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Information on EC 2.6.1.44 - alanine-glyoxylate transaminase and Organism(s) Mus musculus and UniProt Accession Q3UEG6

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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:
Mus musculus
UNIPROT: Q3UEG6
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The taxonomic range for the selected organisms is: Mus musculus
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
alanine glyoxalate transaminase 2
-
alanine-glyoxylate aminotransferase-2
-
AGT
-
-
-
-
AGXT2
-
-
alanine-glyoxylate aminotransferase
-
-
-
-
alanine-glyoxylic aminotransferase
-
-
-
-
L-alanine-glycine transaminase
-
-
-
-
L-alanine-glyoxylate aminotransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
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
-
-
-
r
Nomega,Nomega-dimethyl-L-arginine + pyruvate
5-(N,N-dimethylcarbamidamido)-2-oxopentanoate + alanine
show the reaction diagram
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
L-alanine + hydroxypyruvate
pyruvate + L-serine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-isoleucine + glyoxylate
3-methyl-2-oxopropanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-leucine + glyoxylate
4-methyl-2-oxopentanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-valine + glyoxylate
3-methyl-2-oxobutanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
additional information
?
-
-
isoenzyme 1, little or no activity with 2-oxoglutarate as amino acceptor and alanine, serine, glutamic acid, isoleucine, methionine, glutamine, asparagine, valine, aspartic acid, leucine, phenylalanine, tyrosine, histidine, tryptophan or 5-hydroxytryptophan
-
-
?
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
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroxylamine
Isonicotinic acid hydrazide
-
isoenzyme 1 and isoenzyme 2
Semicarbazide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glucagon
-
induced by, isoenzyme 1 is increased in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.72
glyoxylate
1.4 - 25
L-alanine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23.2
-
isoenzyme 1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1 - 8.4
-
isoenzyme 2
8.3 - 8.6
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
-
isoelectric focusing on a pH 3.5-10 ampholine gradient
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AGT2_MOUSE
513
0
57115
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
2 * 38000, isoenzyme 1, SDS-PAGE
77000
-
-
80000
-
sucrose-density-gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 38000, isoenzyme 1, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 4 weeks without loss of either activity
-
0-6°C, 50 mM potassium phosphate buffer, pH 7.5, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 2 weeks with little loss of either activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoenzyme 1 and 2
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
used in knockout experiments
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
infusion of asymmetric dimethylarginines causes a 3- to 4fold increase in plasma and urine asymmetric dimethylarginine levels and a 2- to 3fold increase in plasma and urine levels of the asymmetric dimethylarginine-specific metabolite of AGXT2, alpha-keto-delTA-(N,N-dimethylguanidino)valeric acid. Plasma levels of alpha-keto-delTA-(N,N-dimethylguanidino)valeric acid are elevated 32fold in the mice, which underwent bilateral nephrectomy. Neither bilateral nephrectomy nor asymmetric dimethylarginine infusion causes upregulation of AGXT2 expression or activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noguchi, T.; Okuno, E.; Takada, Y.; Minatogawa, Y.; Okai, K.; Kido, R.
Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species
Biochem. J.
169
113-122
1978
Canis lupus familiaris, Felis catus, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Caplin, B.; Wang, Z.; Slaviero, A.; Tomlinson, J.; Dowsett, L.; Delahaye, M.; Salama, A.; Salama, A.; Wheeler, D.C.; Leiper, J.
Alanine-glyoxylate aminotransferase-2 metabolizes endogenous methylarginines, regulates NO, and controls blood pressure
Arterioscler. Thromb. Vasc. Biol.
32
2892-2900
2012
Mus musculus (Q3UEG6)
Manually annotated by BRENDA team
Rodionov, R.N.; Martens-Lobenhoffer, J.; Brilloff, S.; Hohenstein, B.; Jarzebska, N.; Jabs, N.; Kittel, A.; Maas, R.; Weiss, N.; Bode-Bger, S.M.
Role of alanine:glyoxylate aminotransferase 2 in metabolism of asymmetric dimethylarginine in the settings of asymmetric dimethylarginine overload and bilateral nephrectomy
Nephrol. Dial. Transplant.
29
2035-2042
2014
Mus musculus
Manually annotated by BRENDA team
Han, Q.; Yang, C.; Lu, J.; Zhang, Y.; Li, J.
Metabolism of oxalate in humans a potential role kynurenine aminotransferase/glutamine transaminase/cysteine conjugate beta-lyase plays in hyperoxaluria
Curr. Med. Chem.
26
4944-4963
2019
Mus musculus (Q3UEG6), Homo sapiens (Q9BYV1)
Manually annotated by BRENDA team