Information on EC 2.6.1.44 - alanine-glyoxylate transaminase

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

EC NUMBER
COMMENTARY hide
2.6.1.44
-
RECOMMENDED NAME
GeneOntology No.
alanine-glyoxylate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-alanine + glyoxylate = pyruvate + glycine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
-
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
glycine biosynthesis III
-
-
glycine metabolism
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9015-67-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
duck
-
-
Manually annotated by BRENDA team
goose
-
-
Manually annotated by BRENDA team
red-faced black spider monkey
SwissProt
Manually annotated by BRENDA team
Goeldis monkey
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
fruit fly
GenBank
Manually annotated by BRENDA team
brown lemur
-
-
Manually annotated by BRENDA team
cat
-
-
Manually annotated by BRENDA team
white leghorn, bantam
-
-
Manually annotated by BRENDA team
common gorilla
SwissProt
Manually annotated by BRENDA team
strain TK-6
UniProt
Manually annotated by BRENDA team
strain TK-6
UniProt
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
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
sparrow
-
-
Manually annotated by BRENDA team
pheasant
-
-
Manually annotated by BRENDA team
white-faced saki monkey
SwissProt
Manually annotated by BRENDA team
orang-utan
-
-
Manually annotated by BRENDA team
-
-
-
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
spinach
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Uroloncha striata domestica
japanese mannikin
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxykynurenine + glyoxylate
xanthurenic acid + glycine
show the reaction diagram
-
-
-
?
glycine + pyruvate
glyoxylate + L-alanine
show the reaction diagram
glycine + pyruvate
L-alanine + glyoxylate
show the reaction diagram
-
-
-
?
kynurenine + glyoxylate
4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
show the reaction diagram
-
-
-
?
L-2-aminobutyrate + glyoxylate
2-oxobutanoate + glycine
show the reaction diagram
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
glycine + pyruvate
show the reaction diagram
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
L-alanine + hydroxypyruvate
pyruvate + L-serine
show the reaction diagram
L-alanine + phenylpyruvate
pyruvate + L-phenylalanine
show the reaction diagram
L-alanine + pyruvate
pyruvate + L-alanine
show the reaction diagram
-
-
-
-
ir
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-aspartate + glyoxylate
2-oxosuccinate + glycine
show the reaction diagram
-
-
-
ir
L-cysteine + pyruvate
3-mercapto-2-oxopropanoate + L-alanine
show the reaction diagram
L-glutamate + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
L-glutamate + glyoxylate
2-oxoglutarate + glycine
show the reaction diagram
-
-
-
?
L-glutamine + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
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
L-histidine + pyruvate
3-(1H-imidazol-4-yl)-2-oxopropanoate + L-alanine
show the reaction diagram
-
-
-
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
L-methionine + glyoxylate
4-methylsulfanyl-2-oxobutanoate + glycine
show the reaction diagram
L-methionine + pyruvate
4-methylsulfanyl-2-oxobutanoate + L-alanine
show the reaction diagram
L-phenylalanine + glyoxylate
phenylpyruvate + glycine
show the reaction diagram
L-phenylalanine + pyruvate
phenylpyruvate + L-alanine
show the reaction diagram
L-serine + glyoxylate
3-hydroxy-2-oxopropanoate + glycine
show the reaction diagram
L-serine + pyruvate
3-hydroxy-2-oxopropanoate + L-alanine
show the reaction diagram
L-tryptophan + glyoxylate
3-indole-2-oxopropanoate + glycine
show the reaction diagram
L-tryptophan + pyruvate
3-indole-2-oxopropanoate + L-alanine
show the reaction diagram
L-tyrosine + glyoxylate
3-(4-hydroxyphenyl)-2-oxopropanoate + glycine
show the reaction diagram
L-tyrosine + pyruvate
3-(4-hydroxyphenyl)-2-oxopropanoate + L-alanine
show the reaction diagram
-
-
-
ir
L-valine + glyoxylate
3-methyl-2-oxobutanoate + glycine
show the reaction diagram
-
isoenzyme 1
-
-
ir
Nomega,Nomega-dimethyl-L-arginine + pyruvate
5-(N,N-dimethylcarbamidamido)-2-oxopentanoate + alanine
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
-
A2V838
enzyme is highly specific for catalyzing glyoxylate to glycine processing, playing a key role in glyoxylate detoxification
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amino-oxyacetic acid
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
Isonicotinic acid hydrazide
L-glutamate
L-Penicillamine
-
10 mM, 86% inhibition
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
additional information
-
not inhibitory: 10 mM EDTA, 10 mM p-chloromercuribenzoate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aminooxyacetic acid
glucagon
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
60 - 100
2-aminobutyrate
2.7
2-oxobutyrate
-
pH 8.0, 37C, alanine as amino donor
18
3-hydroxykynurenine
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 - 64
glyoxylate
3.7
kynurenine
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
0.24 - 149
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
1.7 - 3.32
L-glutamate
0.39 - 256
L-serine
0.21 - 51
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
3-hydroxykynurenine
Aedes aegypti
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
0.33
glycine
Homo sapiens
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
0.068 - 113
glyoxylate
12
kynurenine
Aedes aegypti
Q3LSM4
in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45C
0.07 - 131
L-alanine
0.22
L-cysteine
Homo sapiens
-
pH 7.4
0.36
pyruvate
Homo sapiens
-
pH 7.4, 25C, wild-type enzyme; wild-type, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
8.7
glycine
-
pH 7.0, 27C
1.8
L-glutamate
2.3 - 22.8
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.071
enzyme from cell free extract
2.64
-
isoenzyme 2
4.62
-
recombinant enzyme
10.6
Columba livia domestica
-
-
19
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
7 - 9
-
cytosolic isozyme, no distinct pH optimum
7.5 - 8.5
-
recombinant enzyme
7.8 - 8
-
-
8.1 - 8.4
-
isoenzyme 2
8.3 - 8.6
8.5 - 8.8
-
isoenzyme 2
8.6
-
mitochondrial isozyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
7 - 10
high activity levels are noted at pH 7.0-10.0
7 - 8.2
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
alanine as substrate
60
-
alanine as substrate
additional information
-
activity increases with temperature from 37C to 90C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
80
high activity even at 80C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
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
COMMENTARY hide
LITERATURE
SOURCE
green; green silique
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42700
-
about 42700 Da, SDS-PAGE
48600
-
SDS-PAGE
52000
-
FLAG-tagged enzyme, SDS-PAGE
53000
-
SDS-PAGE
92140
AGT1, calculated from gel filtration
170000
175000
200000
210000
-
isoenzyme AGT 2
213000
-
analytical ultracentrifugation
220000
236000
-
sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
-
1 * 45000, apoenzyme, SDS-PAGE
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
shows little activity at pH 6.0
671871
7 - 10
high activity levels are noted at pH 7.0-10.0
671871
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
90
-
10 min, less than 50% residual activity
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
-
pyridoxal 5'-phosphate stabilizes during purification
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
is inhibited by hypoxia, resulting in a very low amount of glycine in hypoxic seedlings
-
675140
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, stable for about 2 weeks
-
-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
-
-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, 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
-20C, crude homogenate can be stored for 6-12 months with little loss of activity
-
-20C, peroxisomal apoenzyme, may be stored for at least 4 weeks without loss of activity
-
-20C, peroxisomal holoenzyme, may be stored for at least 4 weeks without loss of activity
Columba livia domestica
-
-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
-
-20C, wild-type and mutant enzyme G82E are stable for at least 1 month
-
0-4C, little or no activity is lost when stored for 2 weeks
-
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
4C, peroxisomal apoenzyme, 50% activity is lost when stored for 6 days
-
4C, peroxisomal holoenzyme, 50% activity is lost when stored for 6 days
Columba livia domestica
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant enzyme
butyl-Toyopearl column chromatography, DEAE-Toyopearl column chromatography, hydroxyapatite column chromatography, MonoQ column chromatography, and phenyl Superose gel filtration
co-purified with 2-aminobutyrate aminotranferase
-
DEAE-Sepharose chromatography, phenyl-Sepharose chromatography, hydroxyapatite chromatography, and gel filtration
isoenzyme 1
isoenzyme 1 and 2
nickel-resin affinity chromatography, gel filtration
-
partially
recombinant enzyme
recombinant enzyme SPT10
-
recombinant wild-type and G82E mutant His-tagged enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AGXT cDNA cloned, AGXT*LTM expressed as a GST-fusion protein in Escherichia coli BL21(RIL) and in Sf9 cells
-
cDNA for AGT1 expressed in Escherichia coli BL-21
cDNA isolation
-
cloned and expressed in Escherichia coli JM109
-
Escherichia coli DH1 transformed with pRspt10
-
expressed in Ashbya gossypii strain ATCC10895
-
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 Sf9 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
-
mitochondrial and peroxisomal isozymes generated from a single gene by alternative transcription initiation, cloned and expressed in Escherichia coli DH5 and ER1458
-
sequencing of the 5' region of the AGT gene
single AGT gene cloned
-
used in complementation experiments, AGT1-eGFP fusion protein used in localization experiments
-
used in knockout experiments
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
constitutively expressed
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A112D
-
less than 5% of the specific activity of the wild type enzyme
A280V
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
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
I244T
-
natural mutation in enzyme minor allele, 8-26% of the activity of major allele, in vitro
I279T
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
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
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
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
W251K
-
naturally occuring mutation, mutant protein localized in peroxisome and cytosol
additional information
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
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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)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
nutrition
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overexpression of enzyme in Ashbya gossypii, use for production of riboflavin for human and animal feed supplement
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