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Information on EC 2.6.1.45 - serine-glyoxylate transaminase
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2.6.1.45 serine-glyoxylate transaminaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 2.6.1.45
- hyperoxaluria
- peroxisomal
- oxalate
- pyridoxal
- hydroxypyruvate
-
liver-specific
-
mistargeting
- pyridoxine
-
transamination
-
photorespiratory
-
glutamate:glyoxylate
-
2.6.1.44
- oxalosis
-
photorespiration
-
liver-kidney
- methylovorum
- nephrocalcinosis
-
anlage
- urolithiasis
-
peroxisome-to-mitochondrion
-
intraperoxisomal
- hyphomicrobium
-
plp-dependent
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
alanine:glyoxylate aminotransferase, aminotransferase, serine-glyoxylate, L-serine glyoxylate aminotransferase, Os08g0502700, serine-glyoxylate aminotransferase, serine:glyoxylate aminotransferase, SGAT, SGT, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alanine:glyoxylate aminotransferase
-
the human liver enzyme has also serine:glyoxylate aminotransferase activity
aminotransferase, serine-glyoxylate
-
-
-
-
L-serine glyoxylate aminotransferase
-
-
-
-
serine-glyoxylate aminotransferase
SGAT
serine-glyoxylate aminotransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
-
-
-
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
ping-pong reaction mechanism
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
ping-pong reaction mechanism
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
ping-pong reaction mechanism
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
ping pong bi bi mechanism
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
ping-pong reaction mechanism; reaction is catalyzed via the initial formation of an external Schiff base intermediate
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-serine:glyoxylate aminotransferase
A pyridoxal-phosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY
37259-57-7
-
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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
L-alanine + 2-oxomalonate
pyruvate + 2-aminomalonate
-
-
-
?
L-asparagine + hydroxypyruvate
2-oxosuccinamate + L-serine
-
20% of L-serine transamination activity
-
?
L-serine + 2-oxosuccinamate
3-hydroxypyruvate + L-asparagine
-
poor substrate
-
?
L-serine + hydroxypyruvate
3-hydroxypyruvate + L-serine
-
poor substrate
-
?
L-alanine + glyoxylate
pyruvate + glycine
55% of the activity with L-serine and glyoxylate
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
-
20% of L-serine transamination activity
-
?
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
-
transamination at 38% the rate of L-serine
-
r
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
-
reaction in photorespiratory glycolate pathway
-
-
-
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
-
-
-
ir
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
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
?
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
-
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
-
reverse reaction at 4-11% the rate of forward reaction
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
physiologically irreversible
-
-
-
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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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
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
reaction in photorespiratory glycolate pathway
-
-
-
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
-
involved in glycine metabolism
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
physiologically irreversible
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein, 4 mol per mol enzyme; required for activity
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per subunit
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
oxalate
-
competitive vs. 2-oxomalonate, uncompetitive vs. L-serine
Aminooxyacetate
reacts with the carbonyl group of pyridoxal phosphate, 88% inhibition at 0.01 mM
glyoxylate
-
irreversible inhibition only in the presence of NH4+, inactivation in the absence of amino acid substrates
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
-
0.002 mM, 92% inhibition, serine, L-alanine and glycine protect
p-hydroxymercuribenzoate
the 24.1% decrease in enzyme activity achieved using 1.0 mM inhibitor might be considered to be unspecific
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
pyruvate
-
pH 8.1, 30°C, cosubstrates: L-asparagine, glyoxylate, L-asparagine
additional information
additional information
-
assay method using high performance liquid chromatography with 1-fluoro-2,4-dinitrobenzene pre-column derivatizaion
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
approx. 60% of maximal activity at pH 6, approx. half-maximal activity at pH 9
7.5 - 9.2
-
approx. 50% activity at pH 7.5 and 9.2, no activity below pH 6.7 and above pH 9.9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GM2, glycine-resistant mutant derived from parent strain KM146
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
40000
43000
45000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.1
-
1 mM Tris/glycine, about 60% dimer, 40% monomer in solution; 50 mM Tris/glycine, about 87% dimer, 13% monomer
657439
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM phosphate buffer pH 7, 0.1 mM pyridoxal phosphate, 0.1 mM dithiothreitol, 45% v/v glycerol, at least 5 months
-
5°C, stable overnight, 20% loss of activity per day on further storage, in 20% ethylene glycol or 15% glycerol, 20% loss of activity within 5 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sephacel, phenyl-Sepharose, CM-toyopearl, Cellulofine
-
DEAE-cellulose, agarose gel, Brushite, Sephadex g-200, partial purification
-
pH 5.4, polyethylene glycol 6000, DEAE-Sephadex A25, Sephacryl S-300, partial purification
-
polyethyleneimine, ammonium sulfate, Ultrogel AcA 34, DEAE-cellulose, isoenzymes A and B
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
In the roots of 10-day-old seedlings treated for 2 h with 20 mM Asn, the transcript levels are raised by 2fold. During this treatment, the concentration of Asn in root is raised by ca. 5fold
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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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)
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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)
-
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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
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