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Information on EC 2.6.1.45 - serine-glyoxylate transaminase
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EC Tree
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
-
mistargeting
-
liver-specific
- pyridoxine
-
photorespiration
-
photorespiratory
- oxalosis
-
2.6.1.44
-
glutamate:glyoxylate
- nephrocalcinosis
-
intraperoxisomal
-
liver-kidney
-
peroxisome-to-mitochondrion
-
anlage
- urolithiasis
- hyphomicrobium
-
plp-dependent
- methylovorum
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
AGT1, alanine:glyoxylate aminotransferase, aminotransferase, serine-glyoxylate, FpSGAT, L-serine glyoxylate aminotransferase, More, Os08g0502700, serine-alpha-ketoglutarate aminotransferase, serine-glyoxylate aminotranferase, serine-glyoxylate aminotransferase, 
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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-alpha-ketoglutarate aminotransferase
serine-glyoxylate aminotranferase
serine-glyoxylate aminotransferase
serine:glyoxylate aminotransferase
Sga
Sga20Z
SGAT
SKAT
additional information
serine-glyoxylate aminotransferase
-
-
-
-
additional information
see also EC 2.6.1.51 and 2.6.1.44
-
additional information
see also EC 2.6.1.51 and 2.6.1.44
-
additional information
see also EC 2.6.1.44 and EC 2.6.1.51
additional information
see also EC 2.6.1.44 and EC 2.6.1.51
-
additional information
see also EC 2.6.1.44 and EC 2.6.1.51
-
additional information
see also EC 2.6.1.44 and EC 2.6.1.51
-
additional information
see also EC 2.6.1.44 and EC 2.6.1.51
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
reaction is catalyzed via the initial formation of an external Schiff base intermediate
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
-
-
-
-
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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 + 3-hydroxypyruvate
3-hydroxypyruvate + L-serine
-
-
-
?
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
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
-
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-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
-
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
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
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
-
preferred substrates
-
-
?
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
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
-
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 + 3-hydroxypyruvate
3-hydroxypyruvate + L-serine
-
-
-
?
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
-
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
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
-
physiologically irreversible
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein, 4 mol per mol enzyme
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per subunit
pyridoxal 5'-phosphate
PLP, is bound at the active site but is not held in place by covalent interactions
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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
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
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
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
0.17
glyoxylate
-
pH 7.0, temperature not specified in the publication, recombinant enzyme, with L-serine
0.24
glyoxylate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine
0.59
glyoxylate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-alanine
0.7
glyoxylate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine
1
glyoxylate
pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-alanine
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
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
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
1.62
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
2.6
L-serine
pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate
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
-
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
the C-terminal tripeptide Ser-Arg-Ile (residues 399-401) constitute a type 1 peroxisomal targeting sequence (PTS1)
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
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
-
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 (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
-
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 (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
-
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
-
Show AA Sequence and Transmembrane Helices (585 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
170000
40000
43000
45000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotrimer
tetramer
dimer
crystal structure, enzyme in solution, catalytic enzyme form
tetramer
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in apoform and complexed with L-serine, large, greenish-yellow crystals grow from drops containing equal volumes of 11 mg/ml protein in 0.2 mM PLP, 10% glycerol, and 100 mM Tris-HCl, pH 8.5, and precipitant solution containing 4.1-4.2 M sodium formate, equilibration against the same precipitant, several days, at room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.1 A resolution, respectively, modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P251L
the sat mutation likely affects the dimer interface near the catalytic site, phenotype overview. The point mutation renders the sat mutant plants lethally stunted when grown in normal atmospheric conditions
additional information
additional information
transgenic overexpression of Flaveria pringlei SGAT in Arabidopsis thaliana rosette leaves via transfection with Agrobacterium tumefaciens strain GV3101, quantitative RT-PCR enzyme expression analysis
additional information
-
transgenic overexpression of Flaveria pringlei SGAT in Arabidopsis thaliana rosette leaves via transfection with Agrobacterium tumefaciens strain GV3101, quantitative RT-PCR enzyme expression analysis
-
additional information
-
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 thaliana. 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. Phenotype, detailed overview
additional information
the sga20Z gene is knocked out by the insertion of the kanamycin cassette using double homologous recombination. The growth rate of the DELTAsga strain on methane is significantly lower as compared to the wild-type strain. During growth on methanol, this effect is even more pronounced
additional information
-
the sga20Z gene is knocked out by the insertion of the kanamycin cassette using double homologous recombination. The growth rate of the DELTAsga strain on methane is significantly lower as compared to the wild-type strain. During growth on methanol, this effect is even more pronounced
-
additional information
-
the sga20Z gene is knocked out by the insertion of the kanamycin cassette using double homologous recombination. The growth rate of the DELTAsga strain on methane is significantly lower as compared to the wild-type strain. During growth on methanol, this effect is even more pronounced
-
additional information
-
the sga20Z gene is knocked out by the insertion of the kanamycin cassette using double homologous recombination. The growth rate of the DELTAsga strain on methane is significantly lower as compared to the wild-type strain. During growth on methanol, this effect is even more pronounced
-
additional information
-
the sga20Z gene is knocked out by the insertion of the kanamycin cassette using double homologous recombination. The growth rate of the DELTAsga strain on methane is significantly lower as compared to the wild-type strain. During growth on methanol, this effect is even more pronounced
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.1
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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
-
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
expression in Escherichia coli
gene sgat, transgenic overexpression of Flaveria pringlei SGAT in Arabidopsis thaliana ecotype Col-0 rosette leaves via transfection with Agrobacterium tumefaciens strain GV3101, quantitative RT-PCR enzyme expression analysis
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
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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., 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
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 (Q56YA5), Arabidopsis thaliana
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)
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, Methylomicrobium alcaliphilum (G4T3S7), Methylococcus capsulatus (Q608T3), Methylococcus capsulatus Bath (Q608T3), Methylococcus capsulatus ATCC 33009 (Q608T3), Methylomicrobium alcaliphilum NCIMB 14124 (G4T3S7), Methylomicrobium alcaliphilum 20Z (G4T3S7), Methylomicrobium alcaliphilum 20Z, Methylomicrobium alcaliphilum DSM 19304 (G4T3S7), Methylomicrobium alcaliphilum VKM B-2133 (G4T3S7), Methylococcus capsulatus NCIMB 11132 (Q608T3)
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)
brenda
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