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Information on EC 2.6.1.44 - alanine-glyoxylate transaminase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P43567

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.44 alanine-glyoxylate transaminase
IUBMB Comments
A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine---pyruvate transaminase.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P43567
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
agxt2, alanine-glyoxylate aminotransferase, alanine glyoxylate aminotransferase, spt/agt, alanine-glyoxylate aminotransferase 2, alanine:glyoxylate aminotransferase 1, agt-mi, alanine:2-oxoglutarate aminotransferase, serine pyruvate aminotransferase, cytosolic alanine aminotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AGT
-
-
-
-
alanine-glyoxylate aminotransferase
-
-
-
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alanine-glyoxylic aminotransferase
-
-
-
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alanine:glyoxylate aminotransferase
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-
L-alanine-glycine transaminase
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-
-
-
L-alanine-glyoxylate aminotransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-alanine:glyoxylate aminotransferase
A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine---pyruvate transaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
9015-67-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
additional information
?
-
-
utilizes only glyoxylate as amino acceptor, hydroxypyruvate, 2-oxoglutarate, phenylpyruvate and 2-oxo-4-methyl-thiobutyrate are inactive, only L-alanine as amino donor, L-serine, L-threonine, L-glutamic acid, L-glutamine, L-aspartic acid, L-asparagine, L-ornithine, L-leucine, L-valine, L-isoleucine, L-histidine, L-phenylalanine, L-tryptophan and L-tyrosine are no substrates
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amino-oxyacetic acid
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-
hydroxylamine
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Isonicotinic acid hydrazide
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Semicarbazide
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
glyoxylate
pH 8.0, 37°C
2.26
L-alanine
pH 8.0, 37°C
0.7
glyoxylate
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pH 8.2, 37°C, isoenzyme 2, alanine as amino donor
2.1
L-alanine
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pH 8.2, 37°C, glyoxylate as amino acceptor
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
isoelectric focusing of the crude extract on a pH 3.0-10 pharmalyte gradient, 3 activity peaks with pI 7.4, 7.8 and 8.3
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
2 * 40000, SDS-PAGE
80000
-
sucrose-density-gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystallization data
dimer
-
2 * 40000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM-potassium phosphate buffer, pH 7.5, containing 100 mM NaCl, 0.1 mM pyridoxal 5'-phosphate and 10% glycerol, my be stored for at least 3 months without loss of activity
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0-4°C, little or no activity is lost when stored for 2 weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Ashbya gossypii strain ATCC10895
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
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overexpression of enzyme in Ashbya gossypii, use for production of riboflavin for human and animal feed supplement
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takada, Y.; Noguchi, T.
Characteristics of alanine: glyoxylate aminotransferase from Saccharomyces cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates
Biochem. J.
231
157-163
1985
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kato, T.; Park, E.Y.
Expression of alanine:glyoxylate aminotransferase gene from Saccharomyces cerevisiae in Ashbya gossypii
Appl. Microbiol. Biotechnol.
71
46-52
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Meyer, P.; Liger, D.; Leulliot, N.; Quevillon-Cheruel, S.; Zhou, C.Z.; Borel, F.; Ferrer, J.L.; Poupon, A.; Janin, J.; van Tilbeurgh, H.
Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein
Biochimie
87
1041-1047
2005
Saccharomyces cerevisiae (P43567), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Schlosser, T.; Gatgens, C.; Weber, U.; Stahmann, K.P.
Alanine:glyoxylate aminotransferase of Saccharomyces cerevisiae-encoding gene AGX1 and metabolic significance
Yeast
21
63-73
2004
Saccharomyces cerevisiae (P43567), Saccharomyces cerevisiae
Manually annotated by BRENDA team