway
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
preferred substrates
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
involved in glycine metabolism
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
physiologically irreversible
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
-
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
reaction of serine-pyruvate aminotransferase (SPAT), EC 2.6.1.51
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(NH4)2SO4
-
0.05 mM, 45% inhibition, 5 mM, complete inhibition
AgNO3
-
strong inhibition
ammonium acetate
-
0.1 mM, 42% inhibition, 10 mM, complete inhibition
beta-chloro-L-alanine
reacts with the carbonyl group of pyridoxal phosphate. 53.9% inhibition at 1 mM
beta-chloroalanine
-
competitive vs. L-alanine, uncompetitive vs. 2-oxomalonate
cycloserine
-
weak inhibition
formaldehyde
-
glyoxylate protects
glycine
-
competitive vs. L-serine
HgCl2
-
strong inhibition
Isonicotinic acid hydrazide
-
0.1 mM, 20% inhibition
L-alanine
-
competitive vs. L-serine
L-asparagine
-
competitive vs. serine
L-serine
-
competitive vs. asparagine
oxalate
-
competitive vs. 2-oxomalonate, uncompetitive vs. L-serine
Penicillamine
-
weak inhibition
phenylhydrazine
-
weak inhibition
pyruvate
-
competitive vs. glyoxylate
2-oxoglutarate
2-oxoglutarate at a concentration above 12.5 mM inhibits enzyme SgaBath in the serine-2-oxoglutarate aminotransferase (SKAT) reaction, but has no effect on the serine-glyoxylate aminotranferase (SGAT) reaction, substrate inhibition
2-oxoglutarate
2-oxoglutarate at a concentration above 12.5 mM inhibits enzyme Sga20Z in the serine-2-oxoglutarate aminotransferase (SKAT) reaction, but has no effect on the serine-glyoxylate aminotranferase (SGAT) reaction, substrate inhibition
Aminooxyacetate
reacts with the carbonyl group of pyridoxal phosphate, 88% inhibition at 0.01 mM
Aminooxyacetate
-
1 mM, complete inhibition
Aminooxyacetate
-
competitive inhibition
D-serine
-
competitive inhibition with L-serine
D-serine
-
competitive inhibition
glyoxylate
-
inhibited by glyoxylate above 6 mM
glyoxylate
-
irreversible inhibition only in the presence of NH4+, inactivation in the absence of amino acid substrates
glyoxylate
-
competitive vs. pyruvate
glyoxylate
-
amino acid substrates partially protect
glyoxylate
-
presence of D-serine protects against inhibition
hydroxylamine
-
-
hydroxylamine
-
0.01 mM, 98% inhibition of serine-glyoxylate transamination
hydroxylamine
-
0.01 mM, 85% inhibition of glycin-hydroxypyruvate transamination
hydroxylamine
-
0.1 mM, 97% inhibition, 85% inhibition in the presence of 0.1 mM pyridoxal phosphate
hydroxylamine
-
0.1 mM, 70% inhibition
hydroxylamine
-
0.002 mM, 92% inhibition, serine, L-alanine and glycine protect
N-ethylmaleimide
-
1 mM, 41% inhibition
N-ethylmaleimide
-
weak, but significant inhibition
NH4+
-
reversible inhibition
NH4Cl
-
0.1 mM, 42% inhibition, 10 mM, complete inhibition
NH4Cl
-
glycine-hydroxypyruvate transamination is only weakly inhibited
NH4Cl
-
competitive vs. L-serine
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
1 mM, 37% inhibition
p-hydroxymercuribenzoate
the 24.1% decrease in enzyme activity achieved using 1.0 mM inhibitor might be considered to be unspecific
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
weak but significant inhibition
additional information
-
not inhibited by NaBH4, 3-chloro-D-alanine, 1,10-phenanthroline, 2,2'-dipyridyl, 8-hydroxyquinoline, EDTA, iodoacetate, FeCl3, AlCl3, CdCl2, CoCl2, NiCl2, CaCl2, NaN3, ZnCl2, PbCl2, LiCl, CuCl2, BaCl2, ascorbate, cysteamine, N-ethylmaleimide
-
additional information
-
not inhibited with or without NH4+ by oxalate, formate, acetaldehyde, pyruvate, hydroxypyruvate, 2-oxoglutarate
-
additional information
-
not inhibited by 5,5'-dithio-bis(2-nitrobenzoate)
-
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1.13
2-Oxomalonate
-
pH 8.0
0.63 - 1.1
3-hydroxypyruvate
0.5
glyoxalate
at 30 mM L-alanine
0.57
Hydroxypyruvate
at 15.4 mM glycine
additional information
additional information
-
4.3
2-oxoglutarate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine
5
2-oxoglutarate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine
0.63
3-hydroxypyruvate
-
pH 8.0, 30°C, cosubstrate L-alanine
1.1
3-hydroxypyruvate
-
pH 8.0, 30°C, cosubstrate glycine
0.59
glycine
cosubstrate glyoxylate, pH 8.0, 30°C
1.25
glycine
at 05 mM pyruvate
1.58
glycine
cosubstrate 3-hydroxypyruvate, pH 8.0, 30°C
2.83
glycine
at 0.5 mM hydroxypyruvate
11
glycine
-
pH 8.0, 30°C
0.15
glyoxylate
-
pH 7.0, 27°C
0.17
glyoxylate
-
pH 7.0, temperature not specified in the publication, recombinant enzyme, with L-serine
0.23
glyoxylate
-
pH 7.0, 30°C
0.24
glyoxylate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine
0.45
glyoxylate
cosubstrate L-alanine, pH 7.6, 30°C
0.54
glyoxylate
cosubstrate L-serine, pH 7.6, 30°C
0.59
glyoxylate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-alanine
0.6
glyoxylate
-
pH 8.0, 30°C, cosubstrate L-serine
0.68
glyoxylate
-
recombinant enzyme
0.7
glyoxylate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine
0.91
glyoxylate
at 30 mM serine
1
glyoxylate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-alanine
4.6
glyoxylate
-
pH 8.1, 30°C, cosubstrate L-serine
0.58
L-alanine
at 0.5 mM glyoxylate
0.87
L-alanine
cosubstrate glyoxylate, pH 8.0, 30°C
1.08
L-alanine
cosubstrate 3-hydroxypyruvate, pH 8.0, 30°C
1.25
L-alanine
at 10 mM glyoxylate
2 - 3
L-alanine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate
14
L-alanine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate
20
L-alanine
-
pH 8.0, 30°C
52.53
L-alanine
cosubstrate glyoxylate, pH 7.6, 30°C
2.82
L-asparagine
cosubstrate glyoxylate, pH 8.0, 30°C
3.9
L-asparagine
-
pH 8.1, 30°C, cosubstrate glyoxylate
4.5
L-asparagine
-
pH 8.1, 30°C, cosubstrate pyruvate
8.41
L-asparagine
cosubstrate 3-hydroxypyruvate, pH 8.0, 30°C
0.089
L-serine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with pyruvate
0.089
L-serine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with pyruvate
0.18
L-serine
-
pH 7.0, temperature not specified in the publication, recombinant enzyme, with pyruvate
0.39
L-serine
-
cosubstrate pyruvate
0.5
L-serine
-
pH 8.1, 30°C, cosubstrate pyruvate
0.6
L-serine
-
pH 8.1, 30°C, cosubstrate glyoxylate
0.71
L-serine
-
pH 8.0, 30°C, cosubstrate glyoxylate
0.99
L-serine
cosubstrate 3-hydroxypyruvate, pH 8.0, 30°C
1.06
L-serine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with 2-oxoglutarate
1.17
L-serine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with 2-oxoglutarate
1.53
L-serine
at 0.5 mM glyoxylate
1.62
L-serine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate
2.1
L-serine
-
pH 7.0, temperature not specified in the publication, recombinant enzyme, with glyoxylate
2.19
L-serine
cosubstrate pyruvate, pH 7.6, 30°C
2.41
L-serine
cosubstrate glyoxylate, pH 7.6, 30°C
2.47
L-serine
cosubstrate glyoxylate, pH 8.0, 30°C
2.6
L-serine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate
2.7
L-serine
-
pH 7.0, 27°C
3.86
L-serine
-
recombinant enzyme
5
L-serine
at 10 mM glyoxylate
0.22
pyruvate
at 15.4 mM glycine
0.61
pyruvate
cosubstrate L-serine, pH 7.6, 30°C
2
pyruvate
-
pH 8.1, 30°C, cosubstrate L-serine
2.5
pyruvate
-
pH 8.1, 30°C, cosubstrates: L-asparagine, glyoxylate, L-asparagine
4.5
pyruvate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine
5.8
pyruvate
-
pH 7.0, temperature not specified in the publication, recombinant enzyme, with L-serine
6
pyruvate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine
additional information
additional information
-
kinetic study
-
additional information
additional information
-
assay method using high performance liquid chromatography with 1-fluoro-2,4-dinitrobenzene pre-column derivatizaion
-
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evolution
-
phylogenetic analysis and tree
evolution
phylogenetic analysis and tree
evolution
phylogenetic analysis and tree
evolution
-
phylogenetic analysis and tree
-
evolution
-
phylogenetic analysis and tree
-
evolution
-
phylogenetic analysis and tree
-
evolution
-
phylogenetic analysis and tree
-
evolution
-
phylogenetic analysis and tree
-
evolution
-
phylogenetic analysis and tree
-
evolution
-
phylogenetic analysis and tree
-
malfunction
elevated SGAT activity through transgenic overexpression of Flaveria pringlei SGAT causes clear changes in metabolism and interferes with photosynthetic CO2 uptake and biomass accumulation of Arabidopsis. The faster serine turnover during photorespiration progressively lowers day-time leaf serine contents and in turn induces the phosphoserine pathway. Transcriptional upregulation of this additional route of serine biosynthesis occurs already during the day but particularly at night, efficiently counteracting night-time serine depletion. Additionally, higher SGAT activity results in an increased use of asparagine as the external donor of amino groups to the photorespiratory pathway but does not alter leaf asparagine content at night. These results suggest leaf SGAT activity needs to be dynamically adjusted to ensure (i) variable flux through the photorespiratory pathway at a minimal consumption of asparagine and (ii) adequate serine levels for other cellular metabolism, phenotype analysis. Impact of excess SGAT activity on the photorespiratory pathway and photorespiratory nitrogen cycling, schematic overview
malfunction
the disruption of the sga gene in Methylomicrobium alcaliphilum results in retardation of growth rate of the mutant cells and in a prolonged lag-phase after passaging from methane to methanol. In addition, the growth of the mutant strain is accompanied by formaldehyde accumulation in the culture liquid
malfunction
-
the disruption of the sga gene in Methylomicrobium alcaliphilum results in retardation of growth rate of the mutant cells and in a prolonged lag-phase after passaging from methane to methanol. In addition, the growth of the mutant strain is accompanied by formaldehyde accumulation in the culture liquid
-
malfunction
-
elevated SGAT activity through transgenic overexpression of Flaveria pringlei SGAT causes clear changes in metabolism and interferes with photosynthetic CO2 uptake and biomass accumulation of Arabidopsis. The faster serine turnover during photorespiration progressively lowers day-time leaf serine contents and in turn induces the phosphoserine pathway. Transcriptional upregulation of this additional route of serine biosynthesis occurs already during the day but particularly at night, efficiently counteracting night-time serine depletion. Additionally, higher SGAT activity results in an increased use of asparagine as the external donor of amino groups to the photorespiratory pathway but does not alter leaf asparagine content at night. These results suggest leaf SGAT activity needs to be dynamically adjusted to ensure (i) variable flux through the photorespiratory pathway at a minimal consumption of asparagine and (ii) adequate serine levels for other cellular metabolism, phenotype analysis. Impact of excess SGAT activity on the photorespiratory pathway and photorespiratory nitrogen cycling, schematic overview
-
malfunction
-
the disruption of the sga gene in Methylomicrobium alcaliphilum results in retardation of growth rate of the mutant cells and in a prolonged lag-phase after passaging from methane to methanol. In addition, the growth of the mutant strain is accompanied by formaldehyde accumulation in the culture liquid
-
malfunction
-
the disruption of the sga gene in Methylomicrobium alcaliphilum results in retardation of growth rate of the mutant cells and in a prolonged lag-phase after passaging from methane to methanol. In addition, the growth of the mutant strain is accompanied by formaldehyde accumulation in the culture liquid
-
malfunction
-
the disruption of the sga gene in Methylomicrobium alcaliphilum results in retardation of growth rate of the mutant cells and in a prolonged lag-phase after passaging from methane to methanol. In addition, the growth of the mutant strain is accompanied by formaldehyde accumulation in the culture liquid
-
metabolism
-
enzymic activity within the cell gradually decreases with the increase of cell density. Activity is significantly affected by light intensity and growth in presence of acetate as sole carbon source. Activity increases in presence of high oxygen concentrations and high carbon dioxide concentrations. An increase in oxygen concentration additionally results in a raise of cellular Gly/Ser ratio from 0.79 to 1.49
metabolism
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
metabolism
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
metabolism
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
metabolism
serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate during photorespiration. Besides this, SGAT operates with several other substrates including asparagine, impact of this enzymatic promiscuity on plant metabolism, particularly photorespiration and serine biosynthesis, overview
metabolism
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
-
metabolism
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
-
metabolism
-
serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate during photorespiration. Besides this, SGAT operates with several other substrates including asparagine, impact of this enzymatic promiscuity on plant metabolism, particularly photorespiration and serine biosynthesis, overview
-
metabolism
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
-
metabolism
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
-
metabolism
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
-
metabolism
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
-
metabolism
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds
-
physiological function
overexpression in Lemna minor results in increased enzymic activity and decreased endogenous serine levels under salt stress, leading to enhanced protection against root abscission, higher maximum quantum yield of photosystem II, increased defense from cell damage as a result of improved cell membrane integrity, a decrease of reactive oxygen species accumulation, and a strengthened antioxidant system
physiological function
rice leaves usually show 3-4 times higher abundance of glutamate relative to serine, implicating that glutamate:glyoxylate aminotransferase GGAT may preferentially utilize glyoxylate to form glycine over serine:glyoxylate aminotransferase SGAT. When SGAT or GGAT activity is regulated by gene transformation or nitrogen deficiency, respectively, the glycine content is positively related to GGAT activities, while both serine and glycine contents are negatively related to SGAT activities, suggesting that GGAT preferentially catalyzes the conversion of glyoxylate into glycine while SGAT is mainly responsible for the transamination reaction of serine to hydroxypyruvate in the photorespiratory pathway of rice
physiological function
Arabidopsis thaliana serine:glyoxylate aminotransferase (AGT1) is a multifunctional class IV aminotransferase protein that catalyzes transamination reactions using L-serine, L-alanine, and L-asparagine as amino donors and glyoxylate, pyruvate, and hydroxypyruvate as amino acceptors. AGT1 is a peroxisomal aminotransferase with a central role in photorespiration. This enzyme catalyzes various aminotransferase reactions, including serine:glyoxylate, alanine:glyoxylate, and asparagine:glyoxylate transaminations
physiological function
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
physiological function
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
physiological function
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
physiological function
-
serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate
physiological function
serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate during photorespiration. Besides this, SGAT operates with several other substrates including asparagine, impact of this enzymatic promiscuity on plant metabolism, particularly photorespiration and serine biosynthesis, overview
physiological function
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
-
physiological function
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
-
physiological function
-
serine:glyoxylate aminotransferase (SGAT) converts glyoxylate and serine to glycine and hydroxypyruvate during photorespiration. Besides this, SGAT operates with several other substrates including asparagine, impact of this enzymatic promiscuity on plant metabolism, particularly photorespiration and serine biosynthesis, overview
-
physiological function
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
-
physiological function
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
-
physiological function
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
-
physiological function
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
-
physiological function
-
serine-glyoxylate aminotransferase (Sga) is the indicator enzyme of the serine pathway of assimilation of reduced C1 compounds. The Sga enzyme from the methanotroph catalyses the pyridoxal phosphate-dependent transfer of an amino group from serine to glyoxylate and pyruvate. The enzyme also transfers an amino group from serine to 2-oxoglutarate and from alanine to glyoxylate. Enzyme Sga is important in the serine cycle of type I methanotrophs and this pathway might be related to the removal of excess formaldehyde and/or energy regulation
-
additional information
in the enzyme crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologues of AGT1. Residues Tyr35' and Arg36', entering the active site from the other subunits in the dimer, mediate interactions between AGT and L-serine when used as a substrate. Structural model of AGT1 and structure-function analysis, structure comparisons, detailed overview
additional information
-
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
additional information
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
additional information
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
additional information
-
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
-
additional information
-
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
-
additional information
-
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
-
additional information
-
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
-
additional information
-
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
-
additional information
-
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
-
additional information
-
influence of metabolites on the activity of recombinant serineglyoxylate aminotransferase, overview
-
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Hagishita, T.; Yoshida, T.; Izumi, Y.; Mitsunaga, T.
Immunological characterization of serine-glyoxylate aminotransferase and hydroxypyruvate reductase from a methylotrophic bacterium, Hyphomicrobium methylovorum GM2
FEMS Microbiol. Lett.
142
49-52
1996
Hyphomicrobium methylovorum, Hyphomicrobium sp., Methylorubrum extorquens, Methylobacterium organophilum, Methylobacterium organophilum XX, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
brenda
Smith, I.K.
Purification and characterization of serine:glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris)
Biochim. Biophys. Acta
321
156-164
1973
Phaseolus vulgaris
brenda
Carpe, A.I.; Smith, I.K.
Serine-glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris). II. The reverse reactions
Biochim. Biophys. Acta
370
96-101
1974
Phaseolus vulgaris
brenda
Ireland, R.J.; Joy, K.W.
Purification and properties of an asparagine aminotransferase from Pisum sativum leaves
Arch. Biochem. Biophys.
223
291-296
1983
Pisum sativum
brenda
Nakamura, Y.; Tolbert, N.E.
Serine:glyoxylate, alanine:glyoxylate, and glutamate:glyoxylate aminotransferase reactions in peroxisomes from spinach leaves
J. Biol. Chem.
258
2763-2768
1983
Spinacia oleracea
-
brenda
Hondred, D.; Hunter, J.McC.; Keith, R.; Titus, D.E.; Becker, W.M.
Isolation of serine:glyoxylate aminotransferase from cucumber cotyledons
Plant Physiol.
79
95-102
1985
Cucumis sativus
brenda
Havir, E.A.
Inactivation of serine:glyoxylate and glutamate:glyoxylate aminotransferases from tobaco leaves by glyoxylate in the presence of ammonium ion
Plant Physiol.
80
473-478
1986
Nicotiana tabacum
brenda
Izumi, Y.; Yoshida, T.; Yamada, H.
Purification and characterization of serine-glyoxylate aminotransferase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2
Eur. J. Biochem.
190
285-290
1990
Hyphomicrobium methylovorum
brenda
Paszkowski, A.
Some properties of serine: glyoxylate aminotransferase from rye seedlings (Secale cereale L.)
Acta Biochim. Pol.
38
437-448
1991
Secale cereale
brenda
Paszkowski, A.; Niedzielska, A.
Serine:glyoxylate aminotransferase from the seedlings of rye (Secale cereale L.)
Acta Biochim. Pol.
37
277-282
1990
Secale cereale
brenda
Paszkowski, A.
Inhibition of glutamate: glyoxylate and serine: Glyoxylate aminotransferases from rye seedlings (Secale cereale L.) by glyoxylate or glyoxylate in the presence of ammonium ion
Acta Physiol. Plant.
16
217-223
1994
Secale cereale
-
brenda
Paszkowski, A.
The hydrosulfide groups of glutamate:glyoxylate and serine:glyoxylate aminotransferases from rye (Secale cereale L.) seedlings
Acta Physiol. Plant.
17
85-90
1995
Secale cereale
-
brenda
Hagishita, T.; Yoshida, T.; Izumi, Y.; Mitsunaga, T.
Cloning and expression of the gene for serine-glyoxylate aminotransferase from an obligate methylotroph Hyphomicrobium methylovorum GM2
Eur. J. Biochem.
241
1-5
1996
Hyphomicrobium methylovorum
brenda
Wingler, A.; Ann, V.J.; Lea, P.J.; Leegood, R.C.
Serine: glyoxylate aminotransferase exerts no control on photosynthesis
J. Exp. Bot.
50
719-722
1999
Hordeum vulgare
-
brenda
Karsten, W.E.; Ohshiro, T.; Izumi, Y.; Cook, P.F.
Initial velocity, spectral, and pH studies of the serine-glyoxylate aminotransferase from Hyphomicrobiuim methylovorum
Arch. Biochem. Biophys.
388
267-275
2001
Hyphomicrobium methylovorum
brenda
Karsten, W.E.; Cook, P.F.
Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase
Methods Enzymol.
354
223-237
2002
Hyphomicrobium methylovorum
brenda
Truszkiewicz, W.; Paszkowski, A.
Some structural properties of plant serine:glyoxylate aminotransferase?
Acta Biochim. Pol.
52
527-534
2005
Triticum aestivum, Zea mays
brenda
Zhu, Y.; Lu, X.; Wang, X.; Wang, Y.
Determination of serine:glyoxylate aminotransferase activity by high performance liquid chromatography
Sepu
21
584-586
2003
Lemna gibba
-
brenda
Karsten, W.E.; Ohshiro, T.; Izumi, Y.; Cook, P.F.
Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate
Biochemistry
44
15930-15936
2005
Hyphomicrobium methylovorum
brenda
Tian, B.; Wang, Y.; Zhu, Y.; Lu, X.; Huang, K.; Shao, N.; Beck, C.F.
Synthesis of the photorespiratory key enzyme serine: glyoxylate aminotransferase in C. reinhardtii is modulated by the light regime and cytokinin
Physiol. Plant.
127
571-582
2006
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 325
brenda
Kendziorek, M.; Paszkowski, A.
Properties of serine:glyoxylate aminotransferase purified from Arabidopsis thaliana leaves
Acta Biochim. Biophys. Sin. (Shanghai)
40
102-110
2008
Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana
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Karsten, W.E.; Cook, P.F.
Detection of a gem-diamine and a stable quinonoid intermediate in the reaction catalyzed by serine-glyoxylate aminotransferase from Hyphomicrobium methylovorum
Biochim. Biophys. Acta
1790
575-580
2009
Hyphomicrobium methylovorum
brenda
Nagata, M.; Ichiyama, A.; Takayama, T.; Oda, T.; Mugiya, S.; Ozono, S.
Assay of alanine:glyoxylate aminotransferase in human liver by its serine:glyoxylate aminotransferase activity
Biomed. Res.
30
295-301
2009
Homo sapiens
brenda
Zhang, Q.; Lee, J.; Pandurangan, S.; Clarke, M.; Pajak, A.; Marsolais, F.
Characterization of Arabidopsis serine:glyoxylate aminotransferase, AGT1, as an asparagine aminotransferase
Phytochemistry
85
30-35
2013
Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana
brenda
Yang, L.; Han, H.; Liu, M.; Zuo, Z.; Zhou, K.; L, J.; Zhu, Y.; Bai, Y.; Wang, Y.
Overexpression of the Arabidopsis photorespiratory pathway gene, serine: glyoxylate aminotransferase (AtAGT1), leads to salt stress tolerance in transgenic duckweed (Lemna minor)
Plant Cell Tissue Organ Cult.
113
407-416
2013
Arabidopsis thaliana (Q56YA5)
-
brenda
Li, H.; Zhu, K.; Liu, Q.; Zuo, Z.; Zhu, Y.; Bai, Y.; Wang, Y.
Variations in SGAT enzyme activity of Chiamydomonas reinhardtii L. cells under different cultural conditions
Plant Physiol. Commun.
46
359-364
2010
Chlamydomonas reinhardtii
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brenda
Zhang, Z.; Mao, X.; Ou, J.; Ye, N.; Zhang, J.; Peng, X.
Distinct photorespiratory reactions are preferentially catalyzed by glutamate:glyoxylate and serine:glyoxylate aminotransferases in rice
J. Photochem. Photobiol. B
142
110-117
2015
Oryza sativa Japonica Group (A0A0P0XHN6)
brenda
But, S.Y.; Egorova, S.V.; Khmelenina, V.N.; Trotsenko, Y.A.
Serine-glyoxylate aminotranferases from methanotrophs using different C1-assimilation pathways
Antonie van Leeuwenhoek
112
741-751
2019
Methylosinus trichosporium, Methylotuvimicrobium alcaliphilum (G4T3S7), Methylococcus capsulatus (Q608T3), Methylococcus capsulatus Bath (Q608T3), Methylotuvimicrobium alcaliphilum VKM B-2133 (G4T3S7), Methylococcus capsulatus ATCC 33009 (Q608T3), Methylotuvimicrobium alcaliphilum 20Z (G4T3S7), Methylotuvimicrobium alcaliphilum 20Z, Methylococcus capsulatus NCIMB 11132 (Q608T3), Methylotuvimicrobium alcaliphilum DSM 19304 (G4T3S7), Methylotuvimicrobium alcaliphilum NCIMB 14124 (G4T3S7)
brenda
Liepman, A.H.; Vijayalakshmi, J.; Peisach, D.; Hulsebus, B.; Olsen, L.J.; Saper, M.A.
Crystal structure Of photorespiratory alanine glyoxylate aminotransferase 1 (AGT1) from Arabidopsis thaliana
Front. Plant Sci.
10
1229
2019
Arabidopsis thaliana (Q56YA5)
brenda
Modde, K.; Timm, S.; Florian, A.; Michl, K.; Fernie, A.R.; Bauwe, H.
High serine glyoxylate aminotransferase activity lowers leaf daytime serine levels, inducing the phosphoserine pathway in Arabidopsis
J. Exp. Bot.
68
643-656
2017
Flaveria pringlei, Arabidopsis thaliana (Q56YA5), Arabidopsis thaliana Col-0 (Q56YA5)
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