Information on EC 2.6.1.44 - alanine-glyoxylate transaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
2.6.1.44
-
RECOMMENDED NAME
GeneOntology No.
alanine-glyoxylate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-alanine + glyoxylate = pyruvate + glycine
show the reaction diagram
A pyridoxal-phosphate protein; A pyridoxal-phosphate protein.; 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
-
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
glycine biosynthesis III
-
Glycine, serine and threonine metabolism
-
Metabolic pathways
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-hydroxykynurenine transaminase
Q3LSM4
-
3-hydroxykynurenine transaminase/alanine glyoxylate transaminase
-
-
AGT
-
-
-
-
AGT
Q3LSM4
-
AGT
A2V838
-
AGT-Ma
-
major allele of alanine:glyoxylate aminotransferase
AGT-Mi
-
minor allele of alanine:glyoxylate aminotransferase
AGT1
-
-
AGXT
-
-
AGXT2
-
-
AGXT2
Q9BYV1
-
alanine glyoxylate aminotransferase
-
-
alanine glyoxylate aminotransferase
Q3LSM4
-
alanine glyoxylate aminotransferase
-
-
alanine-glyoxalate aminotransferase
-
-
alanine-glyoxalate transaminase 1
-
-
alanine-glyoxylate aminotransferase
-
-
-
-
alanine-glyoxylate aminotransferase
-
-
alanine-glyoxylate aminotransferase 2
-
-
alanine-glyoxylate aminotransferase isoenzyme 2
-
-
alanine-glyoxylate aminotransferase-2
Q9BYV1
-
alanine-glyoxylic aminotransferase
-
-
-
-
alanine:2-oxoglutarate aminotransferase
-
identical with
alanine:glyoxylate aminotransferase
A2V838
-
alanine:glyoxylate aminotransferase
D2Z0I0
-
alanine:glyoxylate aminotransferase
D2Z0I0
-
-
alanine:glyoxylate aminotransferase
-
-
alanine:glyoxylate aminotransferase
-
-
alanine:glyoxylate aminotransferase 1
-
-
alanine:glyoxylate aminotransferase type 1
-
-
aminotransferase 3
D2Z0I0
-
aminotransferase 3
D2Z0I0
-
-
cytosolic alanine aminotransferase
-
identical with
EC 2.6.1.51
-
serine-pyruvate aminotransferase identical with liver isoenzyme 1
GGT
-, Q9S7E9
-
glyoxylate aminotransferase AGT1
-
-
L-alanine-glycine transaminase
-
-
-
-
L-alanine-glyoxylate aminotransferase
-
-
-
-
serine pyruvate aminotransferase
-
-
serine:pyruvate/alanine:glyoxylate aminotransferase
-
-
serine:pyruvate/alanine:glyoxylate aminotransferase
Rattus norvegicus Wistar
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9015-67-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Yellowfever mosquito
TrEMBL
Manually annotated by BRENDA team
Anas platyrhynchos domestica
duck
-
-
Manually annotated by BRENDA team
AGT1 nucleotide sequence
SwissProt
Manually annotated by BRENDA team
EC2.6.1.4, EC2.6.1.2, EC2.6.1.44; isoform GGT2
Swissprot
Manually annotated by BRENDA team
isoform GGT1
-
-
Manually annotated by BRENDA team
red-faced black spider monkey
SwissProt
Manually annotated by BRENDA team
Goeldis monkey
Q9TTQ8
SwissProt
Manually annotated by BRENDA team
silvery marmoset
-
-
Manually annotated by BRENDA team
common marmoset
-
-
Manually annotated by BRENDA team
Caranx chrysos
yellow mackerel
-
-
Manually annotated by BRENDA team
Diana monkey
SwissProt
Manually annotated by BRENDA team
fat tailed dwarf lemur
-
-
Manually annotated by BRENDA team
Columba livia domestica
pigeon
-
-
Manually annotated by BRENDA team
brown lemur
-
-
Manually annotated by BRENDA team
white leghorn, bantam
-
-
Manually annotated by BRENDA team
common gorilla
SwissProt
Manually annotated by BRENDA team
overexpression in Escherichia coli
-
-
Manually annotated by BRENDA team
patients with primary hyperoxaluria type 1
Swissprot
Manually annotated by BRENDA team
patients with primary hyperoxaluria type I
-
-
Manually annotated by BRENDA team
white-handed gibbon
SwissProt
Manually annotated by BRENDA team
golden lion tamarin
SwissProt
Manually annotated by BRENDA team
Slender loris
-
-
Manually annotated by BRENDA team
japanese macaque
-
-
Manually annotated by BRENDA team
Celebes macaque
SwissProt
Manually annotated by BRENDA team
australian bugerigar
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
Lesser slow loris
-
-
Manually annotated by BRENDA team
Java sparrow
-
-
Manually annotated by BRENDA team
common chimpanzee, sequence of 5' region of the AGT gene
SwissProt
Manually annotated by BRENDA team
anubis baboon
SwissProt
Manually annotated by BRENDA team
white-faced saki monkey
SwissProt
Manually annotated by BRENDA team
orang-utan
-
-
Manually annotated by BRENDA team
fed with vitamin B6 deficient diet
-
-
Manually annotated by BRENDA team
101D, commercial baker's yeast
-
-
Manually annotated by BRENDA team
; expression in Ashbya gossypii
-
-
Manually annotated by BRENDA team
cotton-top tamarin
-
-
Manually annotated by BRENDA team
common squirrel monkey
SwissProt
Manually annotated by BRENDA team
Sardinops sp.
sardine
-
-
Manually annotated by BRENDA team
Scomberomorus sp.
mackerel
-
-
Manually annotated by BRENDA team
gopher gray rock cod
-
-
Manually annotated by BRENDA team
canary
-
-
Manually annotated by BRENDA team
Uroloncha striata domestica
japanese mannikin
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
alanine:glyoxylate aminotransferase deficiency causes primary hyperoxaluria type 1
malfunction
-
mutation W251K involved in primary hyperoxaluria type 1
malfunction
-
deficiency is responsible for Primary Hyperoxaluria Type 1, an autosomal recessive disorder
malfunction
-
causes the hereditary kidney stone disease primary hyperoxaluria type 1
malfunction
-
The hereditary kidney stone disease primary hyperoxaluria type 1 is caused by a deficiency of the peroxisomal enzyme alanine:glyoxylate aminotransferase
malfunction
-
primary hyperoxaluria type 1, a lethal inborn error of glyoxylate metabolism characterized by increased oxalate production, is caused by a deficiency of hepatic peroxisomal alanine:glyoxylate aminotransferase
physiological function
-
overexpression of human AGXT2 protects from asymmetric dimethylarginine-induced inhibition in nitric oxide production
physiological function
-
seems to be required for mobilization and utilization of triglycerides during infection process (to generate glycerol required for mechanical breaching of the host surface)
physiological function
-
indispensable for appressorium function
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxykynurenine + glyoxylate
xanthurenic acid + glycine
show the reaction diagram
Q3LSM4
-
-
-
?
glycine + pyruvate
glyoxylate + L-alanine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
glycine + pyruvate
glyoxylate + L-alanine
show the reaction diagram
-
-
-
-
ir
glycine + pyruvate
L-alanine + glyoxylate
show the reaction diagram
A2V838
-
-
-
?
kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
show the reaction diagram
Q3LSM4
-
-
-
?
L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
show the reaction diagram
-
-
-
-
ir
L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
show the reaction diagram
-
-
-
-
ir
L-alanine + 2-oxobutyrate
pyruvate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
ir
L-alanine + 4-methylthio-2-oxobutyrate
pyruvate + L-methionine
show the reaction diagram
-
poor amino acceptor
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-, Q9W3Z3
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-, Q9S7E9
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
Columba livia domestica
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
r
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-, Q56YA5
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
Scomberomorus sp.
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
P43567, -
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
Q3LSM4
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
isoenzyme 1
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
isoenzyme 2 highly specific, little or no activity with other amino donors/acceptors
-
ir
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
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
key role in the transamination/detoxification of glyoxylate
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
key role in the transamination/detoxification of glyoxylate
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-, Q56YA5
photorespiratory enzyme
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
A2V838
the enzyme is highly specific for catalysing glyoxylate to glycine processing, thereby playing a key role in glyoxylate detoxification, the enzyme is highly specific for catalysing glyoxylate to glycine processing
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
D2Z0I0
high substrate specificity for Ala and glyoxylate
-
-
ir
L-alanine + glyoxylate
glycine + pyruvate
show the reaction diagram
-
-
-
-
?
L-alanine + glyoxylate
glycine + pyruvate
show the reaction diagram
A2V838
transamination half-reaction kinetic parameters
-
-
r
L-alanine + hydroxypyruvate
pyruvate + L-serine
show the reaction diagram
-
-
-
-
ir
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-alanine + phenylpyruvate
pyruvate + L-phenylalanine
show the reaction diagram
-
isoenzyme 1, less effectively acceptor
-
-
ir
L-alanine + pyruvate
pyruvate + L-alanine
show the reaction diagram
-
-
-
-
ir
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
show the reaction diagram
A2V838
-
-
-
?
L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
show the reaction diagram
-
-
-
-
ir
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
show the reaction diagram
A2V838
-
-
-
?
L-asparagine + glyoxylate
4-amino-2,4-dioxobutanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-aspartate + glyoxylate
2-oxosuccinate + glycine
show the reaction diagram
-
-
-
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
show the reaction diagram
-
-
-
-
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
show the reaction diagram
P21549
-
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
-
?
L-glutamate + glyoxylate
2-oxoglutarate + glycine
show the reaction diagram
-, Q9S7E9
-
-
-
?
L-glutamate + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
A2V838
-
-
-
?
L-glutamate + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
-
-
-
-
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
-
-
-
-
ir
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-glutamine + pyruvate
2-oxoglutaramate + L-alanine
show the reaction diagram
-
-
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
show the reaction diagram
-
-
-
-
ir
L-histidine + glyoxylate
3-(1H-imidazol-4-yl)-2-oxopropanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
show the reaction diagram
-, Q9W3Z3
-
-
-
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
-, Q9W3Z3
-
-
-
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
show the reaction diagram
-
-
-
-
ir
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
show the reaction diagram
-
-
-
-
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
show the reaction diagram
A2V838
-
-
-
?
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
show the reaction diagram
-
-
-
-
ir
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
show the reaction diagram
-
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
A2V838
-
-
-
?
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
-
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
-
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
-
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
-, Q56YA5
-
-
-
ir
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
Scomberomorus sp.
-
-
-
-
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
-, Q9W3Z3
-
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
show the reaction diagram
-
-
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
show the reaction diagram
-, Q56YA5
-
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
show the reaction diagram
Scomberomorus sp.
-
-
-
-
ir
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
show the reaction diagram
-
-
-
-
ir
L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
show the reaction diagram
-
-
-
-
ir
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
L-tyrosine + pyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-alanine
show the reaction diagram
-, Q9W3Z3
-
-
-
ir
Nomega,Nomega-dimethyl-L-arginine + pyruvate
5-(N,N-dimethylcarbamidamido)-2-oxopentanoate + alanine
show the reaction diagram
Q9BYV1
-
-
-
?
L-valine + glyoxylate
3-methyl-2-oxobutanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
additional information
?
-
-, Q9W3Z3
aminoadipate, asparagine, aspartate, glutamate, isoleucine, lysine, threonine and valine are no substrates
-
-
-
additional information
?
-
-
aminoadipate, asparagine, aspartate, glutamate, isoleucine, lysine, threonine and valine are no substrates
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
2-oxoglutarate is not an amino acceptor, little or no activity with asparagine, glutamine, glutamate, threonine, cysteine, methionine, arginine, leucine, valine, isoleucine, phenylalanine, tryptophan, histidine or tyrosine as amino donors
-
-
-
additional information
?
-
-
strict specificity for L-alanine and glyoxylate as substrates
-
-
-
additional information
?
-
A2V838
enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
-
-
-
additional information
?
-
P21549
alanine:glyoxylate aminotransferase is able to catalyze the alpha,beta-elimination of beta-chloro-L-alanine with a catalytic efficiency similar to that of the physiological transaminase reaction with L-alanine. The enzyme catalyzes both the alpha,beta-elimination and half-transamination of the natural amino acid L-cysteine together with pyruvate half-transamination, enzyme is able to catalyze the alpha,beta-elimination of beta-chloro-L-alanine with a kcat value of 0.74 per s and a Km value of 0.51 mM
-
-
-
additional information
?
-
-
mitochondrially localized human AGXT2 is able to effectively metabolize asymmetric dimethylarginine in vivo
-
-
-
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-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-, Q9W3Z3
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
-
?
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
Columba livia domestica
-
-
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
Scomberomorus sp.
-
-
-
ir
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
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
key role in the transamination/detoxification of glyoxylate
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-
key role in the transamination/detoxification of glyoxylate
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
-, Q56YA5
photorespiratory enzyme
-
ir
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
A2V838
the enzyme is highly specific for catalysing glyoxylate to glycine processing, thereby playing a key role in glyoxylate detoxification
-
-
?
additional information
?
-
A2V838
enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
activated by heat treatment with pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
Km 0.02 mM
pyridoxal 5'-phosphate
Columba livia domestica, Gallus gallus
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-, Q56YA5
-
pyridoxal 5'-phosphate
-
0.04 mM
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
noncovalently linked
pyridoxal 5'-phosphate
Q3LSM4
0.04 mM
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
like the wild-type, the G82E variant is able to bind 2 mol pyridoxal 5'-phosphate/dimer, it exhibits a significant reduced affinity for pyridoxal 5'-phosphate and even more for pyridoxamine 5'-phosphate compared with wild-type, and an altered conformational state of the bound pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
presence significantly stabilizes enzyme
pyridoxal 5'-phosphate
-
for some mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
D2Z0I0
-
pyridoxal 5'-phosphate
-
2 mol per dimer
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
amino-oxyacetic acid
-
-
amino-oxyacetic acid
-
-
amino-oxyacetic acid
-
competitive inhibitor
aminooxyacetic acid
-
-
D-alanine
-
competitive inhibitor with L-alanine as varied substrate and glyoxylate as fixed substrate. Uncompetitive inhibitor with glyoxylate as varied substrate and L-alanine as fixed substrate; competitive with L-alanine, uncompetitive with glyoxylate
glycine
-
linear competitive inhibitor
glyoxylate
-
above 5 mM
hydroxylamine
-
isoenzyme 1
hydroxylamine
-
isoenzyme; isoenzyme 1
hydroxylamine
-
-
hydroxylamine
-
10 mM, complete inhibition
Isonicotinic acid hydrazide
-
isoenzyme 1 and isoenzyme 2
Isonicotinic acid hydrazide
-
-
L-glutamate
-
GPT 1, alanine:2-oxoglutarate aminotransferase AGT activity
pyruvate
-
mixed type inhibition with L-alanine, competitive with glyoxylate; mixed type inhibitor with L-alanine as varied substrate and glyoxylate as fixed substrate. Competitive inhibitor with glyoxylate as varied substrate and L-alanine as fixed substrate
Semicarbazide
-
isoenzyme 1
Semicarbazide
-
isoenzyme; isoenzyme 1
L-Penicillamine
-
10 mM, 86% inhibition
additional information
-
not inhibitory: 10 mM EDTA, 10 mM p-chloromercuribenzoate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
aminooxyacetic acid
-
presence significantly stabilizes enzyme
aminooxyacetic acid
-
for some enzyme mutants, sensitivity to trypsin can be ameliorated by addition of pyridoxal 5'-phosphate or aminooxyacetic acid
Glucagon
-
induced by, isoenzyme 1 is increased in activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
60
-
2-Aminobutyrate
-
pH 8.0, 37C, glyoxylate as amino acceptor
100
-
2-Aminobutyrate
-
pH 8.0, 37C, pyruvate as amino acceptor
2.7
-
2-oxobutyrate
-
pH 8.0, 37C, alanine as amino donor
18
-
3-hydroxykynurenine
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
22
-
glycine
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
0.07
-
glyoxylate
-
pH 8.2, 37C, isoenzyme 1, alanine as amino donor
0.1
-
glyoxylate
-
pH 8.2, 37C, isoenzyme 1, alanine as amino donor
0.13
-
glyoxylate
-
pH 8.2, 37C, isoenzyme 1, alanine as amino donor
0.13
-
glyoxylate
-
G41V, pH not specified in the publication, temperature not specified in the publication
0.14
-
glyoxylate
-, Q9S7E9
cosubstrate L-glutamate, pH 7.5, 25C
0.15
-
glyoxylate
-
pH 7.0, 27C, alanine as amino donor
0.15
-
glyoxylate
-
mutant G82E, 25C; pH 7.4, 25C, mutant enzyme G82E
0.15
-
glyoxylate
-
G82E, pH not specified in the publication, temperature not specified in the publication
0.18
-
glyoxylate
-
pH 8.0, 37C
0.2
-
glyoxylate
-
pH 8.2, 37C, isoenzyme 1, alanine as amino donor
0.21
-
glyoxylate
-, Q9S7E9
cosubstrate L-glutamate, pH 7.5, 25C
0.22
-
glyoxylate
-
minor allele wild type enzyme
0.22
-
glyoxylate
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
0.23
-
glyoxylate
-
pH 8.0, 37C, recombinant His-AGT, L-alanine as amino donor
0.23
-
glyoxylate
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
0.23
-
glyoxylate
-
major allele wild type enzyme
0.23
-
glyoxylate
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
0.25
-
glyoxylate
-
minor allele mutant enzyme F152I
0.25
-
glyoxylate
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
0.28
-
glyoxylate
-
major allele wild mutant enzyme F152I
0.28
-
glyoxylate
-
F152I, pH not specified in the publication, temperature not specified in the publication
0.31
-
glyoxylate
-, Q9S7E9
cosubstrate L-alanine, pH 7.5, 25C
0.32
-
glyoxylate
-
-
0.32
-
glyoxylate
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
0.34
-
glyoxylate
-
major allele wild mutant enzyme F152A
0.36
-
glyoxylate
-
pH 7.4, 37C, alanine as amino donor
0.39
-
glyoxylate
-
pH 8.0, 37C, recombinant AGT-His, L-alanine as amino donor
0.41
-
glyoxylate
-
G41R, pH not specified in the publication, temperature not specified in the publication
0.44
-
glyoxylate
-
pH 8.0, 37C, alanine as amino donor
0.51
-
glyoxylate
-, Q9S7E9
cosubstrate L-alanine, pH 7.5, 25C
0.67
-
glyoxylate
-
pH 8.0, 37C, 2-aminobutyrate as amino donor
0.7
-
glyoxylate
-
pH 8.2, 37C, isoenzyme 2, alanine as amino donor
0.72
-
glyoxylate
-
pH 8.0, 37C, alanine as amino donor
0.9
-
glyoxylate
D2Z0I0
in 50 mM NaPO4 (pH 8.0), at 70C
1
-
glyoxylate
-
pH 8.2, 37C, isoenzyme 2, alanine as amino donor
1.6
-
glyoxylate
-
pH 7.0, 50C, alanine as amino donor
2.5
-
glyoxylate
-
pH 8.0, 37C, L-alanine as amino donor
64
-
glyoxylate
-, Q9W3Z3
pH 7.0, 50C, alanine as amino donor
3.7
-
kynurenine
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
0.24
-
L-alanine
-
pH 7.5, 37C, mitochondrial isozyme, glyoxylate as amino acceptor
0.52
-
L-alanine
-
isoenzyme AGT 1
0.88
-
L-alanine
-
GPT 1, alanine:2-oxoglutarate aminotransferase AGT activity
0.92
-
L-alanine
-
-
1.11
-
L-alanine
-
pH 7.5, 37C, cytosolic isozyme, glyoxylate as amino acceptor
1.4
-
L-alanine
-
pH 8.2, 37C, isoenzyme 1, glyoxylate as amino acceptor
1.6
-
L-alanine
-
pH 7.0, 27C, glyoxylate as amino acceptor
2.1
-
L-alanine
-
pH 8.2, 37C, isoenzyme 1, glyoxylate as amino acceptor
2.1
-
L-alanine
-
pH 8.2, 37C, glyoxylate as amino acceptor
2.26
-
L-alanine
-
pH 8.0, 37C
2.6
-
L-alanine
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
2.9
-
L-alanine
-
pH 8.0, 37C, 2-oxobutyrate as amino acceptor
3
-
L-alanine
-
pH 8.2, 37C, isoenzyme 1, glyoxylate as amino acceptor
3.3
-
L-alanine
-
isoenzyme AGT 2
3.56
-
L-alanine
-, Q9S7E9
pH 7.5, 25C
3.9
-
L-alanine
-
pH 8.2, 37C, isoenzyme 1, glyoxylate as amino acceptor
4.76
-
L-alanine
-, Q9S7E9
pH 7.5, 25C
8.1
-
L-alanine
D2Z0I0
in 50 mM NaPO4 (pH 8.0), at 70C
9.1
-
L-alanine
-
pH 8.0, 37C, recombinant His-AGT, glyoxylate as amino acceptor
9.4
-
L-alanine
-
pH 8.0, 37C, recombinant AGT-His, glyoxylate as amino acceptor
11
-
L-alanine
-
pH 8.0, 37C, glyoxylate as amino acceptor
13.5
-
L-alanine
-
pH 8.0, 37C, glyoxylate as amino acceptor
14.9
-
L-alanine
-
pH 7.4, 37C, glyoxylate as amino acceptor
15
-
L-alanine
-
mutant G82E, 25C; pH 7.4, 25C, mutant enzyme G82E
15
-
L-alanine
-
G82E, pH not specified in the publication, temperature not specified in the publication
18
-
L-alanine
-
pH 7.0, 50C, glyoxylate as amino acceptor
22
-
L-alanine
-
G41R, pH not specified in the publication, temperature not specified in the publication
25
-
L-alanine
-
pH 8.2, 37C, isoenzyme 2, glyoxylate as amino acceptor
28
-
L-alanine
-
minor allele wild type enzyme
28
-
L-alanine
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
30
-
L-alanine
-
pH 8.2, 37C, isoenzyme 2, glyoxylate as amino acceptor
30
-
L-alanine
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
31
-
L-alanine
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
31
-
L-alanine
-
major allele wild type enzyme
31
-
L-alanine
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
34
-
L-alanine
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
37
-
L-alanine
-
major allele mutant enzyme F152I
37
-
L-alanine
-
F152I, pH not specified in the publication, temperature not specified in the publication
41
-
L-alanine
-
minor allele mutant enzyme F152I
41
-
L-alanine
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
42
-
L-alanine
-
G41V, pH not specified in the publication, temperature not specified in the publication
46
-
L-alanine
-
major allele mutant enzyme F152A
101.2
-
L-alanine
-, Q56YA5
pH 7.0, 37C, glyoxylate as amino acceptor
149
-
L-alanine
-, Q9W3Z3
pH 7.0, 50C, glyoxylate as amino acceptor
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
1.7
-
L-glutamate
-
pH 7.0, 27C, glyoxylate as amino acceptor
1.97
-
L-glutamate
-, Q9S7E9
pH 7.5, 25C
3.32
-
L-glutamate
-, Q9S7E9
pH 7.5, 25C
0.39
-
L-serine
-, Q56YA5
pH 7.0, 37C, SGT activity, pyruvate as amino acceptor
1.52
-
L-serine
-, Q56YA5
pH 7.0, 37C, SGT activity, glyoxylate as amino acceptor
256
-
L-serine
-, Q9W3Z3
pH 7.0, 50C, glyoxylate as amino acceptor
0.21
-
pyruvate
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
2.5
-
pyruvate
-
pH 8.0, 37C, 2-aminobutyrate as amino donor
51
-
pyruvate
-, Q9W3Z3
pH 7.0, 50C, serine as amino donor
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
20
-
3-hydroxykynurenine
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
0.33
-
glycine
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
0.068
-
glyoxylate
-
mutant G82E, 25C; pH 7.4, 25C, mutant enzyme G82E
0.068
-
glyoxylate
-
G82E, pH not specified in the publication, temperature not specified in the publication
11.1
-
glyoxylate
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
16
-
glyoxylate
-
pH 7.0, 50C, L-alanine as amino donor
18.3
-
glyoxylate
-
G41V, pH not specified in the publication, temperature not specified in the publication
20.5
-
glyoxylate
-
G41R, pH not specified in the publication, temperature not specified in the publication
22.6
-
glyoxylate
-
major allele wild mutant enzyme F152A
37
-
glyoxylate
-
minor allele wild type enzyme
37
-
glyoxylate
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
39
-
glyoxylate
-
major allele wild mutant enzyme F152I
39
-
glyoxylate
-
F152I, pH not specified in the publication, temperature not specified in the publication
40
-
glyoxylate
-
minor allele mutant enzyme F152I
40
-
glyoxylate
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
45
-
glyoxylate
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
45
-
glyoxylate
-
major allele wild type enzyme
45
-
glyoxylate
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
113
-
glyoxylate
-, Q9W3Z3
pH 7.0, 50C, L-alanine as amino donor
12
-
kynurenine
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
0.07
-
L-alanine
-
mutant G82E, 25C; pH 7.4, 25C, mutant enzyme G82E
0.07
-
L-alanine
-
G82E, pH not specified in the publication, temperature not specified in the publication
10.6
-
L-alanine
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
17.1
-
L-alanine
-
G41V, pH not specified in the publication, temperature not specified in the publication
19.8
-
L-alanine
-
G41R, pH not specified in the publication, temperature not specified in the publication
20
-
L-alanine
-
pH 7.0, 50C, glyoxylate as amino acceptor
21.2
-
L-alanine
-
major allele mutant enzyme F152A
33
-
L-alanine
-
minor allele wild type enzyme
33
-
L-alanine
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
33.6
-
L-alanine
-
minor allele mutant enzyme F152I
33.6
-
L-alanine
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
34.2
-
L-alanine
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
35
-
L-alanine
-
major allele mutant enzyme F152I
35
-
L-alanine
-
F152I, pH not specified in the publication, temperature not specified in the publication
45
-
L-alanine
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
45
-
L-alanine
-
major allele wild type enzyme
45
-
L-alanine
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
117
-
L-alanine
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
131
-
L-alanine
-, Q9W3Z3
pH 7.0, 50C, glyoxylate as amino acceptor
0.22
-
L-cysteine
-
pH 7.4
0.36
-
pyruvate
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.45
-
glyoxylate
-
G82E, pH not specified in the publication, temperature not specified in the publication
11154
35
-
glyoxylate
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
11154
50
-
glyoxylate
-
G41R, pH not specified in the publication, temperature not specified in the publication
11154
66
-
glyoxylate
-
major allele wild mutant enzyme F152A
11154
139
-
glyoxylate
-
major allele wild mutant enzyme F152I
11154
139
-
glyoxylate
-
F152I, pH not specified in the publication, temperature not specified in the publication
11154
143
-
glyoxylate
-
G41V, pH not specified in the publication, temperature not specified in the publication
11154
160
-
glyoxylate
-
minor allele mutant enzyme F152I
11154
160
-
glyoxylate
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
11154
168
-
glyoxylate
-
minor allele wild type enzyme
11154
168
-
glyoxylate
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
11154
196
-
glyoxylate
-
major allele wild type enzyme
11154
196
-
glyoxylate
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
11154
0.005
-
L-alanine
-
G82E, pH not specified in the publication, temperature not specified in the publication
12048
0.35
-
L-alanine
-
P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication
12048
0.41
-
L-alanine
-
G41V, pH not specified in the publication, temperature not specified in the publication
12048
0.46
-
L-alanine
-
major allele mutant enzyme F152A
12048
0.82
-
L-alanine
-
minor allele mutant enzyme F152I
12048
0.82
-
L-alanine
-
P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication
12048
0.9
-
L-alanine
-
G41R, pH not specified in the publication, temperature not specified in the publication
12048
0.95
-
L-alanine
-
major allele mutant enzyme F152I
12048
0.95
-
L-alanine
-
F152I, pH not specified in the publication, temperature not specified in the publication
12048
1.2
-
L-alanine
-
minor allele wild type enzyme
12048
1.2
-
L-alanine
-
P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication
12048
1.4
-
L-alanine
-
major allele wild type enzyme
12048
1.4
-
L-alanine
-
major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication
12048
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
14.3
-
D-alanine
-
with L-alanine as varied substrate and glyoxylate as fixed substrate, Kis
28.7
-
D-alanine
-
with glyoxylate as varied substrate and L-alanine as fixed substrate, Kii
8.7
-
glycine
-
pH 7.0, 27C
1.8
-
L-glutamate
-
pH 7.0, 27C
1.8
-
L-glutamate
-
GPT 1, alanine:2-oxoglutarate aminotransferase AGT activity
2.3
-
pyruvate
-
glyoxylate as varied substrate and L-alanine as fixed substrate
15.8
-
pyruvate
-
with L-alanine as varied substrate and glyoxylate as fixed substrate, Kis
22.8
-
pyruvate
-
with L-alanine as varied substrate and glyoxylate as fixed substrate, Kii
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.071
-
D2Z0I0
enzyme from cell free extract
2.64
-
-
isoenzyme 2
2.93
-
-
isoenzyme 2
4.62
-
-
recombinant enzyme
10.6
-
Columba livia domestica
-
-
19
-
D2Z0I0
after 270fold purification
21.4
-
-
isoenzyme 1
23.2
-
-
isoenzyme 1
29
-
-
37C, pH 7.5
51.8
-
-
purified recombinant enzyme
86.3
-
-
isoenzyme 1
91
-
-
isoenzyme 1
160
-
-
isoenzyme 1
160
-
-
pH 8.0, 37C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
9
-
cytosolic isozyme, no distinct pH optimum
7.5
8.5
-
recombinant enzyme
7.8
8
-
-
8.1
8.4
-
isoenzyme 2
8.5
8.8
-
isoenzyme 2
8.6
-
-
mitochondrial isozyme
9
-
Columba livia domestica
-
-
9
-
-
best pH for activity towards alanine
9
-
Q9W3Z3
best pH for activity towards alanine
9
-
Q3LSM4
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
10
Q3LSM4
high activity levels are noted at pH 7.0-10.0
7
8.2
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
80
-, Q9W3Z3
alanine as substrate
60
-
-
alanine as substrate
additional information
-
-
activity increases with temperature from 37C to 90C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80
-
Q3LSM4
high activity even at 80C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
-
-
calculated
5.9
-
-
isoelectric focusing on a pH 3.5-10 ampholine gradient
6
-
-
isoelectric focusing on a pH 3.5-10 ampholine gradient
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
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
expressed primarily in the kidney
Manually annotated by BRENDA team
-, Q9S7E9
mature; mature leaf
Manually annotated by BRENDA team
Scomberomorus sp.
-
-
Manually annotated by BRENDA team
Anas platyrhynchos domestica, Anser anser domesticus, Columba livia domestica, Gallus gallus, Melopsittacus undulatus, Padda oryzivora, Passer montanus saturatus, Phasianus versicolor, Serinus canaria, Uroloncha striata domestica
-
-
Manually annotated by BRENDA team
-, Q9S7E9
grown in dark or in light; grown in dark or in light
Manually annotated by BRENDA team
-, Q9S7E9
green; green silique
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
additional information
-, Q9S7E9
not in root
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
apoenzyme in the peroxisomes, holoenzyme in the mitochondrion
Manually annotated by BRENDA team
-
mutant enzyme G170R
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Anas platyrhynchos domestica, Anser anser domesticus, Columba livia domestica
-
holoenzyme in the peroxisomes
Manually annotated by BRENDA team
-
apoenzyme in the peroxisomes, holoenzyme in the mitochondrion
Manually annotated by BRENDA team
-
apoenzyme in the peroxisomes, holoenzyme in the mitochondrion
Manually annotated by BRENDA team
-
holoenzyme in the peroxisomes
Manually annotated by BRENDA team
Uroloncha striata domestica
-
apoenzyme in the peroxisomes, holoenzyme in the mitochondrion
Manually annotated by BRENDA team
-
wild type enzyme
Manually annotated by BRENDA team
-
sequence contains two sites of peroxisomal targeting sequences around amino acids 59-66 and 389-392
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42700
-
-
about 42700 Da, SDS-PAGE
48600
-
-
SDS-PAGE
52000
-
-
FLAG-tagged enzyme, SDS-PAGE
53000
-
-
SDS-PAGE
69000
-
D2Z0I0
gel filtration
77000
-
-
isoenzyme 1, gel filtration
80000
-
-
sucrose-density-gradient centrifugation
80000
-
-
peroxisomal and mitochondrial alanine-glyoxylate aminotransferase 1; sucrose-density-gradient centrifugation
80000
-
-
sucrose-density-gradient centrifugation
80000
-
-
peroxisomal and mitochondrial alanine-glyoxylate aminotransferase 1
90000
-
Columba livia domestica
-
gel filtration, sucrose density gradient centrifugation
90000
-
-
-
90000
-
-, Q56YA5
-
92140
-
-, Q56YA5
AGT1, calculated from gel filtration
110000
-
-
-
170000
-
-
isoenzyme 2, gel filtration
170000
-
-
PAGE
175000
-
-
liver isoenzyme 2, gel filtration
200000
-
Scomberomorus sp.
-
alanine-glyoxylate aminotransferase I
200000
-
Columba livia domestica, Gallus gallus
-
mitochondrial holo enzyme, sucrose density gradient centrifugation
210000
-
-
isoenzyme AGT 2
213000
-
-
analytical ultracentrifugation
220000
-
-
gel filtration
220000
-
-
-
236000
-
-
sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q9S7E9
x * 53300, calculated; x * 53400, calculated
?
-
x * 41736, calculated
?
-
x * 43000, SDS-PAGE
dimer
-
2 * 38000, isoenzyme 1, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
Columba livia domestica
-
2 * 45000, holoenzyme, SDS-PAGE
dimer
-
2 * 43000, immunoreaction; 2 * 43000, SDS-PAGE
dimer
-
2 * 44400, homodimer, recombinant enzyme, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
dimer
-, Q56YA5
2 * 45000, SDS-PAGE
dimer
-
2 * 43000, homodimer; 2 * 43000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
crystallization data
dimer
Rattus norvegicus Wistar
-
2 * 45000, SDS-PAGE
-
homodimer
-
2 * 43000, SDS-PAGE
homodimer
-
x-ray crystallography
homodimer
-
-
homodimer
-
gel filtration
tetramer
-
4 * 56000, SDS-PAGE
tetramer
Scomberomorus sp.
-
-
tetramer
Columba livia domestica, Gallus gallus
-
4 * 50000, mitochondrial holoenzyme, antibody cross reaction
tetramer
-
4 * 42000, SDS-PAGE, 4 * 45169, claculated
monomer
-
1 * 45000, apoenzyme, SDS-PAGE
additional information
-
N-terminal animo acid sequence
additional information
-
the two allelic forms consist of a wild-type major allele, AGTma, and a minor allele, AGTmi. Wild-type minor allele displays about 46-50% of the activity of the major allele
additional information
-
analysis of wild-type and mutants after partial digestions using trypsin. 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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapour diffusion method with 12% polyethylene glycol 8000, 0.13 M magnesium acetate, 4% butanol, and 0.1 M cacodylic acid at pH 6.5
-
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
-
using 10% (w/v) PEG 4000 in 0.1 M Na HEPES pH 7.5
-
crystallization of the native and selenomethionyl alanine:glyoxylate aminotransferase is performed using the hanging-drop vapour-diffusion method. Crystal struture is determined at 2.3 A resolution; crystallization of the native and selenomethionyl enzyme is performed using the hanging-drop vapour-diffusion method. Crystal structure is determined at 2.3 A resolution; native enzyme and selenomethionine derivative, to 2.3 A and 2.55 A resolution, respectively. Enzyme is a tetramer. The monomer consists of an N-terminal arm of residues 117, a small domain from residues 1847 and 295405 and a large domain of residues 48294. The amino-acid residues involved in cofactor binding are Asn175, Tyr206, Lys234 and Arg242. The guanidino group of Arg361 forms a salt bridge with one carboxylate of the maleate, Thr108 forms a salt bridge with the side-chain carboxylate of the maleate
Q9C4M4
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
Q3LSM4
shows little activity at pH 6.0
7
10
Q3LSM4
high activity levels are noted at pH 7.0-10.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70.1
-
-
the melting temperature of the minor allele holoenzyme is at 70.1C
76.3
-
-
the melting temperature of the major allele holoenzyme is at 76.3C
80
-
-
10 min, stabel up to
80
-
Q3LSM4
high activity even at 80C
90
-
-
10 min, less than 50% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pyridoxal 5'-phosphate stabilizes during purification
-
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
is inhibited by hypoxia, resulting in a very low amount of glycine in hypoxic seedlings
-
675140
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 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
-
0-6C, 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
-
-20C, peroxisomal holoenzyme, may be stored for at least 4 weeks without loss of activity
Columba livia domestica
-
4C, peroxisomal holoenzyme, 50% activity is lost when stored for 6 days
Columba livia domestica
-
-20C, 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
-
0-6C, 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
-
-20C, peroxisomal apoenzyme, may be stored for at least 4 weeks without loss of activity
-
4C, peroxisomal apoenzyme, 50% activity is lost when stored for 6 days
-
-20C, wild-type and mutant enzyme G82E are stable for at least 1 month
-
-20C, 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
-
0-6C, 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
-
-20C, 50 mM potassium phosphate buffer, 0.1 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, may be stored for at least 4 weeks without loss of either activity
-
-20C, crude homogenate can be stored for 6-12 months with little loss of activity
-
-20C, purified enzyme, 50% glycerol, can be stored for at least 3 months with little loss in activity
-
-20C, purified enzyme, freezing results in formation of floculence and complete loss of activity
-
0-6C, 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
-
-20C, 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
-
0-4C, little or no activity is lost when stored for 2 weeks
-
-18C, stable for about 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DEAE-Sepharose chromatography, phenyl-Sepharose chromatography, hydroxyapatite chromatography, and gel filtration
Q3LSM4
recombinant enzyme
-, Q56YA5
partially
Caranx chrysos
-
-
Columba livia domestica
-
isoenzyme 1
-
nickel-resin affinity chromatography, gel filtration
-
recombinant wild-type and G82E mutant His-tagged enzyme
-
butyl-Toyopearl column chromatography, DEAE-Toyopearl column chromatography, hydroxyapatite column chromatography, MonoQ column chromatography, and phenyl Superose gel filtration
D2Z0I0
isoenzyme 1 and 2
-
co-purified with 2-aminobutyrate aminotranferase
-
isoenzyme 1 and 2
-
recombinant enzyme SPT10
-
partially
Sardinops sp.
-
-
Scomberomorus sp.
-
; recombinant enzyme
Q9C4M4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNA isolation
-
expressed in Sf9 cells
Q3LSM4
cDNA for AGT1 expressed in Escherichia coli BL-21
-, Q56YA5
sequencing of the 5' region of the AGT gene
Q9TTS7
sequencing of the 5' region of the AGT gene
Q9TTQ8
single AGT gene cloned
-
sequencing of the 5' region of the AGT gene
Q9TTR4
sequencing of the 5' region of the AGT gene
Q9TTQ0
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 Escherichia coli JM109 cells
-
expressed in Mus musculus embryonic stem cells
-
expressed in stably transformed CHO cells
-
expression in Escherichia coli
-
expression in Escherichia coli; wild-type and G82E mutant His-tagged enzyme expressed in Escherichia coli
-
expression in HeLa cell; 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
-
expression of of untagged alanine-glyoxylate aminotransferase in Escherichia coli
-
for sequence determination, GFP-fusion proteins used in localization experiments
-
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
-
sequencing of the 5' region of the AGT gene
Q9TTP9
sequencing of the 5' region of the AGT gene
Q9TTP8
sequencing of the 5' region of the AGT gene
-
used in complementation experiments, AGT1-eGFP fusion protein used in localization experiments
-
used in knockout experiments
-
used in knockout experiments
Q9BYV1
sequencing of the 5' region of the AGT gene
Q9TTP2
sequencing of the 5' region of the AGT gene
Q9TSP4
sequencing of the 5' region of the AGT gene
Q9TTP3
Escherichia coli DH1 transformed with pRspt10
-
mitochondrial and peroxisomal isozymes generated from a single gene by alternative transcription initiation, cloned and expressed in Escherichia coli DH5 and ER1458
-
expressed in Ashbya gossypii strain ATCC10895
-
sequencing of the 5' region of the AGT gene
Q9TTP0
expression in Escherichia coli
Q9C4M4
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
constitutively expressed
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A112D
-
less than 5% of the specific activity of the wild type enzyme
A280V
P21549
natural mutant from patient with primary hyperoxaluria type 1, 92% of normal enzyme activity
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
F152A
-
the mutant shows decreased activity compared to the wild type enzyme
F152I
-
natural mutation in enzyme minor allele, decreased activity
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
F152I
-
soluble, catalytically active
F52I
-
natural mutation in enzyme major allele, 13% of the activity of major allele; natural mutation in enzyme minor allele, 14% of the activity of minor allele
G156R
-
less than 5% of the specific activity of the wild type enzyme
G161R
P21549
natural mutant from patient with primary hyperoxaluria type 1, 6.2% of normal enzyme activity
G161R
-
less than 5% of the specific activity of the wild type enzyme
G170R
-
mutation associated with primary hyperoxaluria type I, no effect on affinity for pyridoxal 5-phosphate
G170R
-
42% of the specific activity of the wild type enzyme
G170R
-
mainly localized in mitochondria compared to the peroxisomal wild type enzyme
G170R
-
natural mutation in enzyme minor allele, 40-57% of the activity of major allele, in vitro
G170R
-
the mutant shows decrease in protein stability
G41R
-
mutation associated with primary hyperoxaluria type I, enhanced activity after re-folding
G41R
-
24% of the specific activity of the wild type enzyme
G41R
-
natural mutation in enzyme major allele, 46.5% of the activity of major allele; natural mutation in enzyme minor allele, 23.7% of the activity of minor allele
G41R
-
the mutation on the minor and major alleles causes hyperoxaluria type 1, the variant under physiological conditions forms insoluble inactive high-order aggregates through intermolecular electrostatic interactions, the mutation decreases resistance to thermal denaturation and inactivation
G41R
-
naturally occuring mutation, predicted to be responsible for the depletion of immunoreactive enzyme protein and formation of intraperoxisomal aggregates
G41V
-
mutation associated with primary hyperoxaluria type I, enhanced activity after re-folding
G41V
-
18% of the specific activity of the wild type enzyme
G41V
-
the mutation on the major alle causes hyperoxaluria type 1, the variant under physiological conditions forms insoluble inactive high-order aggregates through intermolecular electrostatic interactions, the mutation decreases resistance to thermal denaturation and inactivation
G41V
-
naturally occuring mutation
G82E
-
less than 5% of the specific activity of the wild type enzyme
G82E
-
natural enzyme variant. Significant reduction in affinty for pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate. Mutant displays an altered conformational state of the bound pyridoxal 5'-phosphate and a decrease in overall catlytic activity to 0.1% of wild-type; naturally occuring variant. Like the wild-type, the G82E variant is able to bind 2 mol pyridoxal 5'-phosphate/dimer, it exhibits a significant reduced affinity for pyridoxal 5'-phosphate and even more for pyridoxamine 5'-phosphate compared with wild-type, and an altered conformational state of the bound pyridoxal 5'-phosphate. Dramatic decrease of the overall catalytic activity (about 0.1% of that of normal alanine:glyoxylate aminotransferase), appears to be related to the inability to undergo an efficient transaldimination of the pyridoxal 5'-phosphate form of the enzyme with amino acids as well as an efficient conversion of AGT-pyridoxamine 5'-phosphate into AGT-pyridoxal 5'-phosphate
G82E
-
naturally occuring mutation, decreased catalytic activity
I244T
-
natural mutation in enzyme minor allele, 8-26% of the activity of major allele, in vitro
I279T
P21549
natural mutant from patient with primary hyperoxaluria type 1, 98% of normal enzyme activity
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
P10L/P11L
-
Kcat value 56% of wild type protein, aggregation occuring at a slower rate than that of DELTA 1-21 protein
P11L
-
50% of activity of enzyme from major allele
P11L
-
one of the mutations of the minor allele
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
-
minor allele, naturally occuring variant; mutant protein (minor allel) is about 95% peroxisomal and 5% mitochondrial; P11/I340 major allele is 100% peroxisomal, minor allele in both the holo and apo forms is more sensitive to thermal denaturation and to urea unfolding than major allele
P11L/I340M
-
naturally occuring mutations, minor allele
P11L/I340M
-
naturally occuring mutations, encoded by the minor allele, up to 100% activity
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
-
natural mutation in enzyme major allele, 14% of the activity of wild-type tmajor allele, in vitro; natural mutation in enzyme minor allele, no in vitro enzymic activity
R233C
-
natural mutation in enzyme major allele, 21% of the activity of major allele; natural mutation in enzyme minor allele, below 5% of the activity of minor allele
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
-
less than 5% of the specific activity of the wild type enzyme
S205P
-
natural mutation in enzyme major allele, decreased activity
S218L
P21549
natural mutant from patient with primary hyperoxaluria type 1, 10% of normal enzyme activity
S218L
-
less than 5% of the specific activity of the wild type enzyme
V336D
-
natural mutation in enzyme major allele, 22.4% of the activity of major allele; natural mutation in enzyme minor allele, 5.2% of the activity of minor allele
W108R
-
less than 5% of the specific activity of the wild type enzyme
K209R
-
less than 5% of the specific activity of the wild type enzyme
additional information
P21549
analysis of additional mutations
additional information
-
expression of green fluorescent protein-tagged enzyme in HeLa cells. Identification of two sites of peroxisomal targeting sequences around amino acids 59-66 and 389-392. A truncated mutant missing the COOH-terminal amino acids, 1216 is not targeted into peroxisome. Deletion mutant lacking amino acids 221390 or amino acids 221389 are not targeted into peroxisome. Deltion mutants lacking 221388 or 221386 are targeted
additional information
-
human enzyme can substitute for function of yeast Agx1. Mutations associated with disease in humans show reduced growth in yeast, refecting reduced protein levels
additional information
-
after random mutagenesis the subcellular distribution of mutant proteins (GFP-fusion proteins) is analyzed
W251K
-
naturally occuring mutation, mutant protein localized in peroxisome and cytosol
additional information
-
enzyme knockout strain, 2% residual activity, no glycine auxotrophic phenotype. Glycine auxtrophy requires additional deletion of genes for threonine aldolase, and for mitochondrial and cytosolic serine hydroxymethyltransferase
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
hereditary disease primary hyperoxaluria type 1 is caused by a deficiency of the liver-specific peroxisomal enzyme alanine:glyoxylate aminotransferase, diagnosis with selective inhibitors and enzyme assays
medicine
-
primary hyperoxaluria type I is a severe kidney stone disease caused by mutations in the protein alanine:glyoxylate aminotransferase
medicine
-
after 4 weeks of vitamin B6-deficient diet, hepatic enzyme activity and mRNA level are significantly lower than in control animals. Urinary oxalate-to-creatinine and glycolate-to-creatinine ratios are higher than in controls, but urinary glycine-to-creatinine and citrate-to-creatinine ratios are significantly lower
nutrition
-
overexpression of enzyme in Ashbya gossypii, use for production of riboflavin for human and animal feed supplement