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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-oxomalonate
3-hydroxypyruvate + 2-aminomalonate
L-serine + 2-oxosuccinamate
3-hydroxypyruvate + L-asparagine
-
poor substrate
-
?
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
-
-
-
?
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-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
-
-
-
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
-
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
-
-
-
?
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
-
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
-
-
-
r
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
-
?
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(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
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
-
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
0.23
glyoxylate
-
pH 7.0, 30°C
0.45
glyoxylate
cosubstrate L-alanine, pH 7.6, 30°C
0.54
glyoxylate
cosubstrate L-serine, pH 7.6, 30°C
0.6
glyoxylate
-
pH 8.0, 30°C, cosubstrate L-serine
0.68
glyoxylate
-
recombinant enzyme
0.91
glyoxylate
at 30 mM serine
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
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
0.28
L-serine

-
pH 8.0
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
1.53
L-serine
at 0.5 mM 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
2.7
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
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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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., Methylobacterium organophilum, Methylobacterium organophilum XX, Methylorubrum extorquens, 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, Arabidopsis thaliana (Q56YA5)
brenda
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, Arabidopsis thaliana (Q56YA5)
brenda
Yang, L.; Han, H.; Liu, M.; Zuo, Z.; Zhou, K.; Lü, 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
-
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)
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brenda