Information on EC 2.6.1.45 - serine-glyoxylate transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.6.1.45
-
RECOMMENDED NAME
GeneOntology No.
serine-glyoxylate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
show the reaction diagram
ping-pong reaction mechanism
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
show the reaction diagram
ping-pong reaction mechanism
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
show the reaction diagram
ping pong bi bi mechanism
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
show the reaction diagram
ping-pong reaction mechanism
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
show the reaction diagram
ping-pong reaction mechanism; reaction is catalyzed via the initial formation of an external Schiff base intermediate
-
L-serine + glyoxylate = 3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
formaldehyde assimilation I (serine pathway)
-
Glycine, serine and threonine metabolism
-
Glyoxylate and dicarboxylate metabolism
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
photorespiration
-
SYSTEMATIC NAME
IUBMB Comments
L-serine:glyoxylate aminotransferase
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
-
serine-glyoxylate aminotransferase
-
-
serine-glyoxylate aminotransferase
Chlamydomonas reinhardtii 325
-
-
-
serine-glyoxylate aminotransferase
-
-
serine:glyoxylate aminotransferase
Q56YA5
-
SGAT
Chlamydomonas reinhardtii 325
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37259-57-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Landsberg erecta
SwissProt
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 325
strain 325
-
-
Manually annotated by BRENDA team
cucumber, cv. Improved Long Green
-
-
Manually annotated by BRENDA team
GM2, glycine-resistant mutant derived from parent strain KM146
-
-
Manually annotated by BRENDA team
strains NCIB10099, X, JTS-811, ZV622 and 53-49
-
-
Manually annotated by BRENDA team
duckweed
-
-
Manually annotated by BRENDA team
Methylobacterium organophilum XX
strain XX
-
-
Manually annotated by BRENDA team
kidney bean, cv. Red Kidney
-
-
Manually annotated by BRENDA team
pea, cv. Little Marvel
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycine + 3-hydroxypyruvate
glyoxylate + L-serine
show the reaction diagram
Q56YA5
-
-
-
r
glycine + pyruvate
glyoxylate + L-alanine
show the reaction diagram
Q56YA5
-
-
-
r
L-alanine + 2-oxomalonate
pyruvate + 2-aminomalonate
show the reaction diagram
-
-
-
?
L-alanine + 3-hydroxypyruvate
pyruvate + L-serine
show the reaction diagram
Q56YA5
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
Q56YA5
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
poor substrate
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
20% of L-serine transamination activity
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
Q56YA5
55% of the activity with L-serine and glyoxylate
-
-
?
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
show the reaction diagram
-
-
-
?
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
show the reaction diagram
-
-
-
-
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
show the reaction diagram
Q56YA5
-
-
-
r
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
show the reaction diagram
-
20% of L-serine transamination actiivty
-
r
L-asparagine + glyoxylate
2-oxosuccinamate + glycine
show the reaction diagram
-
transamination at 38% the rate of L-serine
-
r
L-asparagine + hydroxypyruvate
2-oxosuccinamate + L-serine
show the reaction diagram
-
20% of L-serine transamination activity
-
?
L-asparagine + pyruvate
2-oxosuccinamate + L-alanine
show the reaction diagram
Q56YA5
-
-
-
r
L-serine + 2-oxomalonate
3-hydroxypyruvate + 2-aminomalonate
show the reaction diagram
-
-
-
-
L-serine + 2-oxomalonate
3-hydroxypyruvate + 2-aminomalonate
show the reaction diagram
-
-
-
?
L-serine + 2-oxomalonate
3-hydroxypyruvate + 2-aminomalonate
show the reaction diagram
-
-
-
-
?
L-serine + 2-oxosuccinamate
3-hydroxypyruvate + L-asparagine
show the reaction diagram
-
poor substrate
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
Q56YA5
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
Q56YA5
-
-
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
highly specific
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
no activity with Phe, Arg, Val, Trp, Thr, Met
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
no activity with Phe, Arg, Val, Trp, Thr, Met
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
reverse reaction at 4-11% the rate of forward reaction
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
reverse reaction at 4-11% the rate of forward reaction
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
reverse reaction at 4-11% the rate of forward reaction
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
nearly irreversible, trace amounts of L-serine, no activity with D-serine
-
ir
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
preferred substrates
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
preferred substrates
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
preferred substrates, no or trace activity with oxaloacetate, 2-oxoglutarate
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
no or trace activity with oxaloacetate, 2-oxoglutarate, 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
show the reaction diagram
-
no activity with Tyr, Ile, Pro, Cys, Leu, Asp, equilibrium towards glycine production
-
r
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
involved in glycine metabolism
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
physiologically irreversible
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
reaction in photorespiratory glycolate pathway
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
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
show the reaction diagram
-
plays essential role in methanol assimilation through serine pathway
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
part of the C-1 assimilation pathway
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
Methylobacterium organophilum XX
-
-
-
?
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
Chlamydomonas reinhardtii 325
-
-
-
-
?
L-serine + hydroxypyruvate
3-hydroxypyruvate + L-serine
show the reaction diagram
-
poor substrate
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
-
-
-
-
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
Q56YA5
-
-
-
r
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
-
8% of glyoxylate transamination activity
-
r
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
-
8% of glyoxylate transamination activity
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
-
poor substrate, 10% of glyoxylate transamination activity
-
?
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
-
6% of glyoxylate transamination activity
-
r
L-serine + pyruvate
3-hydroxypyruvate + L-alanine
show the reaction diagram
-
equilibrium towards alanine production
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
-
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
involved in glycine metabolism
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
physiologically irreversible
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
reaction in photorespiratory glycolate pathway
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
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
show the reaction diagram
-
plays essential role in methanol assimilation through serine pathway
-
-
-
L-serine + glyoxylate
3-hydroxypyruvate + glycine
show the reaction diagram
-
part of the C-1 assimilation pathway
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
Km-value: 0.0025 mM; required for activity
pyridoxal 5'-phosphate
-
required for activity
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein, 4 mol per mol enzyme; required for activity
pyridoxal 5'-phosphate
-
loosely bound; required for activity
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per subunit
pyridoxal 5'-phosphate
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
0.05 mM, 45% inhibition, 5 mM, complete inhibition
AgNO3
-
strong inhibition
Aminooxyacetate
-
1 mM, complete inhibition
Aminooxyacetate
-
competitive inhibition
Aminooxyacetate
Q56YA5
reacts with the carbonyl group of pyridoxal phosphate, 88% inhibition at 0.01 mM
ammonium acetate
-
0.1 mM, 42% inhibition, 10 mM, complete inhibition
beta-chloro-L-alanine
Q56YA5
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
D-serine
-
competitive inhibition
D-serine
-
competitive inhibition with L-serine
formaldehyde
-
glyoxylate protects
glycine
-
competitive vs. L-serine
glyoxylate
-
competitive vs. pyruvate
glyoxylate
-
irreversible inhibition only in the presence of NH4+, inactivation in the absence of amino acid substrates
glyoxylate
-
amino acid substrates partially protect
glyoxylate
-
presence of D-serine protects against inhibition
glyoxylate
-
inhibited by glyoxylate above 6 mM
HgCl2
-
strong inhibition
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
hydroxylamine
-
0.1 mM, 70% 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
N-ethylmaleimide
-
1 mM, 41% inhibition
N-ethylmaleimide
-
-
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
oxalate
-
competitive vs. 2-oxomalonate, uncompetitive vs. L-serine
p-chloromercuribenzoate
-
1 mM, 37% inhibition
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
weak but significant inhibition
p-hydroxymercuribenzoate
Q56YA5
the 24.1% decrease in enzyme activity achieved using 1.0 mM inhibitor might be considered to be unspecific
Penicillamine
-
weak inhibition
phenylhydrazine
-
weak inhibition
pyruvate
-
competitive vs. glyoxylate
SH-group inhibitor
-
-
-
MgCl2
-
weak inhibition
additional information
-
not inhibited with or without NH4+ by oxalate, formate, acetaldehyde, pyruvate, hydroxypyruvate, 2-oxoglutarate
-
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 by 5,5'-dithio-bis(2-nitrobenzoate)
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.13
-
2-Oxomalonate
-
pH 8.0
0.63
-
3-hydroxypyruvate
-
pH 8.0, 30C, cosubstrate L-alanine
1.1
-
3-hydroxypyruvate
-
pH 8.0, 30C, cosubstrate glycine
0.59
-
glycine
-
cosubstrate glyoxylate, pH 8.0, 30C
1.25
-
glycine
Q56YA5
at 05 mM pyruvate
1.58
-
glycine
-
cosubstrate 3-hydroxypyruvate, pH 8.0, 30C
2.83
-
glycine
Q56YA5
at 0.5 mM hydroxypyruvate
11
-
glycine
-
pH 8.0, 30C
0.5
-
glyoxalate
Q56YA5
at 30 mM L-alanine
0.15
-
glyoxylate
-
pH 7.0, 27C
0.23
-
glyoxylate
-
pH 7.0, 30C
0.6
-
glyoxylate
-
pH 8.0, 30C, cosubstrate L-serine
0.68
-
glyoxylate
-
recombinant enzyme
0.91
-
glyoxylate
Q56YA5
at 30 mM serine
4.6
-
glyoxylate
-
pH 8.1, 30C, cosubstrate L-serine
0.57
-
Hydroxypyruvate
Q56YA5
at 15.4 mM glycine
0.58
-
L-alanine
Q56YA5
at 0.5 mM glyoxylate
0.87
-
L-alanine
-
cosubstrate glyoxylate, pH 8.0, 30C
1.08
-
L-alanine
-
cosubstrate 3-hydroxypyruvate, pH 8.0, 30C
1.25
-
L-alanine
Q56YA5
at 10 mM glyoxylate
20
-
L-alanine
-
pH 8.0, 30C
2.82
-
L-asparagine
-
cosubstrate glyoxylate, pH 8.0, 30C
3.9
-
L-asparagine
-
pH 8.1, 30C, cosubstrate glyoxylate
4.5
-
L-asparagine
-
pH 8.1, 30C, cosubstrate pyruvate
8.41
-
L-asparagine
-
cosubstrate 3-hydroxypyruvate, pH 8.0, 30C
0.28
-
L-serine
-
pH 8.0
0.39
-
L-serine
-
cosubstrate pyruvate
0.5
-
L-serine
-
pH 8.1, 30C, cosubstrate pyruvate
0.6
-
L-serine
-
pH 8.1, 30C, cosubstrate glyoxylate
0.71
-
L-serine
-
pH 8.0, 30C, cosubstrate glyoxylate
0.99
-
L-serine
-
cosubstrate 3-hydroxypyruvate, pH 8.0, 30C
1.53
-
L-serine
Q56YA5
at 0.5 mM glyoxylate
2.4
-
L-serine
-
-
2.47
-
L-serine
-
cosubstrate glyoxylate, pH 8.0, 30C
2.7
-
L-serine
-
pH 7.0, 27C
3.86
-
L-serine
-
recombinant enzyme
0.22
-
pyruvate
Q56YA5
at 15.4 mM glycine
2
-
pyruvate
-
pH 8.1, 30C, cosubstrate L-serine
2.5
-
pyruvate
-
pH 8.1, 30C, cosubstrates: L-asparagine, glyoxylate, L-asparagine
5
-
L-serine
Q56YA5
at 10 mM glyoxylate
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.86
-
L-alanine
Q56YA5
at 10 mM glyoxylate
6.4
-
L-serine
Q56YA5
at 10 mM glyoxylate
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00012
-
Aminooxyacetate
-
-
0.0036
-
beta-chloroalanine
-
pH 8.0
1.6
-
D-serine
-
-
33
-
glycine
-
pH 7.0, 27C
0.4
-
glyoxylate
-
pH 8.1, 30C
45
-
L-alanine
-
pH 7.0, 27C
3
-
L-asparagine
-
pH 8.1, 30C
0.12
-
L-serine
-
pH 8.1, 30C
0.27
-
oxalate
-
pH 8.0
25
-
pyruvate
-
pH 8.1, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
34.4
-
-
-
39.3
-
-
-
53.2
-
-
-
72
-
-
recombinant enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.1
-
-
-
8.5
-
-
substrates L-alanine and 3-hydroxypyruvate
9
-
-
substrates glycine and 3-hydroxypyruvate
9.2
-
Q56YA5
-
additional information
-
-
pI: 6.9
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
approx. 60% of maximal activity at pH 6, approx. half-maximal activity at pH 9
7
-
-
gradual decrease in activity above
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
43880
-
-
calculated from amino acid sequence
45000
-
-
gel filtration, Mes buffer pH 6.5
47700
-
-
estimated from amino acid sequence
79000
-
-
gel filtration, Mes buffer pH 6.5
82400
-
Q56YA5
gel filtration
85000
91200
-
gel filtration
88000
-
-
gel filtration, phosphate buffer pH 7.0
105000
-
-
gel filtration
105000
-
-
gel filtration, phosphate buffer pH 7.0
140000
-
-
HPLC, gel filtration
150000
-
-
Sephacryl S-200, gel filtration
170000
-
-
gel filtration, purification reduces molecular weight to 62000 Da
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 45000, pH value above 7.0, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
Q56YA5
2 * 39800, SDS-PAGE
monomer
-
1 * 45000, pH value below 7.0, SDS-PAGE
oligomer
-
x * 45000 + x * 47000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 40000, recombinant enzyme, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
11
-
stable for 30 min at 30C
6.5
9.1
-
stable, no dissociation of dimer
6.5
-
-
about 50% dimer, 50% monomer in solution
9.1
-
-
1 mM Tris/glycine, about 60% dimer, 40% monomer in solution; 50 mM Tris/glycine, about 87% dimer, 13% monomer
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
and below, 30 min stable
40
-
-
30 min, 16% loss of activity
45
-
-
52% loss of activity after 30 min
50
-
-
30 min, 93% loss of activity
55
-
-
30 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
imidazole decreases stability
-
sucrose, pyridoxal phosphate or 2-mercaptoethanol stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 mM phosphate buffer pH 7, 0.1 mM pyridoxal phosphate, 0.1 mM dithiothreitol, 45% v/v glycerol, at least 5 months
-
-10C, 2 months
-
5C, 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
-
-18C, 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
polyethyleneimine, ammonium sulfate, Ultrogel AcA 34, DEAE-cellulose, isoenzymes A and B
-
ammonium sulfate, DEAE-Sephacel, phenyl-Sepharose, CM-toyopearl, Cellulofine
-
Ni-NTA column chromatography
-
recombinant enzyme
-
ammonium sulfate, agarose A-15, chromatofocusing, partial purification
-
DEAE-cellulose, agarose gel, Brushite, Sephadex g-200, partial purification
-
pH 5.4, polyethylene glycol 6000, DEAE-Sephadex A25, Sephacryl S-300, partial purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expressed in Escherichia coli strain HB101
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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