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Information on EC 2.6.1.44 - alanine-glyoxylate transaminase and Organism(s) Homo sapiens and UniProt Accession P21549

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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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Homo sapiens
UNIPROT: P21549
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The taxonomic range for the selected organisms is: Homo sapiens
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-Ma
major allele of alanine:glyoxylate aminotransferase
AGT-Mi
minor allele of alanine:glyoxylate aminotransferase
alanine glyoxylate aminotransferase
-
alanine-glyoxylate aminotransferase
-
alanine: glyoxylate aminotransferase
-
alanine:glyoxylate aminotransferase
-
AGT1
-
-
AGXT
-
-
AGXT2
alanine glyoxalate transaminase 2
-
alanine glyoxylate aminotransferase
-
-
alanine-glyoxalate transaminase 1
-
-
alanine-glyoxylate aminotransferase
alanine-glyoxylate aminotransferase 2
-
-
alanine-glyoxylic aminotransferase
-
-
-
-
alanine:glyoxylate aminotransferase
alanine:glyoxylate aminotransferase 2
-
alanine:glyoxylate aminotransferase type 1
-
-
L-alanine-glycine transaminase
-
-
-
-
L-alanine-glyoxylate aminotransferase
-
-
-
-
additional information
see also EC 2.6.1.51
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-alanine + glyoxylate = pyruvate + glycine
show the reaction diagram
pyridoxamine 5'-phosphate remains bound to the enzyme during the catalytic cycle. The enzyme-pyridoxamine 5'-phosphate complex displays a reactivity towards oxo acids higher than that of the apo-enzyme in presence of pyridoxamine
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
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
show the reaction diagram
-
enzyme catalyzes both beta-elimination and half-transamination of L-cysteine together with pyruvate transamination via a ketimine common intermediate. L-cysteine partitions between the two reactions with a ratio of 2.5
-
?
glycine + pyruvate
L-alanine + glyoxylate
show the reaction diagram
-
-
-
?
L-alanine + glyoxylate
glycine + pyruvate
show the reaction diagram
transamination half-reaction kinetic parameters
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
show the reaction diagram
-
-
-
?
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
show the reaction diagram
-
-
-
?
L-glutamate + glyoxylate
2-oxoglutarate + glycine
show the reaction diagram
-
-
-
?
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
show the reaction diagram
-
-
-
?
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
-
-
-
?
additional information
?
-
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
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aminooxyacetic acid
-
D-cycloserine
DCS, commercialized as Seromycin, a reversible inhibitor of AGT. DCS displays a time-dependent binding mainly generating an oxime intermediate, inhibition mechanism, overview
L-Cycloserine
LCS, a reversible inhibitor of AGT. LCS undergoes half-transamination generating a ketimine intermediate and behaves as a classical competitive inhibitor, inhibition mechanism, overview
amino-oxyacetic acid
D-alanine
pyruvate
additional information
the cycloserine enantiomers are reversible inhibitors of human alanine:glyoxylate aminotransferase. DCS, but not LCS, is able to promote the correct folding of the G41R variant, as revealed by its increased specific activity and expression as a soluble protein. This effect also translates into an increased glyoxylate detoxification ability of cells expressing the variant upon treatment with DCS. DCS might play a role as pharmacological chaperone. Inhibitor docking study and mass spectrometric analysis, identification of the wild-type and mutant AGT-cycloserine reaction products. Inhibitor effects on recombinant wild-type AGT and the G41R variant in CHO-GO cells, that overexpress glycolate oxidase, overview. Cell survival of CHO-GO-AGT-wild-type cells is much higher than that of CHO-GO-AGT-G41R mutant cells
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aminooxyacetic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038 - 1
glyoxylate
28 - 84
L-alanine
1
L-cysteine
pH 7.4, Km value of L-cysteine is decreased by 40fold and 200fold in comparison with those of L-alanine and L-serine
22
glycine
0.13 - 2.5
glyoxylate
9.1 - 42
L-alanine
0.21
pyruvate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19 - 45
glyoxylate
0.147 - 45
L-alanine
0.22
L-cysteine
pH 7.4
0.33
glycine
0.068 - 45
glyoxylate
0.07 - 45
L-alanine
0.36
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
23 - 196
glyoxylate
0.24 - 1.45
L-alanine
0.45 - 196
glyoxylate
0.005 - 1.4
L-alanine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.3 - 28.7
D-alanine
2.3 - 22.8
pyruvate
additional information
additional information
inhibition kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51.8
-
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
recombinant enzyme
7.8 - 8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.2
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
very low content
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AGT1_HUMAN
392
0
43010
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42700
-
about 42700 Da, SDS-PAGE
43000
48600
-
SDS-PAGE
52000
-
FLAG-tagged enzyme, SDS-PAGE
90000
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer or dimer
the enzyme displays a a dimer-monomer equilibrium
dimer
homodimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant S187F, to a resolution of 2.9 A. The overall conformation of the variant is similar to that of normal AGTwith a displacement of the PLP-binding Lys209 and Val185, located on the re and si side of PLP, respectively, and slight conformational changes of other active site residues, in particular Trp108, the base stacking residue with the pyridine cofactor moiety. This results in a mispositioning of the AGT-pyridoxamine 5'-phosphate complex and of the external aldimine
purified recombinant wild-type enzyme in complex with inhibitors L- and D-cycloserine (LCS and DCS), hanging drop vapor diffusion technique, mixing of 0.001 ml of protein/ligand solution containing 0.215 mM enzyme, 2 mM DCS, and 50 mM potassium phosphate, pH 7.4, with an equal volume of reservoir solution containing 10-12% PEG 6000, 5% 2-methyl-2,4-pentanediol (MPD), and 0.1 M MES, pH 6.5, single crystals are cryoprotected by fast soaking into a reservoir solution containing 2 mM DCS and 25% MPD, for the AGT-LCS complex, AGT native crystals grown in the described conditions, with the exception of DCS, are soaked into a solution containing the reservoir and 20 mM LCS and 20% MPD, X-ray diffraction structure determination and analysis at 2.7-3.0 A resolution, modelling
using 10% (w/v) PEG 4000 in 0.1 M Na HEPES pH 7.5
crystals belong to space group P4(1)2(1)2 or its enantiomorph with uni-cell parameters a = b = 90.81, c = 142.62 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A280V
natural mutant from patient with primary hyperoxaluria type 1, 92% of normal enzyme activity
F152A
the mutant shows decreased activity compared to the wild type enzyme
F152I
the mutation is associated with primary hyperoxaluria type 1 in combination with the minor AGT allele and shows decreased activity compared to the wild type enzyme
F238S
site-directed mutagenesis
F240S
site-directed mutagenesis
G161R
natural mutant from patient with primary hyperoxaluria type 1, 6.2% of normal enzyme activity
G170R
the mutant shows decrease in protein stability
G216R
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure, it also shows a strongly reduced catalytic efficiency
G41R
the naturally occuring missense mutation causes AGT misfolding, which induces aggregation and proteolytic degradation. Enzyme inhibitor D-cycloserin significantly improves the glyoxylate detoxification ability of CHO-GO cells expressing the enzyme mutant G41R variant, because it increases cell viability upon glycolate treatment. These data confirm that the treatment increases the amount of intraperoxisomal functional AGT able to metabolize glyoxylate
G42E
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure
G63R
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure
I279T
natural mutant from patient with primary hyperoxaluria type 1, 98% of normal enzyme activity
P11L
naturally occuring polymorphic mutation
P11L/I56N
site-directed mutagenesis, the Ile56Asn mutation induces a structural defect mostly related to the apo-form of enzyme AGT. The effects are more pronounced when the substitution of Ile56 is combined with the Pro11Leu and, at higher degree, the Pro11Arg mutation
P11R
naturally occuring pathogenic mutation
P11R/I56N
site-directed mutagenesis, the Ile56Asn mutation induces a structural defect mostly related to the apo-form of enzyme AGT. The effects are more pronounced when the substitution of Ile56 is combined with the Pro11Leu and, at higher degree, the Pro11Arg mutation
R118A
site-directed mutagenesis
R118A/F238S/F240S
site-directed mutagenesis, the apo and the holo forms of the triple mutant R118A-Mi/F238S-Mi/F240S-Mi display a dimer-monomer equilibrium dissociation constant value at least about 260 and 31fold larger, respectively, than the corresponding ones of wild-type AGT-Mi. In the presence of cofactor pyridoxala 5'-phosphate (PLP), the apo-monomer of the triple mutant undergoes a biphasic process: the fast phase represents the formation of an inactive PLP-bound monomer, while the slow phase depicts the monomer-monomer association that parallels the regain of transaminase activity. The latter events occur with a rate constant of about 20 nM/min. In the absence of PLP, the apomonomer is also able to dimerize but with a rate constant value about 2700fold lower. Kinetics of dimerization of triple variant, overview
R36H
site-directed mutagenesis, the mutant displays structural alterations mainly related to the apoform and consisting of an altered tertiary and quaternary structure
S187F
mutation gives rise to a variant associated with primary hyperoxaluria type I. Mutation shows a 300- to 500fold decrease in both the rate constant of L-alanine half-transamination and the kcat of the overall transamination, a different pyridoxamine 5'-phosphate binding mode and affinity, and a different microenvironment of the external aldimine
S218L
natural mutant from patient with primary hyperoxaluria type 1, 10% of normal enzyme activity
A112D
-
less than 5% of the specific activity of the wild type enzyme
C173Y
-
less than 5% of the specific activity of the wild type enzyme
D183N
-
less than 5% of the specific activity of the wild type enzyme
DELTA 1-21
-
purified protein does not show bound PLP (affinity is about 80fold lower than wild type protein), catalytic activity about 1000fold lower than wild type protein, expressed in Escherichia coli in an insoluble form, peroxisomal localization, expressed in CHO cells the mutant protein forms large stable but catalytically inactive aggregates in the peroxisomes
F152I
G156R
-
less than 5% of the specific activity of the wild type enzyme
G161C
-
5% of wild-type expression level, reduced catalytic activity
G161R
G161S
-
12% of wild-type expression level, reduced catalytic activity
G170R
I244T
-
natural mutation in enzyme minor allele, 8-26% of the activity of major allele, in vitro
I340M
-
polymorphism associated with enzyme from minor allele, significantly higher Km-value than that for major allele, 90% of activity of enzyme from major allele
K209R
-
less than 5% of the specific activity of the wild type enzyme
P10L/P11L
-
Kcat value 56% of wild type protein, aggregation occuring at a slower rate than that of DELTA 1-21 protein
P11L/F152I/I340M
-
naturally occuring mutations, mistargeted to the mitochondria, forms dimers, catlytically active
P11L/G170R/I340M
-
naturally occuring mutations, creates a hidden N-terminal mitochondrial targeting sequence, the unmasking of which occurs in the hereditary calcium oxalate kidney stone disease primary hyperoxaluria type 1; this unmasking is due to the additional presence of a common disease-specific G170R mutation, forms dimers, catalytically active
P11L/G41R/I340M
-
naturally occuring mutations, mistargeted to the mitochondria, catalytically inactive, aggregates
P11L/I244T/I340M
-
naturally occuring mutations, mistargeted to the mitochondria, forms dimers, catlytically active
P11L/I340M
P11L/I340M/F152I
-
naturally occuring mutation, possibly mistargeting into mitochondrial matrix
P11L/I340M/G170R
-
naturally occuring mutations, pathogenic variant
P11L/I340M/G41R
-
naturally occuring mutation, predicted to be responsible for the depletion of immunoreactive enzyme protein and formation of intraperoxisomal aggregates
R233C
S158L
-
natural mutation in enzyme major allele, no in vitro enzymic activity
S187F
-
less than 5% of the specific activity of the wild type enzyme
S205P
S218L
-
less than 5% of the specific activity of the wild type enzyme
V336D
W108R
-
less than 5% of the specific activity of the wild type enzyme
W251K
naturally occuring mutation, mutant protein localized in peroxisome and cytosol
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70.1
the melting temperature of the minor allele holoenzyme is at 70.1°C
76.3
the melting temperature of the major allele holoenzyme is at 76.3°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
human AGT can substitute for function of yeast Agx1 (Yeast alanine:glyoxylate aminotransferase) and that mutations associated with disease in humans show reduced growth in yeast. The reduced growth of minor allele mutants reflects reduced protein levels, indicating that these proteins are less stable than wild-type AGT in yeast
-
major allele (P11/I340) is more stable against increasing urea concentrations than minor allele (P11L/I340M) or mutant protein P11L/I340M/G170R
-
partial digestion by trypsin provides an indicator of proper folding of the enzyme, while for some mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid
-
partial trypsin digestion provides an indicator of proper folding of the mutant enzyme. For selected mutations the sensitivity to trypsin can be ameliorated by addition of pyridoxal phosphate or aminooxy acetic acid as specific pharmacological chaperones
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, wild-type and mutant enzyme G82E are stable for at least 1 month
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-resin affinity chromatography, gel filtration
recombinant enzyme
-
recombinant wild-type and G82E mutant His-tagged enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
gene AGT, recombinant expression of wild-type and mutant G41R enzymes in Escherichia coli strain BL21, recombinant expression of wild-type AGT and the G41R variant in CHO-GO cells, that overexpress glycolate oxidase
gene AGXT, quantitative real-time reverse transcription-PCR enzyme expression analysis
gene AGXT, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
gene AGXT, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
AGXT cDNA cloned, AGXT*LTM expressed as a GST-fusion protein in Escherichia coli BL21(RIL) and in Sf9 cells
-
cloned and expressed in Escherichia coli JM109
-
expressed in COS-1a cells
-
expressed in COS-7 cells and human umbilical vein endothelial cells with a C-terminal FLAG epitope tag
-
expressed in Escherichia coli
-
expressed in Mus musculus embryonic stem cells
-
expressed in stably transformed CHO cells
-
expression in CHO cell
-
expression in Escherichia coli
expression in HeLa cell
-
expression of of untagged alanine-glyoxylate aminotransferase in Escherichia coli
-
expression vectors of the enhanced green fluorescent protein-tagged alanine:glyoxylate aminotransferase and deletion mutants are introduced into HeLa cells to identify the peroxisomal targeting signal of the alanine:glyoxylate aminotransferase
-
for sequence determination, GFP-fusion proteins used in localization experiments
gene AGXT2, real-time RT-PCR enzyme expression analysis
His-tagged protein expressed in Escherichia coli JM109, expressed in CHO cells
-
human AGT can substitute for function of yeast Agx1 (yeast alanine:glyoxylate aminotransferase) and that mutations associated with disease in humans show reduced growth in yeast. The reduced growth of minor allele mutants reflects reduced protein levels, indicating that these proteins are less stable than wild-type AGT in yeast
-
human AGT expressed in Escherichia coli B834(DE3)
-
mammalian expression vector pHYK, expressed in COS-1 cells
-
wild-type and G82E mutant His-tagged enzyme expressed in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation of enzyme with guanidine-HCl and re-folding, complete renaturation. Mutations G41V and G41R, associated with primary hyperoxaluria type I, show enhanced activity after re-folding. Pyridoxal 5’-phosphate is not required for proper re-folding
-
quick dilution (100fold) to an urea concentration that would be expected to support native enzyme, only about 20 and 5% of activity is recovered for major allele (P11/I340) and P11L/I340M (minor allele, respectively)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
loss of AGXT expression is correlated with a poor prognosis and differentiation of hepatocellular carcinoma (HCC)
analysis
-
development of an indirect glycolate cytotoxicity assay using CHO cells expressing glycolate oxidase and various normal and mutant forms of AGT
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Danpure, C.J.; Fryer, P.; Griffiths, S.; Guttridge, K.M.; Jennings, P.R.; Allsop, J.; Moser, A.B.; Naidu, S.; Moser, H.W.; et al.
Cytosolic compartmentalization of hepatic alanine:glyoxylate aminotransferase in patients with aberrant peroxisomal biogenesis and its effect on oxalate metabolism
J. Inherit. Metab. Dis.
17
27-40
1994
Homo sapiens
Manually annotated by BRENDA team
Horvath, V.A.P.; Wanders, R.J.A.
Aminooxy acetic acid: a selective inhibitor of alanine:glyoxylate aminotransferase and its use in the diagnosis of primary hyperoxaluria type I
Clin. Chim. Acta
243
105-114
1995
Homo sapiens
Manually annotated by BRENDA team
Leiper, J.M.; Oatey, P.B.; Danpure, C.J.
Inhibition of alanine:glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1
J. Cell. Biol.
135
939-951
1996
Homo sapiens
Manually annotated by BRENDA team
Rumsby, G.; Weir, T.; Samuell, C.T.
A semiautomated alanine:glyoxylate aminotransferase assay for the tissue diagnosis of primary hyperoxaluria type 1
Ann. Clin. Biochem.
34
400-404
1997
Homo sapiens
-
Manually annotated by BRENDA team
Holbrook, J.D.; Birdsey, G.M.; Yang, Z.; Bruford, M.W.; Danpure, C.J.
Molecular adaptation of alanine: glyoxylate aminotransferase targeting in primates
Mol. Biol. Evol.
17
387-400
2000
Mico argentatus, Callithrix jacchus, Cheirogaleus medius, Homo sapiens, Macaca fuscata, Eulemur fulvus, Loris tardigradus, Nycticebus pygmaeus, Pongo pygmaeus, Saguinus oedipus, Papio anubis (Q9TSP4), Saimiri sciureus (Q9TTP0), Pan troglodytes (Q9TTP2), Pithecia pithecia (Q9TTP3), Macaca nigra (Q9TTP7), Leontopithecus rosalia (Q9TTP8), Hylobates lar (Q9TTP9), Gorilla gorilla (Q9TTQ0), Callimico goeldii (Q9TTQ8), Cercopithecus diana (Q9TTR4), Ateles paniscus (Q9TTS7)
Manually annotated by BRENDA team
Lumb, M.J.; Danpure, C.J.
Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations
J. Biol. Chem.
275
36415-36422
2000
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Roe, S.M.; Pearl, L.H.; Danpure, C.J.
Crystallization and preliminary crystallographic analysis of human alanine:glyoxylate aminotransferase and its polymorphic variants
Acta Crystallogr. Sect. D
57
1936-1937
2001
Homo sapiens
Manually annotated by BRENDA team
Danpure, C.J.; Lumb, M.J.; Birdsey, G.M.; Zhang, X.
Alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting in human hereditary kidney stone disease
Biochim. Biophys. Acta
1647
70-75
2003
Homo sapiens
Manually annotated by BRENDA team
Santana, A.; Salido, E.; Torres, A.; Shapiro, L.J.
Primary hyperoxaluria type 1 in the Canary Islands: A conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase
Proc. Natl. Acad. Sci. USA
100
7277-7282
2003
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Roe, S.M.; Hou, Y.; Bartlam, M.; Rao, Z.; Pearl, L.H.; Danpure, C.J.
Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1
J. Mol. Biol.
331
643-652
2003
Homo sapiens
Manually annotated by BRENDA team
Coulter-Mackie, M.B.; Lian, Q.; Applegarth, D.; Toone, J.
The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1
Mol. Genet. Metab.
86
172-178
2005
Homo sapiens (P21549), Homo sapiens
Manually annotated by BRENDA team
Coulter-Mackie, M.B.; Lian, Q.; Wong, S.G.
Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor
Protein Expr. Purif.
41
18-26
2005
Homo sapiens
Manually annotated by BRENDA team
Koul, S.; Johnson, T.; Pramanik, S.; Koul, H.
Cellular transfection to deliver alanine-glyoxylate aminotransferase to hepatocytes: a rational gene therapy for primary hyperoxaluria-1 (PH-1)
Am. J. Nephrol.
25
176-182
2005
Homo sapiens
Manually annotated by BRENDA team
Huber, P.A.; Birdsey, G.M.; Lumb, M.J.; Prowse, D.T.; Perkins, T.J.; Knight, D.R.; Danpure, C.J.
Peroxisomal import of human alanine:glyoxylate aminotransferase requires ancillary targeting information remote from its C terminus
J. Biol. Chem.
280
27111-27120
2005
Homo sapiens
Manually annotated by BRENDA team
Coulter-Mackie, M.B.; Lian, Q.
Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations
Mol. Genet. Metab.
89
349-359
2006
Homo sapiens
Manually annotated by BRENDA team
Salido, E.C.; Li, X.M.; Lu, Y.; Wang, X.; Santana, A.; Roy-Chowdhury, N.; Torres, A.; Shapiro, L.J.; Roy-Chowdhury, J.
Alanine-glyoxylate aminotransferase-deficient mice, a model for primary hyperoxaluria that responds to adenoviral gene transfer
Proc. Natl. Acad. Sci. USA
103
18249-18254
2006
Homo sapiens
Manually annotated by BRENDA team
Cellini, B.; Bertoldi, M.; Montioli, R.; Paiardini, A.; Borri Voltattorni, C.
Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications
Biochem. J.
408
39-50
2007
Homo sapiens, Homo sapiens (A2V838)
Manually annotated by BRENDA team
Bertoldi, M.; Cellini, B.; Paiardini, A.; Montioli, R.; Borri Voltattorni, C.
Reactions of human liver peroxisomal alanine:glyoxylate aminotransferase with beta -chloro-L-alanine and L-cysteine: Spectroscopic and kinetic analysis
Biochim. Biophys. Acta
1784
1356-1362
2008
Homo sapiens (P21549)
Manually annotated by BRENDA team
Ikeda, M.; Kanouchi, H.; Minatogawa, Y.
Characterization of peroxisomal targeting signals on alanine: glyoxylate aminotransferase
Biol. Pharm. Bull.
31
131-134
2008
Homo sapiens
Manually annotated by BRENDA team
Hopper, E.D.; Pittman, A.M.; Fitzgerald, M.C.; Tucker, C.L.
In vivo and in vitro examination of stability of primary hyperoxaluria-associated human alanine:glyoxylate aminotransferase
J. Biol. Chem.
283
30493-30502
2008
Homo sapiens
Manually annotated by BRENDA team
Coulter-Mackie, M.B.; Lian, Q.
Partial trypsin digestion as an indicator of mis-folding of mutant alanine:glyoxylate aminotransferase and chaperone effects of specific ligands. Study of a spectrum of missense mutants
Mol. Genet. Metab.
94
368-374
2008
Homo sapiens
Manually annotated by BRENDA team
Cellini, B.; Montioli, R.; Bianconi, S.; Lopez-Alonso, J.P.; Voltattorni, C.B.
Construction, purification and characterization of untagged human liver alanine-glyoxylate aminotransferase expressed in Escherichia coli
Protein Pept. Lett.
15
153-159
2008
Homo sapiens
Manually annotated by BRENDA team
Djordjevic, S.; Zhang, X.; Bartlam, M.; Ye, S.; Rao, Z.; Danpure, C.J.
Structural implications of a G170R mutation of alanine:glyoxylate aminotransferase that is associated with peroxisome-to-mitochondrion mistargeting
Acta Crystallogr. Sect. F
66
233-236
2010
Homo sapiens (P21549)
Manually annotated by BRENDA team
Cellini, B.; Montioli, R.; Paiardini, A.; Lorenzetto, A.; Voltattorni, C.B.
Molecular insight into the synergism between the minor allele of human liver peroxisomal alanine:glyoxylate aminotransferase and the F152I mutation
J. Biol. Chem.
284
8349-8358
2009
Homo sapiens (P21549), Homo sapiens
Manually annotated by BRENDA team
Rodionov, R.N.; Murry, D.J.; Vaulman, S.F.; Stevens, J.W.; Lentz, S.R.
Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production
J. Biol. Chem.
285
5385-5391
2010
Homo sapiens
Manually annotated by BRENDA team
Cellini, B.; Montioli, R.; Paiardini, A.; Lorenzetto, A.; Maset, F.; Bellini, T.; Oppici, E.; Voltattorni, C.B.
Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I
Proc. Natl. Acad. Sci. USA
107
2896-2901
2010
Homo sapiens
Manually annotated by BRENDA team
Kawai, C.; Minatogawa, Y.; Akiyoshi, H.; Hirose, S.; Suehiro, T.; Tone, S.
A novel mutation of human liver alanine:glyoxylate aminotransferase causes primary hyperoxaluria type 1: immunohistochemical quantification and subcellular distribution
Acta Histochem. Cytochem.
45
121-129
2012
Homo sapiens (A2V838)
Manually annotated by BRENDA team
Cellini, B.; Montioli, R.; Voltattorni, C.B.
Human liver peroxisomal alanine:glyoxylate aminotransferase: characterization of the two allelic forms and their pathogenic variants
Biochim. Biophys. Acta
1814
1577-1584
2011
Homo sapiens
Manually annotated by BRENDA team
Cellini, B.; Lorenzetto, A.; Montioli, R.; Oppici, E.; Voltattorni, C.B.
Human liver peroxisomal alanine:glyoxylate aminotransferase: Different stability under chemical stress of the major allele, the minor allele, and its pathogenic G170R variant
Biochimie
92
1801-1811
2010
Homo sapiens
Manually annotated by BRENDA team
Montioli, R.; Fargue, S.; Lewin, J.; Zamparelli, C.; Danpure, C.J.; Borri Voltattorni, C.; Cellini, B.
The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase
Int. J. Biochem. Cell Biol.
44
536-546
2012
Homo sapiens
Manually annotated by BRENDA team
Fargue, S.; Lewin, J.; Rumsby, G.; Danpure, C.J.
Four of the most common mutations in primary hyperoxaluria type 1 unmask the cryptic mitochondrial targeting sequence of alanine:glyoxylate aminotransferase encoded by the polymorphic minor allele
J. Biol. Chem.
288
2475-2484
2013
Homo sapiens
Manually annotated by BRENDA team
Ichiyama, A.
Studies on a unique organelle localization of a liver enzyme, serine:pyruvate (or alanine:glyoxylate) aminotransferase
Proc. Jpn. Acad. Ser. B Phys. Biol. Sci.
87
274-286
2011
Homo sapiens
Manually annotated by BRENDA team
Oppici, E.; Roncador, A.; Montioli, R.; Bianconi, S.; Cellini, B.
Gly161 mutations associated with Primary Hyperoxaluria Type I induce the cytosolic aggregation and the intracellular degradation of the apo-form of alanine:glyoxylate aminotransferase
Biochim. Biophys. Acta
1832
2277-2288
2013
Homo sapiens
Manually annotated by BRENDA team
Fargue, S.; Knight, J.; Holmes, R.P.; Rumsby, G.; Danpure, C.J.
Effects of alanine:glyoxylate aminotransferase variants and pyridoxine sensitivity on oxalate metabolism in a cell-based cytotoxicity assay
Biochim. Biophys. Acta
1862
1055-1062
2016
Homo sapiens
Manually annotated by BRENDA team
Oppici, E.; Fodor, K.; Paiardini, A.; Williams, C.; Voltattorni, C.B.; Wilmanns, M.; Cellini, B.
Crystal structure of the S187F variant of human liver alanine: glyoxylate [corrected] aminotransferase associated with primary hyperoxaluria type I and its functional implications
Proteins
81
1457-1465
2013
Homo sapiens (P21549)
Manually annotated by BRENDA team
Jarzebska, N.; Georgi, S.; Jabs, N.; Brilloff, S.; Maas, R.; Rodionov, R.N.; Zietz, C.; Montresor, S.; Hohenstein, B.; Weiss, N.
Kidney and liver are the main organs of expression of a key metabolic enzyme alanine glyoxylate aminotransferase 2 in humans
Atheroscler. Suppl.
40
106-112
2019
Homo sapiens (Q9BYV1), Homo sapiens
Manually annotated by BRENDA team
Dindo, M.; Grottelli, S.; Annunziato, G.; Giardina, G.; Pieroni, M.; Pampalone, G.; Faccini, A.; Cutruzzola, F.; Laurino, P.; Costantino, G.; Cellini, B.
Cycloserine enantiomers are reversible inhibitors of human alanine glyoxylate aminotransferase implications for primary hyperoxaluria type 1
Biochem. J.
476
3751-3768
2019
Homo sapiens (P21549)
Manually annotated by BRENDA team
Dindo, M.; Montioli, R.; Busato, M.; Giorgetti, A.; Cellini, B.; Borri Voltattorni, C.
Effects of interface mutations on the dimerization of alanine glyoxylate aminotransferase and implications in the mistargeting of the pathogenic variants F152I and I244T
Biochimie
131
137-148
2016
Homo sapiens (P21549), Homo sapiens
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
Dindo, M.; Oppici, E.; DellOrco, D.; Montone, R.; Cellini, B.
Correlation between the molecular effects of mutations at the dimer interface of alanine-glyoxylate aminotransferase leading to primary hyperoxaluria type I and the cellular response to vitamin B6
J. Inherit. Metab. Dis.
41
263-275
2018
Homo sapiens (P21549)
Manually annotated by BRENDA team
Sun, Y.; Li, W.; Shen, S.; Yang, X.; Lu, B.; Zhang, X.; Lu, P.; Shen, Y.; Ji, J.
Loss of alanine-glyoxylate and serine-pyruvate aminotransferase expression accelerated the progression of hepatocellular carcinoma and predicted poor prognosis
J. Transl. Med.
17
390
2019
Homo sapiens (P21549)
Manually annotated by BRENDA team
Dindo, M.; Mandrile, G.; Conter, C.; Montone, R.; Giachino, D.; Pelle, A.; Costantini, C.; Cellini, B.
The ILE56 mutation on different genetic backgrounds of alanine glyoxylate aminotransferase clinical features and biochemical characterization
Mol. Genet. Metab.
131
171-180
2020
Homo sapiens (P21549)
-
Manually annotated by BRENDA team