Information on EC 2.6.1.2 - alanine transaminase

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

EC NUMBER
COMMENTARY
2.6.1.2
-
RECOMMENDED NAME
GeneOntology No.
alanine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
show the reaction diagram
ping pong bi bi mechanism
-
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
show the reaction diagram
ping pong type reaction
-
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
show the reaction diagram
ping pong bi bi mechanism
-
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
show the reaction diagram
ping pong bi bi mechanism
-
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
alanine biosynthesis II
-
alanine degradation II (to D-lactate)
-
alanine degradation III
-
Alanine, aspartate and glutamate metabolism
-
anaerobic energy metabolism (invertebrates, cytosol)
-
C4 photosynthetic carbon assimilation cycle, NAD-ME type
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
Carbon fixation in photosynthetic organisms
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
L-alanine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly instead of alanine.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AlaAT1
-
-
alanine aminotransferase
-
-
-
-
alanine aminotransferase
-
-
alanine aminotransferase
-
-
alanine aminotransferase
-
-
alanine aminotransferase-1
-
-
alanine transaminase
-
-
alanine-2-oxoglutarate aminotransferase
-
-
alanine-alpha-ketoglutarate aminotransferase
-
-
-
-
alanine-pyruvate aminotransferase
-
-
-
-
alanine: 2-oxoglutarate aminotransferase
-
-
ALAT
-
-
ALT
-
-
-
-
aminotransferase, alanine
-
-
-
-
beta-A:P TAm
-
-
beta-A:P TAm
Pseudomonas aeruginosa PAO2
-
-
-
beta-alanine aminotransferase
-
-
-
-
beta-alanine aminotransferase
-
-
beta-alanine: pyruvate transaminase
-
-
beta-alanine: pyruvate transaminase
Pseudomonas aeruginosa PAO2
-
-
-
Bh D-AlaAT
-
-
glutamate pyruvate 2-phosphotransferase
-
-
glutamate-pyruvate transaminase
-
-
glutamic acid-pyruvic acid transaminase
-
-
-
-
glutamic-alanine transaminase
-
-
-
-
glutamic-pyruvic aminotransferase
-
-
-
-
glutamic-pyruvic transaminase
-
-
-
-
GmAlaAT
-
-
GPT
-
-
-
-
HvAlaAT
P52894
-
L-alanine aminotransferase
-
-
-
-
L-alanine transaminase
-
-
-
-
OsAlaAT
-
-
Pp beta-AlaAT
-
-
pyruvate transaminase
-
-
-
-
pyruvate-alanine aminotransferase
-
-
-
-
pyruvate-glutamate transaminase
-
-
-
-
ZmAlaAT1
-
-
ZmAlaAT2
-
-
L-alanine-alpha-ketoglutarate aminotransferase
-
-
-
-
additional information
-
formerly known as glutamate pyruvate transaminase (GPT)
CAS REGISTRY NUMBER
COMMENTARY
9000-86-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cultivar Bugang
-
-
Manually annotated by BRENDA team
; HIV/HCV co-infected patients
-
-
Manually annotated by BRENDA team
hepatitis C patients
-
-
Manually annotated by BRENDA team
high alanine aminotransferase activity is a marker of risk for type 2 diabetis
-
-
Manually annotated by BRENDA team
isoform Alt1; isoform Alt2
-
-
Manually annotated by BRENDA team
recombinant protein
-
-
Manually annotated by BRENDA team
4 isoforms
-
-
Manually annotated by BRENDA team
soil fungus
-
-
Manually annotated by BRENDA team
isoform Pyd4, involved in both beta-alanine and gamma-aminobutanoic acid transamination
UniProt
Manually annotated by BRENDA team
Leptosphaeria michotii
fungi
-
-
Manually annotated by BRENDA team
six isoforms with different pH-optima
-
-
Manually annotated by BRENDA team
strain PAO1, encoded in the dadRAX locus
-
-
Manually annotated by BRENDA team
strain PAO2
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PAO2
strain PAO2
-
-
Manually annotated by BRENDA team
7 days old
-
-
Manually annotated by BRENDA team
male animals, under starvation, isoforms AlaAT I and AlaAT II
-
-
Manually annotated by BRENDA team
Sprague-Dawley female rats
-
-
Manually annotated by BRENDA team
mollusca: bivalvia
-
-
Manually annotated by BRENDA team
tomato, 2 alanine aminotransferases, soluble and Triton X-100 extractable
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + 5-aminopentanoate
glutamate + 5-oxopentanoate
show the reaction diagram
-
121% of the activity with beta-alanine
-
?
2-oxoglutarate + 6-aminohexanoate
glutamate + 6-oxohexanoate
show the reaction diagram
-
8% of the activity with beta-alanine
-
?
2-oxoglutarate + DL-3-aminoisobutanoate
glutamate + 3-oxoisobutanoate
show the reaction diagram
-
51% of the activity with beta-alanine
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + glutamate
show the reaction diagram
-
at 131% of the activity with beta-alanine
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
A5H0J5, -
-
-
-
?
aspartate + 2-oxoglutarate
malate + L-glutamate
show the reaction diagram
-, Q9P9M8
14% of activity with glutamate and pyruvate
-
?
aspartate + pyruvate
malate + alanine
show the reaction diagram
-, Q9P9M8
10% of activity with alanine and 2-oxoglutarate
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
A5H0J5, -
-
-
-
?
beta-alanine + glyoxylic acid
malonic semialdehyde + glycine
show the reaction diagram
-
7% of the activity with 2-oxoglutarate
-
?
beta-alanine + pyruvate
malonic semialdehyde + alanine
show the reaction diagram
-
1% of the activity with 2-oxoglutarate
-
?
DL-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
DL-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
-
DL-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
63-70% of the activity with L-alanine
-
-
?
DL-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
63% specific activity compared to L-alanine
-
-
?
glycine + 2-oxoglutarate
glyoxylate + glutamate
show the reaction diagram
-
24% of activity with DL-alanine
-
?
glyoxylate + alanine
glycine + pyruvate
show the reaction diagram
-
-
-
?
glyoxylate + alanine
glycine + pyruvate
show the reaction diagram
-
70% of activity with glutamate
-
ir
glyoxylate + glutamate
glycine + 2-oxoglutarate
show the reaction diagram
-
-
-
?
glyoxylate + glutamate
glycine + 2-oxoglutarate
show the reaction diagram
-
-
-
ir
glyoxylate + glutamine
glycine + 2-oxosuccinamate
show the reaction diagram
-
42% of activity with glutamate
-
?
glyoxylate + methionine
glycine + 4-methylsulfanyl-2-oxobutanoate
show the reaction diagram
-
37% of activity with glutamate
-
?
L-alanine + 2-oxobutyrate
pyruvate + 2-aminobutanoate
show the reaction diagram
-
10.2% of the activity with 2-oxoglutarate
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?, r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-, Q9P9M8
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
P52894
-
-
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
with 2-oxoglutarate specific for L-alanine
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
highly specific for alanine and 2-oxoglutarate
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
highly specific for alanine and 2-oxoglutarate
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
rate of the forward reaction is 4 times higher than the rate of the reverse reaction, no activity with aspartate, glycine, threonine, leucine, methionine, arginine, phenylalanine, tyrosine, tryptophan, glyoxylate and 2-oxo-3-methylvalerate
-
r
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
Leptosphaeria michotii
-
no activity with L-aspartate, cysteine sulfinate, 2-aminobutanoate and cyclic amino acids
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
glutamate-glyoxylate aminotransferase is identical with alanine-2-oxoglutarate aminotransferase
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
D-alanine at 2% of the activity with L-alanine
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
cannot use glyoxylate as keto donor
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
important function in beta-alanine metabolism
-
-
-
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
mitochondrial isoenzyme shows higher affinity for L-alanine, mainly functions in the direction of conversion of alanine to pyruvate whereas the cytosolic isoenzyme would function in both directions
-
-
-
L-alanine + glyoxylate
pyruvate + L-glycine
show the reaction diagram
-
-
-
-
ir
L-aspartate + 2-oxoglutarate
2-oxobutan-1,4-dioate + L-glutamate
show the reaction diagram
-
6-8% of the activity with L-alanine
-
-
?
L-aspartate + 2-oxoglutarate
2-oxobutan-1,4-dioate + L-glutamate
show the reaction diagram
-
6% specific activity compared to L-alanine
-
-
?
L-erythrulose + ?
2-amino-1,3,4-butanetriol + ?
show the reaction diagram
-
-
-
-
?
L-glutamate + 2-oxobutyrate
2-oxoglutarate + 2-aminobutanoate
show the reaction diagram
-
32.4% of the activity with pyruvate
-
?
L-leucine + 2-oxoglutarate
2-oxo-4-methylpentanoate + L-glutamate
show the reaction diagram
-
8% of the activity with L-alanine
-
-
?
L-leucine + 2-oxoglutarate
2-oxo-4-methylpentanoate + L-glutamate
show the reaction diagram
-
9% specific activity compared to L-alanine
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
75% of activity with DL-alanine
-
?
L-methylbenzylamine + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
L-tyrosine + 2-oxoglutarate
(4-hydroxyphenyl)pyruvate + L-glutamate
show the reaction diagram
-
12.5% specific activity compared to L-alanine
-
-
?
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
show the reaction diagram
P52894
-
-
-
r
serine + 2-oxoglutarate
3-hydroxy-2-oxopropanoate + glutamate
show the reaction diagram
-
22% of activity with DL-alanine
-
?
tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + glutamate
show the reaction diagram
-
36.5% of activity with DL-alanine
-
?
L-tyrosine + 2-oxoglutarate
2-deamino-2-oxotyrosine + L-glutamate
show the reaction diagram
-
12-14% of the activity with L-alanine
-
-
?
additional information
?
-
-
no specificity for L-glutamate, L-cysteine, L-glycine, L-methionine, L-isoleucine, L-threonine, L-valine, L-histidine, beta-alanine, L-arginine hydrochloride, L-cysteine hydrochloride, L-hydroxyproline, DL-phenylalanine, DL-threonine, DL-aspartate, DL-isoleucine, DL-tryptophan, DL-norleucine, DL-histidine hydrochloride, DL-homocysteine, L-beta-phenylalanine
-
-
-
additional information
?
-
-
phenylserine, phenylaminopropanol, phenylaminopropandiol, ethylbenzylamine, and phenylglycinol are not accepted as substrates
-
-
-
additional information
?
-
-
the acetylpolyamine amidohydrolase regulator alanine transaminase and racemase coupled with SpuC, the major putrescine-pyruvate transaminase, are key components to maintaining alanine homeostasis. The alanine-pyruvate cycle is indispensable for polyamine utilization, corresponding mutant strains are severely hampered in polyamine utilization, overview
-
-
-
additional information
?
-
P52894
enzyme is also able to utilize aspartate and oxaloacetate with 10% efficiency as compared to the native substrates
-
-
-
additional information
?
-
Pseudomonas aeruginosa PAO2
-
phenylserine, phenylaminopropanol, phenylaminopropandiol, ethylbenzylamine, and phenylglycinol are not accepted as substrates
-
-
-
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 + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
important function in beta-alanine metabolism
-
-
-
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
-
mitochondrial isoenzyme shows higher affinity for L-alanine, mainly functions in the direction of conversion of alanine to pyruvate whereas the cytosolic isoenzyme would function in both directions
-
-
-
additional information
?
-
-
the acetylpolyamine amidohydrolase regulator alanine transaminase and racemase coupled with SpuC, the major putrescine-pyruvate transaminase, are key components to maintaining alanine homeostasis. The alanine-pyruvate cycle is indispensable for polyamine utilization, corresponding mutant strains are severely hampered in polyamine utilization, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein, 2 mol pyridoxal phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
a pyridoxal phosphate protein, 2 mol pyridoxal phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
1 mol of pyridoxal 5'-phosphate per mol of dimer
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
activates the enzyme with a Km of 0.057 mM
pyridoxal 5'-phosphate
-
2 mM, required
pyridoxal 5'-phosphate
A5H0J5, -
required
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
additional information
-
anaerobically induced isoform does not require the presence of pyridoxal 5'-phosphate to retain its activity
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
2 mM, 51% inhibition
2-oxoglutarate
-
substrate inhibition at neutral pH, not seen at pH 8.8
3-chloro-L-alanine
-
0.1 mM, 78% inhibition
4-hydroxymercuribenzoate
-
-
6-Azauracil
-
1.5 mM, 50% inhibition
acarbose
-
0.1% acarbose fed to diabetic mice induces a decrease of the catalytic activity to 69.6%
Aminooxyacetate
-
0.0004 mM, 85% inhibition of mitochondrial alanine aminotransferase
Aminooxyacetate
-
1 mM, complete inhibition
Aminooxyacetate
-
2 mM, complete inhibition
Aminooxyacetate
-
1 mM, 98% inhibition
Aminooxyacetate
-
competitive to L-alanine, uncompetitive to 2-oxoglutarate
Aminooxyacetate
-
complete inhibition, both isoforms
aminooxyacetic acid
-
2.5 mM, complete inhibition
Cd2+
-
0.1 mM, complete inhibition
Cd2+
-
0.2 mM, 39% inhibition of alanine aminotransferase activity measured in soft body and gills, 0.6 mM, 46% inhibition
Citric acid
-
-
Cu2+
-
reversed by L-cysteine and pyridoxal phosphate
Cu2+
-
inhibition of alanine aminotransferase activity in gills
Cycloserine
-
1 mM, 10 mM, 50 mM, 10%, 52% and 100% inhibition respectively
Cycloserine
-
0.1 mM, 98% inhibition
Cycloserine
P52894
-
D-alanine
-
competitive vs. L-alanine
Fumaric acid
-
-
Glutarate
-
10 mM, 94% inhibition
Glutarate
-
about 70% inhibition, both isoforms
Glutarate
-
2.5 mM, 69% inhibition
Hg2+
-
93% inhibition
Hg2+
-
0.1 mM, 81% inhibition
HgCl2
-
almost complete inhibition, both isoforms
HgCl2
-
2.5 mM, 96% inhibition
hydroxylamine
-
activity recovered by pyridoxal 5'-phosphate
hydroxylamine
-
1 mM, 96% inhibition
hydroxylamine
-
2 mM, 96% inhibition
hydroxylamine
-
2 mM, 73% inhibition
hydroxylamine
-
complete inhibition, both isoforms
hydroxylamine
-
2.5 mM, complete inhibition
Isonicotinic hydrazide
-
-
L-ascorbic acid
-
2 mM, 25% inhibition
malate
-
5 mM, 25% inhibition
Maleate
-
about 70% inhibition, both isoforms
-
Maleate
-
2.5 mM, 70% inhibition
-
O-carboxy-methyl hydroxylamine hemihydrochloride
P52894
-
-
O-carboxy-methyl hydroxylamine hemihydrochloride
-
-
-
o-phenanthroline
-
weak
oxalic acid
-
-
p-chloromercuribenzoate
-
reactivation by dithiothreitol
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
1 mM, complete inhibition
p-hydroxymercuribenzoate
-
; 1 mM, 87% inhibition
p-hydroxymercuribenzoate
-
0.1 mM, 72% inhibition
p-hydroxymercuribenzoate
-
complete inhibition, both isoforms
p-hydroxymercuribenzoate
-
2.5 mM, complete inhibition
Pb2+
-
reversed by L-cysteine and pyridoxal phosphate
Pb2+
-
0.7 mM, 58% inhibition of alanine aminotransferase activity measured in soft body, 0.35 mM, 32% inhibition
Phenelzine
-
monoamine oxidase inhibitor used as antidepressant/antipanic drug, maximum inhibition, i.e. 32%, of brain alanine aminotransferase at 15 mg/kg
phenylhydrazine
-
-
Semicarbazide
-
1 mM, 40% inhibition
Semicarbazide
-
10 mM, 97% inhibition
succinate
-
competitive inhibitor
vigabatrin
-
structural analogue to gamma-amino butyric acid, anti-epilepsy drug, 1 mM, approx. 80% inhibition in vitro, in vivo alanine aminotransferase activity is reduced 30-40% 1-2h after administration
Zn2+
-
1 mM, 75% inhibition
Maleic acid
-
-
additional information
-
not inhibited by 6-azauridine or 6-azauridine 5'-phosphate
-
additional information
-
not inhibited by EDTA, o-phenanthroline and L-ascorbate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NH4+
-
ammonium as nitrogen source induces both gene expression and enzyme activity of AlaAT
additional information
-
an 1.5fold increase in enzyme activity is detected under hypoxic conditions
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0058
-
2-oxoglutarate
-
pH 7.5, 35C
0.028
-
2-oxoglutarate
-
pH 7.5, 22C, isoenzyme 3
0.05
-
2-oxoglutarate
-
pH 7.3, 40C
0.05
-
2-oxoglutarate
-
25C, pH 8.0
0.09
-
2-oxoglutarate
-
pH 7.5, 22C, isoenzyme 2
0.12
-
2-oxoglutarate
-
200 mM L-alanine and 2 mM 2-oxoglutarate in 0.1 M phosphate buffer, pH 7.4, at 37C
0.15
-
2-oxoglutarate
-
pH 7.5, 25C
0.19
-
2-oxoglutarate
-
pH 7.8, 30C, mitochondrial enzyme
0.19
-
2-oxoglutarate
-
AlaAT1, pH 7.3, 25C
0.2
-
2-oxoglutarate
Leptosphaeria michotii
-
-
0.22
-
2-oxoglutarate
-
pH 7.8, 30C, cytosolic enzyme
0.23
-
2-oxoglutarate
-
-
0.25
-
2-oxoglutarate
-
25C, pH 8.0
0.28
-
2-oxoglutarate
-
pH 7.25, 37C
0.29
-
2-oxoglutarate
-
pH 7.4, 25C
0.3
-
2-oxoglutarate
-
pH 7.5, 22C, isoenzyme 2
0.3
-
2-oxoglutarate
P52894
25C, pH 8.0
0.32
-
2-oxoglutarate
-
25C, pH 8.0
0.33
-
2-oxoglutarate
-
pH 7.4, 25C
0.35
-
2-oxoglutarate
-
AlaAT2, pH 7.3, 25C
0.37
-
2-oxoglutarate
-
pH 7.5, 25C
0.37
-
2-oxoglutarate
-
25C, pH 8.0
0.4
-
2-oxoglutarate
-
pH 7.8, 30C, mitochondrial alanine aminotransferase
0.45
-
2-oxoglutarate
-
pH 7.3, 37C
0.54
-
2-oxoglutarate
-
pH 8.8, 37C
0.7
-
2-oxoglutarate
-
pH 7.5, mitochondrial and cytosolic alanine aminotransferase
0.9
-
2-oxoglutarate
-, Q9P9M8
pH 7.2, 80C, native enzyme
1.1
-
2-oxoglutarate
-, Q9P9M8
pH 7.2, 80C, recombinant enzyme
1.4
-
2-oxoglutarate
-
pH 8.8, 37C, cosubstrate beta-alanine
1.6
-
2-oxoglutarate
-
-
1.85
-
2-oxoglutarate
-
pH 8.6, 37C
2.1
-
2-oxoglutarate
A5H0J5, -
pH 8.0, 30C
5
-
2-oxoglutarate
-
pH 8.0, 23C
0.51
-
4-aminobutanoate
-
pH 8.8, 37C, cosubstrate 2-oxoglutarate
0.25
-
alanine
-
pH 7.5, 22C, isoenzyme 1
2
-
alanine
-
pH 7.8, 30C, mitochondrial alanine aminotransferase
2.8
-
alanine
-
pH 7.25, 37C
2.8
-
alanine
-, Q9P9M8
pH 7.2, 80C, native enzyme
3
-
alanine
-
pH 7.5, 22C, isoenzyme 2
3.1
-
alanine
-
pH 7.5, 22C, isoenzyme 3
6.2
-
alanine
-
-
6.67
-
alanine
-
pH 7.5, 25C
17
-
alanine
-
pH 8.0, 23C
21
-
alanine
-
pH 7.8, 30C, cytosolic enzyme
3.9
-
beta-Alanine
-
pH 8.8, 37C, cosubstrate 2-oxoglutarate
7.6
-
beta-Alanine
A5H0J5, -
; pH 8.0, 30C
8.3
-
DL-alanine
-
pH 8.6, 37C
0.55
-
glutamate
-
pH 7.5, 22C, isoenzyme 1
0.8
-
glutamate
-
pH 7.5, 22C, isoenzyme 3
1
-
glutamate
-
pH 8.0, 23C
1.15
-
glutamate
-
pH 7.5, 22C, isoenzyme 2
2.3
-
glutamate
-
pH 7.25, 37C
4.3
-
glutamate
-
pH 7.5, cytosolic alanine aminotransferase
4.3
-
glutamate
-, Q9P9M8
pH 7.2, 80C, native enzyme
4.7
-
glutamate
-, Q9P9M8
pH 7.2, 80C, recombinant enzyme
5
-
glutamate
-
pH 7.5, 25C
15
-
glutamate
-
pH 7.3, 37C
32
-
glutamate
-
pH 7.8, 30C, mitochondrial alanine aminotransferase
0.9
-
glyoxylate
-
pH and temperature not specified in the publication
0.21
-
L-alanine
-
25C, pH 8.0
0.4
-
L-alanine
-
25C, pH 8.0
0.51
-
L-alanine
-
200 mM L-alanine and 2 mM 2-oxoglutarate in 0.1 M phosphate buffer, pH 7.4, at 37C
0.59
-
L-alanine
-
pH 7.5, 35C
0.62
-
L-alanine
-
25C, pH 8.0
1.5
2
L-alanine
-
25C, pH 8.0
2.6
-
L-alanine
-
pH 7.5, 25C
2.7
-
L-alanine
-
pH 7.3, 40C
3.06
-
L-alanine
-
25C, pH 8.0
3.2
-
L-alanine
-, Q9P9M8
pH 7.2, 80C, recombinant enzyme
3.6
-
L-alanine
-
25C, pH 8.0
3.8
-
L-alanine
P52894
25C, pH 8.0
5.1
-
L-alanine
-
pH 7.5, mitochondrial alanine aminotransferase
5.1
-
L-alanine
-
pH 7.8, 30C, mitochondrial enzyme
5.15
-
L-alanine
-
25C, pH 8.0
6.05
-
L-alanine
-
AlaAT1, pH 7.3, 25C
6.85
-
L-alanine
Leptosphaeria michotii
-
-
6.9
-
L-alanine
-
AlaAT2, pH 7.3, 25C
8.1
-
L-alanine
-
pH and temperature not specified in the publication
8.2
-
L-alanine
-
pH 7.3, 37C
10.12
-
L-alanine
-
pH 7.4, 37C
18.5
-
L-alanine
-
pH 7.4, 25C
19.05
-
L-alanine
-
-
23.55
-
L-alanine
-
pH 7.4, 25C
30.3
-
L-alanine
-
pH 7.5, cytosolic alanine aminotransferase
0.2
-
L-glutamate
-
25C, pH 8.0
0.24
-
L-glutamate
-
25C, pH 8.0
0.44
-
L-glutamate
-
25C, pH 8.0
0.52
-
L-glutamate
-
pH 7.3, 40C
0.55
-
L-glutamate
-
25C, pH 8.0
0.56
-
L-glutamate
-
25C, pH 8.0
0.57
-
L-glutamate
-
25C, pH 8.0
0.68
-
L-glutamate
-
25C, pH 8.0
0.8
-
L-glutamate
P52894
25C, pH 8.0
3.22
-
L-glutamate
-
pH 7.4, 37C
6.25
-
L-glutamate
-
AlaAT1, pH 7.3, 25C
6.3
-
L-glutamate
-
pH 7.5, 25C
6.6
-
L-glutamate
-
pH 7.5, mitochondrial alanine aminotransferase
6.66
-
L-glutamate
-
AlaAT2, pH 7.3, 25C
0.022
-
pyruvate
-
pH 7.5, 22C, isoenzyme 3
0.04
-
pyruvate
-
pH 7.5, 22C, isoenzyme 2
0.06
-
pyruvate
-
pH 8.0, 23C
0.09
-
pyruvate
-
pH 7.25, 37C
0.11
-
pyruvate
-
25C, pH 8.0
0.16
-
pyruvate
-
pH 7.5, 25C
0.2
-
pyruvate
P52894
25C, pH 8.0
0.2
-
pyruvate
-
25C, pH 8.0
0.22
-
pyruvate
-
AlaAT1, pH 7.3, 25C
0.24
-
pyruvate
-
pH 7.3, 40C
0.29
-
pyruvate
-
AlaAT2, pH 7.3, 25C
0.33
-
pyruvate
-
pH 7.5, 25C
0.4
-
pyruvate
-
pH 7.5 mitochondrial alanine aminotransferase
0.4
-
pyruvate
-
pH 7.8, 30C, mitochondrial alanine aminotransferase
0.4
-
pyruvate
-
25C, pH 8.0
0.42
-
pyruvate
-
25C, pH 8.0
0.45
-
pyruvate
-
pH 7.5, 22C, isoenzyme 1
0.5
-
pyruvate
-
pH 7.5, cytosolic alanine aminotransferase
0.54
-
pyruvate
-
25C, pH 8.0
0.87
-
pyruvate
-
pH 7.3, 37C
5.4
-
pyruvate
-, Q9P9M8
pH 7.2, 80C, native enzyme
5.6
-
pyruvate
-, Q9P9M8
pH 7.2, 80C, recombinant enzyme
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.08
-
2-oxoglutarate
-
cofactor: L-alanine, 25C, pH 8.0
0.33
-
2-oxoglutarate
-
cofactor: L-alanine, 25C, pH 8.0
0.38
-
2-oxoglutarate
-
cofactor: L-alanine, 25C, pH 8.0
1.25
-
2-oxoglutarate
-
cofactor: L-alanine, 25C, pH 8.0
4.98
-
2-oxoglutarate
-
cofactor: L-alanine, 25C, pH 8.0
5.49
-
2-oxoglutarate
-
cofactor: L-alanine, 25C, pH 8.0
6.09
-
2-oxoglutarate
-
cofactor: L-alanine, 25C, pH 8.0
12.11
-
2-oxoglutarate
P52894
cofactor: L-alanine, 25C, pH 8.0
134.9
-
2-oxoglutarate
-
AlaAT1, cosubstrate: L-alanine, pH 7.3, 25C
170
-
2-oxoglutarate
-
AlaAT2, cosubstrate: L-alanine, pH 7.3, 25C
0.08
-
L-alanine
-
cofactor: 2-oxoglutarate, 25C, pH 8.0
0.33
-
L-alanine
-
cofactor: 2-oxoglutarate, 25C, pH 8.0
0.38
-
L-alanine
-
cofactor: 2-oxoglutarate, 25C, pH 8.0
1.25
-
L-alanine
-
cofactor: 2-oxoglutarate, 25C, pH 8.0
4.98
-
L-alanine
-
cofactor: 2-oxoglutarate, 25C, pH 8.0
5.49
-
L-alanine
-
cofactor: 2-oxoglutarate, 25C, pH 8.0
6.09
-
L-alanine
-
cofactor: 2-oxoglutarate, 25C, pH 8.0
12.11
-
L-alanine
P52894
cofactor: 2-oxoglutarate, 25C, pH 8.0
17.1
-
L-alanine
-
200 mM L-alanine and 2 mM 2-oxoglutarate in 0.1 M phosphate buffer, pH 7.4, at 37C
134.9
-
L-alanine
-
AlaAT1, cosubstrate: 2-oxoglutarate, pH 7.3, 25C
170
-
L-alanine
-
AlaAT2, cosubstrate: 2-oxoglutarate, pH 7.3, 25C
0.17
-
L-glutamate
-
cofactor: pyruvate, 25C, pH 8.0
0.67
-
L-glutamate
-
cofactor: pyruvate, 25C, pH 8.0
2.8
-
L-glutamate
-
cofactor: pyruvate, 25C, pH 8.0
3.06
-
L-glutamate
-
cofactor: pyruvate, 25C, pH 8.0
6.56
-
L-glutamate
-
cofactor: pyruvate, 25C, pH 8.0
6.86
-
L-glutamate
-
cofactor: pyruvate, 25C, pH 8.0
8.64
-
L-glutamate
-
cofactor: pyruvate, 25C, pH 8.0
25.62
-
L-glutamate
P52894
cofactor: pyruvate, 25C, pH 8.0
127.7
-
L-glutamate
-
AlaAT1, cosubstrate: pyruvate, pH 7.3, 25C
136
-
L-glutamate
-
AlaAT2, cosubstrate: pyruvate, pH 7.3, 25C
0.17
-
pyruvate
-
cofactor: L-glutamate, 25C, pH 8.0
0.67
-
pyruvate
-
cofactor: L-glutamate, 25C, pH 8.0
2.8
-
pyruvate
-
cofactor: L-glutamate, 25C, pH 8.0
3.06
-
pyruvate
-
cofactor: L-glutamate, 25C, pH 8.0
6.56
-
pyruvate
-
cofactor: L-glutamate, 25C, pH 8.0
6.86
-
pyruvate
-
cofactor: L-glutamate, 25C, pH 8.0
8.64
-
pyruvate
-
cofactor: L-glutamate, 25C, pH 8.0
25.62
-
pyruvate
P52894
cofactor: L-glutamate, 25C, pH 8.0
127.7
-
pyruvate
-
AlaAT1, cosubstrate: L-glutamate, pH 7.3, 25C
136
-
pyruvate
-
AlaAT2, cosubstrate: L-glutamate, pH 7.3, 25C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
22290
-
2-oxoglutarate
-
AlaAT1, cosubstrate: L-alanine, pH 7.3, 25C
2883
24640
-
2-oxoglutarate
-
AlaAT2, cosubstrate: L-alanine, pH 7.3, 25C
2883
22290
-
L-alanine
-
AlaAT1, cosubstrate: 2-oxoglutarate, pH 7.3, 25C
12048
24640
-
L-alanine
-
AlaAT2, cosubstrate: 2-oxoglutarate, pH 7.3, 25C
12048
19630
-
L-glutamate
-
AlaAT1, cosubstrate: pyruvate, pH 7.3, 25C
12211
20510
-
L-glutamate
-
AlaAT2, cosubstrate: pyruvate, pH 7.3, 25C
12211
19630
-
pyruvate
-
AlaAT1, cosubstrate: L-glutamate, pH 7.3, 25C
16065
20510
-
pyruvate
-
AlaAT2, cosubstrate: L-glutamate, pH 7.3, 25C
16065
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00034
-
Aminooxyacetate
-
pH 7.4, 25C
0.00064
-
Aminooxyacetate
-
pH 7.4, 25C
17
-
succinate
-
pH 8.6, 37C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.119
-
Cycloserine
P52894
25C, pH 8.0
0.0069
-
O-carboxy-methyl hydroxylamine hemihydrochloride
P52894
25C, pH 8.0
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.12
-
-
enzyme from cell lysate
0.75
-
A5H0J5, -
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30C
1.39
-
-
-
1.6
-
A5H0J5, -
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
3.52
-
A5H0J5, -
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30C
3.55
-
-
-
4
-
-
25C
4.5
-
A5H0J5, -
substrate beta-alanine, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
30.58
-
-
isoform AlaAT I
43.3
-
-
isoform AlaAT II
50
-
-
pH 7.4, 25C
60.2
-
-
25C
89.5
-
-
pH 7.4, 25C
127.5
-
-
-
156
-
-
reverse reaction
158
-
-, Q9P9M8
native enzyme
213
-
-
-
229.8
-
-
after purification
243
-
-, Q9P9M8
recombinant enzyme
360
-
Leptosphaeria michotii
-
-
594
-
-
forward reaction
2231
-
-
-
additional information
-
-
372 units/mg
additional information
-
-
11.2 units/ml
additional information
-
-
upon waterlogging-induced hypoxia, AlaAT activity increases strongly. Concomitantly, alanine accumulates. During re-oxygenation, AlaAT activity remains high, but the transcript level and the alanine content decreases
additional information
-
-
specific activities of AlaAT is lowest in shoots of etiolated seedlings and increased in plants exposed to light; specific activity of AlaAT increases steadily upon hypoxia
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
forward and reverse reaction
6.5
7.8
-, Q9P9M8
native and recombinant enzyme
6.5
-
-
-
7
-
-
isoform in eggs, and larva
7.3
-
-
assay at
7.4
-
-
in phosphate buffer
7.4
-
-
isoform in eggs
7.4
-
-
assay at
7.5
8.5
-
-
7.5
-
Leptosphaeria michotii
-
-
7.5
-
-
-
7.5
-
-
assay at
7.6
-
-
-
7.6
-
-
isoform in larvae
7.8
-
-
-
7.8
-
-
isoform in eggs
8
8.3
-
with alanine and 2-oxoglutarate
8
-
-
isoform in larvae
8
-
A5H0J5, -
;
8.2
-
-
isoform in eggs
8.3
-
-
in borate buffer
8.6
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
9.5
-
active over whole range
5.5
8.2
-, Q9P9M8
native and recombinant enzyme
5.5
9.5
-
approx. 70% of maximal activity at pH 5.5, approx. 50% of maximal activity at pH 9.5
6.3
7.8
-
approx. 40% of maximal activity at pH 6.3, 75% of maximal activity at pH 6.8
6.4
8.7
-
at least 50% of maximal activity at pH 6.4 and 8.7
6.5
8
-
almost full activity within this range
7
7.5
-
rapid decrease of activity below pH 7 and above pH 7.5
7
9
A5H0J5, -
more than 70% of maximum activity
7.9
8.4
-
highest activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
35
-
-
-
37
-
-
assay at
37
-
-
assay at
additional information
-
-, Q9P9M8
above 95C, native and recombinant enzyme
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
55
-
strong decrease above
30
95
-, Q9P9M8
native and recombinant enzyme
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.2
-
-
isoform AlaAT I, isoelectric focusing
4.2
-
-
isoelectrofocusing
5.3
-
-
isoform AlaAT II, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
three isoforms with different pH-optima
Manually annotated by BRENDA team
-
highest activity, two isoforms with different pH-optima
Manually annotated by BRENDA team
-
cytosolic enzyme
Manually annotated by BRENDA team
-
increase in alanine aminotransferase activity during lactation and weaning when compared to virgin rats
Manually annotated by BRENDA team
-
sceletal muscle
Manually annotated by BRENDA team
-
mitochondrial enzyme
Manually annotated by BRENDA team
-
highest expression found. Under normal conditions: lowest activity
Manually annotated by BRENDA team
-
highest expression found
Manually annotated by BRENDA team
-
mitochondrial enzyme
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17700
-
-
SDS-PAGE
18300
-
-
gel filtration
18370
-
-
isoform AlaAT I, gel filtration
53000
-
-
enzyme containing a His- and a T5-tag, SDS-PAGE
54820
-
-
calculated from sequence of cDNA
55100
-
-
LC mass spectrometry
57900
-
-
SDS-PAGE
61300
-
-
SDS-PAGE
69000
-
-
-
69000
-
-
gel filtration, 1.5fold larger than single peptide mass, indicating that the enzyme is a monomer or homodimer
80000
-
-
gel filtration
92000
-
-
-
93400
-
-, Q9P9M8
gel filtration
95000
-
-
gel filtration
95000
-
-
gel filtration
97000
-
-
gel filtration
99000
-
-
gel filtration
100000
-
-
gel filtration
101000
-
-
SDS-PAGE
102000
-
-
gel filtration
105000
-
-
gel filtration
110000
-
Leptosphaeria michotii
-
-
111000
-
A5H0J5, -
gel filtration; PAGE
112000
118000
-
gel filtration
112000
-
-
sucrose density gradient centrifugation
114800
-
-
isoform AlaAT II, gel filtration
115000
-
-
gel filtration
118000
-
-
sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 54000 + x * 56000, SDS-PAGE
?
-
x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
dimer
Leptosphaeria michotii
-
-
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-, Q9P9M8
2 * 46000, SDS-PAGE
dimer
A5H0J5, -
2 * 55500, gel filtration; 2 * 56000, SDS-PAGE
monomer
-
1 * 75000, SDS-PAGE
monomer
-
x * 17700, isoform AlaAT I, x * 112200, isoform AlaAT II, SDS-PAGE
monomer
-
1 * 65000
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HvAlaAT is crystallized in complex with pyridoxal 5'-phosphate and L-cycloserine. Structure of this complex is solved at 2.7 A resolution
P52894
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
strong loss of activity below
7
9
A5H0J5, -
70% of activity remaining at pH values of 7 and 9
7.5
-
-
40C, 30 min, 50% loss of activity
8.5
9.5
-
more stable at alkaline pH than at neutral pH
9
-
-
40C, 30 min, 5% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
isoenzymes 2 and 3, 10-20% loss of activity after 3 h
40
-
-
30 min, 50% loss of activity at pH 7.5, 5% loss of activity at pH 9.0
50
-
-
quickly inactivated, 100 mM alanine gives slight protection
50
-
-
50% loss of activity after 10 min
60
-
-
more than 85% loss of activity after 5 min
additional information
-
-
pyridoxal 5-phosphate, L-alanine or 2-oxoglutarate protect against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pyridoxal 5'-phosphate, L-alanine or 2-oxoglutarate protects against heat inactivation
-
during the purification procedure the enzyme needs protective substances, i.e. glycerol, 2-mercaptoethanol and alanine
-
uneffected by repeated freezing and thawing
-
enzyme does not tolerate freezing at any stage after sonication of the isolated mitochondria
-
K+ or L-alanine stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, stable for several h in solution
-
-20C, 20 mM Tris-HCl, pH 7.5, freezing is worse than storage at 4C or 25C
-
-80C, 20 mM Tris-HCl, pH 7.5, 20% loss of activity in first two days, thereafter stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
-
-80C, 20 mM Tris-HCl, pH 7.5, stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
-
25C, 20 mM Tris-HCl, pH 7.5, 56% loss of activity in first two days. Addition of 25% glycerol preserves most of the activity
-
25C, 20 mM Tris-HCl, pH 7.5, 80-90% residual activity after 10 days, 60% residual activity after 20 days. Addition of 25% glycerol preserves most of the activity
-
37C, 20 mM Tris-HCl, pH 7.5, 50% loss of activity in 24 h, and complete loss of activity within one week
-
37C, 20 mM Tris-HCl, pH 7.5, 72% loss of activity in first two days
-
4C, 20 mM Tris-HCl, pH 7.5, 53% loss of activity in first two days. Addition of 25% glycerol preserves most of the activity
-
4C, 20 mM Tris-HCl, pH 7.5, stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
-
-20C, 10% glycerol, half-life of 2 weeks
-
4C, 12 days, 57% residual activity
A5H0J5, -
-25C, 10 mM potassium phosphate, pH 7.5, 1 mM EDTA, 2 mM 2-mercaptoethanol, 0.04 mM pyridoxal 5'-phosphate, a few days, 50% loss of activity
-
4C, 80% saturated solution of ammonium sulfate, 10 days, 40% loss of activity
-
-20C, 50 mM potassium phosphate buffer, pH 7.5, 5 mM 2-mercaptoethanol, 5% glycerol, stable for at least 5 weeks
-
0-5C, 50 mM potassium phosphate buffer, pH 7.5, 5 mM 2-mercaptoethanol, 5% glycerol, stable for 2 weeks
-
-20C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate, DEAE-cellulose, 3 isoforms
-
ammonium sulfate, Sephadex G-150, DEAE-Sephadex, partial purification
-
DEAE-Sephadex
-
HisTrap HP column chromatography
-
Ni2+-NTA agarose resin chromatography and Poly-Prep mini-column chromatography
-
ammonium sulfate, DEAE-Sepharose, partial purification of cytosolic and mitochondrial isoenzymes
-
recombinant enzyme
-
anaerobically induced isoform, ammonium sulfate, gel filtration, Q-Sepharose, Mono P, Mono Q
-
using a DE52 column, butyl-Toyopearl column, DEAE-Toyopearl column, CHT ceramic hydroxyapatite column and MonoQ column
-
partial
-
Sepharose S12 gel filtration and nickel-chelating Sepharose column chromatography
A5H0J5, -
-
Leptosphaeria michotii
-
Dowex 50WX8 200-400 mesh chromatography
-
heat treatment, ammonium sulfate, DEAE-Sepharose, hydroxylapatite, Sephacryl S-200
-
2 minor forms: AlaAT-1, AlaAT-3, 1 major form, AlaAT-2, ammonium sulfate, DEAE-cellulose, Sephacryl S-200, phenyl-Sepharose
-
native enzyme, Q-Sepharose, phenyl-Sepharose, hydroxyapatite, S-Sepharose, Mono Q, Superdex 200, recombinant enzyme, heat treatment, Mono Q
-, Q9P9M8
heat treatment, ammonium sulfate, DEAE-cellulose, isoelectric focusing, Sephadex G-150, hydroxylapatite, DEAE-cellulose
-
Sephadex G-150 column chromatography, DEAE-Sephadex A-25 column chromatography, and hydroxyapatite column chromatography
-
ammonium sulfate, DEAE-Sephadex, Sephadex G-200, partial purification
-
Sephadex G-150, DEAE-cellulose, ammonium sulfate, isoelectric focusing
-
using anion exchange protein Pak Q 8HR column attached to HPLC system
-
using saline precipitation, gel filtration, preparative electrophoresis and anion exchange chromatography on protein-Pak Q 8HR column attached to HPLC
-
ammonium sulfate, hydroxylapatite, preparative electrophoresis
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
expression in Sf9 cell
-
expressed in Arabidopsis thaliana
-
expressed in Escherichia coli as a His-tagged fusion protein
P52894
expression as His-tagged protein
A5H0J5, -
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli strain BL21gold(DE3)
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
-, Q9P9M8
expressed in Escherichia coli as a His-tagged fusion protein
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium as nitrogen source induces both gene expression and enzyme activity of AlaAT
-
ethanol administration causes a 3-3.5fold increase in serum ALT levels in superoxide dismutase deficient mice compared with their pair-fed controls and with wild-type ethanol-fed mice
-
in response to temperature changes, AlaAT levels reach a peak after 12 h in 10C water and after 48 h in 30Cwater, in response to salinity changes, AlaAT levels peak after 120 h in both 25 psu water (hyposalinity) and 45 psu water (hypersalinity)
-
nitrogen deprivation results in reduced transcript levels for AlaAT. The effect is more pronounced for AlaAT1
-
hypoxia induces transcript levels for AlaAT1 but not AlaAT2. Hypoxia induces AlaAT1 earlier in roots than in shoots
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
electrochemical immunosensor system for enzyme with detection limit of 10 pg/ml and 26.3 nA/(ng/ml), application as indicator for hepatocellular damage
additional information
-
a mutant strain is severely hampered in polyamine utilization, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
treatment of HIV/HCV co-infected patients with pegylated interferon and ribavirin. At week 1, serum HCV RNA levels and changes in alanine aminotransferase levels relative to baseline can identify likely responders better than plasma ribavirin levels. During the first four weeks of treatment, median plasma ribavirin levels and area under the ribavirin curve are significantly lower in sustained responders compared with nonresponders
medicine
-
patients with hepatitis C treated with NS3-4A protease inhibitor telaprevir and/or peginterferon alpha-2a. Patients receiving telaprevir alone show a decrease in mean neopterin and alanine aminotransferase levels. Patients receiving peginterferon alpha-2a plus telaprevir or peginterferon alpha-2a plus placebo show an ioncrease in neopterin levels and decrease in alanine aminotransferase level, suggesting that treatment of chronic hepatitis C patients with an NS3-4A protease inhibitor ameliorates inflammation. Interferon-mediated immunomodulatory effects remain intact when interferon is combined with telaprevir
medicine
-
enzyme is an effective neuroprotectant against glutamate excitotoxicity. When exposure is limited to endogenously released glutamate, neuroprotection by enzyme is not dependent on added pyruvate