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Information on EC 2.6.1.2 - alanine transaminase
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2.6.1.2 alanine transaminaseIUBMB Comments
A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly instead of alanine.
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Word Map
- 2.6.1.2
-
alt
- bilirubin
- necrosis
-
hepatotoxicity
- creatinine
- cholesterol
- triglyceride
- urea
- fibrosis
- hepatocytes
- viral
- albumin
- cirrhosis
-
enrol
- superoxide
- diabetes
- malondialdehyde
- dismutase
- gsh
- platelet
-
virological
- bile
- steatosis
- wistar
- ccl4
- nafld
-
hepatoprotective
- sod
-
gamma-glutamyl
- transaminases
- acetaminophen
-
portal
- jaundice
- prothrombin
-
reperfusion
- steatohepatitis
- cholestasis
- gamma-glutamyltransferase
-
nonalcoholic
-
ccl4-induced
-
hbeag
-
tetrachloride
- seroconversion
- transpeptidase
- lamivudine
-
anti-hcv
- analysis
- medicine
- viremia
-
waist
- ribavirin
- agriculture
- synthesis
- tenofovir
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
AAT, AKT, AlaAT, AlaAT1, AlaAT2, alanine aminotransferase, alanine aminotransferase 1, alanine aminotransferase-1, alanine transaminase, alanine-2-oxoglutarate aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAT
AlaAT
AlaAT1
AlaAT2
alanine aminotransferase
alanine-alpha-ketoglutarate aminotransferase
-
-
-
-
alanine-pyruvate aminotransferase
-
-
-
-
ALT
ALT1
aminotransferase, alanine
-
-
-
-
beta-A:P TAm
beta-alanine aminotransferase
beta-alanine: pyruvate transaminase
c-AAT
glutamic acid-pyruvic acid transaminase
-
-
-
-
glutamic-alanine transaminase
-
-
-
-
glutamic-pyruvic aminotransferase
-
-
-
-
glutamic-pyruvic transaminase
-
-
-
-
GPT
L-alanine aminotransferase
-
-
-
-
L-alanine transaminase
-
-
-
-
L-alanine-alpha-ketoglutarate aminotransferase
-
-
-
-
pyruvate transaminase
-
-
-
-
pyruvate-alanine aminotransferase
-
-
-
-
pyruvate-glutamate transaminase
-
-
-
-
additional information
-
formerly known as glutamate pyruvate transaminase (GPT)
alanine aminotransferase
-
-
-
-
ALT
-
-
-
-
beta-alanine aminotransferase
-
-
-
-
GPT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
ping pong bi bi mechanism
-
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
ping pong bi bi mechanism
-
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
ping pong bi bi mechanism
-
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-alanine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly instead of alanine.
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CAS REGISTRY NUMBER
COMMENTARY
9000-86-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + 5-aminopentanoate
glutamate + 5-oxopentanoate
-
121% of the activity with beta-alanine
-
?
2-oxoglutarate + 6-aminohexanoate
glutamate + 6-oxohexanoate
-
8% of the activity with beta-alanine
-
?
2-oxoglutarate + DL-3-aminoisobutanoate
glutamate + 3-oxoisobutanoate
-
51% of the activity with beta-alanine
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + glutamate
-
at 131% of the activity with beta-alanine
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
aspartate + 2-oxoglutarate
malate + L-glutamate
14% of activity with glutamate and pyruvate
-
?
aspartate + pyruvate
malate + alanine
10% of activity with alanine and 2-oxoglutarate
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
?
beta-alanine + glyoxylic acid
malonic semialdehyde + glycine
-
7% of the activity with 2-oxoglutarate
-
?
beta-alanine + pyruvate
malonic semialdehyde + alanine
-
1% of the activity with 2-oxoglutarate
-
?
glycine + 2-oxoglutarate
glyoxylate + glutamate
-
24% of activity with DL-alanine
-
?
glyoxylate + glutamine
glycine + 2-oxosuccinamate
-
42% of activity with glutamate
-
?
glyoxylate + methionine
glycine + 4-methylsulfanyl-2-oxobutanoate
-
37% of activity with glutamate
-
?
L-alanine + 2-oxobutyrate
pyruvate + 2-aminobutanoate
-
10.2% of the activity with 2-oxoglutarate
-
?
L-alanine + glyoxylate
pyruvate + glycine
L-glutamate and L-alanine are by far the best amino-group donors
-
-
?
L-glutamate + 2-oxobutyrate
2-oxoglutarate + 2-aminobutanoate
-
32.4% of the activity with pyruvate
-
?
L-glutamate + glyoxylate
2-oxoglutaramate + glycine
L-glutamate and L-alanine are by far the best amino-group donors
-
-
?
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
-
75% of activity with DL-alanine
-
?
L-tyrosine + 2-oxoglutarate
(4-hydroxyphenyl)pyruvate + L-glutamate
-
12.5% specific activity compared to L-alanine
-
-
?
L-tyrosine + 2-oxoglutarate
2-deamino-2-oxotyrosine + L-glutamate
-
12-14% of the activity with L-alanine
-
-
?
serine + 2-oxoglutarate
3-hydroxy-2-oxopropanoate + glutamate
-
22% of activity with DL-alanine
-
?
tyrosine + 2-oxoglutarate
3-(4-hydroxyphenyl)-2-oxopropanoate + glutamate
-
36.5% of activity with DL-alanine
-
?
DL-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
63-70% of the activity with L-alanine
-
-
?
DL-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
63% specific activity compared to L-alanine
-
-
?
glyoxylate + alanine
glycine + pyruvate
-
70% of activity with glutamate
-
ir
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
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 + 2-oxoglutarate
pyruvate + L-glutamate
-
highly specific for alanine and 2-oxoglutarate
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
cannot use glyoxylate as keto donor
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
Leptosphaeria michotii
-
no activity with L-aspartate, cysteine sulfinate, 2-aminobutanoate and cyclic amino acids
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
important function in beta-alanine metabolism
-
-
-
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
with 2-oxoglutarate specific for L-alanine
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
glutamate-glyoxylate aminotransferase is identical with alanine-2-oxoglutarate aminotransferase
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
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
-
D-alanine at 2% of the activity with L-alanine
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
highly specific for alanine and 2-oxoglutarate
-
r
L-aspartate + 2-oxoglutarate
2-oxobutan-1,4-dioate + L-glutamate
-
6-8% of the activity with L-alanine
-
-
?
L-aspartate + 2-oxoglutarate
2-oxobutan-1,4-dioate + L-glutamate
-
6% specific activity compared to L-alanine
-
-
?
L-leucine + 2-oxoglutarate
2-oxo-4-methylpentanoate + L-glutamate
-
8% of the activity with L-alanine
-
-
?
L-leucine + 2-oxoglutarate
2-oxo-4-methylpentanoate + L-glutamate
-
9% specific activity compared to L-alanine
-
-
?
additional information
?
-
enzyme is also able to utilize aspartate and oxaloacetate with 10% efficiency as compared to the native substrates
-
-
-
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
?
-
-
phenylserine, phenylaminopropanol, phenylaminopropandiol, ethylbenzylamine, and phenylglycinol are not accepted as substrates
-
-
-
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
?
-
-
enzyme displays both cystine C-S lyase activity, EC 4.4.1.8, and alanine aminotransferase activity. No in vitro tyrosine aminotransferase activity is detetced
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
-
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 + 2-oxoglutarate
pyruvate + L-glutamate
-
important function in beta-alanine metabolism
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
anaerobically induced isoform does not require the presence of pyridoxal 5'-phosphate to retain its activity
-
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
interacts with residues Ser105, Ser239, Arg248 and Tyr68, and the backbone amides of Val104 and Ser105
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
substrate inhibition at neutral pH, not seen at pH 8.8
acarbose
-
0.1% acarbose fed to diabetic mice induces a decrease of the catalytic activity to 69.6%
Phenelzine
-
monoamine oxidase inhibitor used as antidepressant/antipanic drug, maximum inhibition, i.e. 32%, of brain alanine aminotransferase at 15 mg/kg
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
Aminooxyacetate
-
competitive to L-alanine, uncompetitive to 2-oxoglutarate
Aminooxyacetate
-
0.0004 mM, 85% inhibition of mitochondrial alanine aminotransferase
Cd2+
-
0.2 mM, 39% inhibition of alanine aminotransferase activity measured in soft body and gills, 0.6 mM, 46% inhibition
Pb2+
-
0.7 mM, 58% inhibition of alanine aminotransferase activity measured in soft body, 0.35 mM, 32% inhibition
additional information
-
not inhibited by 6-azauridine or 6-azauridine 5'-phosphate
-
additional information
-
not inhibited by EDTA, o-phenanthroline and L-ascorbate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
2-oxoglutarate
-
200 mM L-alanine and 2 mM 2-oxoglutarate in 0.1 M phosphate buffer, pH 7.4, at 37°C
0.9
glyoxylate
-
pH and temperature not specified in the publication
0.51
L-alanine
-
200 mM L-alanine and 2 mM 2-oxoglutarate in 0.1 M phosphate buffer, pH 7.4, at 37°C
8.1
L-alanine
-
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.1
L-alanine
-
200 mM L-alanine and 2 mM 2-oxoglutarate in 0.1 M phosphate buffer, pH 7.4, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
beta-chloro-L-alanine
Brevibacterium flavum
-
pH 8.0, temperature not specified in the publication
68
DL-2-aminobutanoate
Brevibacterium flavum
-
pH 8.0, temperature not specified in the publication
1.3
L-Cycloserine
Brevibacterium flavum
-
pH 8.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.75
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30°C
1.6
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30°C
3.52
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30°C
4.5
substrate beta-alanine, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30°C
additional information
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.6
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
tomato, 2 alanine aminotransferases, soluble and Triton X-100 extractable
-
-
brenda
bifunctional cystine C-S lyase, EC 4.4.1.8, and alanine aminotransferase
-
-
brenda
-
636717, 636722, 636729, 673124, 673126, 673914, 673921, 674076, 675072, 675182, 675788, 677259, 721277, 737435
-
-
brenda
high alanine aminotransferase activity is a marker of risk for type 2 diabetis
-
-
brenda
isoform Pyd4, involved in both beta-alanine and gamma-aminobutanoic acid transamination
UniProt
brenda
isoform derived from yeast-like symbionts of Sogatella furcifera
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
broad expression in the head, wings, legs, thorax and abdomen; high transcript level
brenda
broad expression in the head, wings, legs, thorax and abdomen
brenda
-
increase in alanine aminotransferase activity during lactation and weaning when compared to virgin rats
brenda
predominantly expressed in developing seeds during active starch synthesis
brenda
broad expression in the head, wings, legs, thorax and abdomen
brenda
broad expression in the head, wings, legs, thorax and abdomen
brenda
additional information
additional information
only trace amounts of transcripts are detected in the heads, wings, legs and thoraces
brenda
additional information
only trace amounts of transcripts are detected in the heads, wings, legs and thoraces
brenda
additional information
-
expressed in all plant tissues, with relatively low levels in the latex and pedicel
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
RNAi knockdown of the enzyme has no effect on phenotype
physiological function
homozygous Qsd1 RNAi knockdown plants show less than 5% germination after 21 days at 21°C, while heterozygous plants show intermediate levels of about 40% germination, compared with 80-90% for wild-type
physiological function
an AlaAT1 mutant has less amylose and its amylopectinis structurally altered. Expression of the starchsynthesis genes AGPases, SSI, SSIIa, and PPDKB is decreased in the mutant
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17700
45000
50000
54000
56000
69000
95000
112000 - 118000
112200
-
x * 17700, isoform AlaAT I, x * 112200, isoform AlaAT II, SDS-PAGE
69000
-
gel filtration, 1.5fold larger than single peptide mass, indicating that the enzyme is a monomer or homodimer
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
monomer
-
x * 17700, isoform AlaAT I, x * 112200, isoform AlaAT II, SDS-PAGE
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
2.11 A crystal structure of full-length AlaA, and comparison of its overall structure and active site composition with AlaC and valine-pyruvate aminotransferase AvtA. An intact Schiff base linkage exists between Lys240 and pyridoxal 5'-phosphate. A substrate-mimicking acetate ion is deeply buried in the active site, mimicking the structure of the Michaelis complex with alanine
HvAlaAT is crystallized in complex with pyridoxal 5'-phosphate and L-cycloserine. Structure of this complex is solved at 2.7 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
additional information
-
pyridoxal 5-phosphate, L-alanine or 2-oxoglutarate protect against heat inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during the purification procedure the enzyme needs protective substances, i.e. glycerol, 2-mercaptoethanol and alanine
-
enzyme does not tolerate freezing at any stage after sonication of the isolated mitochondria
-
pyridoxal 5'-phosphate, L-alanine or 2-oxoglutarate protects against heat inactivation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate buffer, pH 7.5, 5 mM 2-mercaptoethanol, 5% glycerol, stable for at least 5 weeks
-
-25°C, 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
-
-80°C, 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
-
-80°C, 20 mM Tris-HCl, pH 7.5, stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
-
0-5°C, 50 mM potassium phosphate buffer, pH 7.5, 5 mM 2-mercaptoethanol, 5% glycerol, stable for 2 weeks
-
25°C, 20 mM Tris-HCl, pH 7.5, 56% loss of activity in first two days. Addition of 25% glycerol preserves most of the activity
-
25°C, 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
-
37°C, 20 mM Tris-HCl, pH 7.5, 50% loss of activity in 24 h, and complete loss of activity within one week
-
4°C, 20 mM Tris-HCl, pH 7.5, 53% loss of activity in first two days. Addition of 25% glycerol preserves most of the activity
-
4°C, 20 mM Tris-HCl, pH 7.5, stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
-
4°C, 80% saturated solution of ammonium sulfate, 10 days, 40% loss of activity
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
2 minor forms: AlaAT-1, AlaAT-3, 1 major form, AlaAT-2, ammonium sulfate, DEAE-cellulose, Sephacryl S-200, phenyl-Sepharose
-
ammonium sulfate, DEAE-Sepharose, partial purification of cytosolic and mitochondrial isoenzymes
-
anaerobically induced isoform, ammonium sulfate, gel filtration, Q-Sepharose, Mono P, Mono Q
-
heat treatment, ammonium sulfate, DEAE-cellulose, isoelectric focusing, Sephadex G-150, hydroxylapatite, DEAE-cellulose
-
heat treatment, ammonium sulfate, DEAE-Sepharose, hydroxylapatite, Sephacryl S-200
-
native enzyme, Q-Sepharose, phenyl-Sepharose, hydroxyapatite, S-Sepharose, Mono Q, Superdex 200, recombinant enzyme, heat treatment, Mono Q
-
Ni2+-NTA agarose resin chromatography and Poly-Prep mini-column chromatography
-
Sephadex G-150 column chromatography, DEAE-Sephadex A-25 column chromatography, and hydroxyapatite column chromatography
-
Sepharose S12 gel filtration and nickel-chelating Sepharose column chromatography
using a DE52 column, butyl-Toyopearl column, DEAE-Toyopearl column, CHT ceramic hydroxyapatite column and MonoQ column
-
using saline precipitation, gel filtration, preparative electrophoresis and anion exchange chromatography on protein-Pak Q 8HR column attached to HPLC
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ammonium as nitrogen source induces both gene expression and enzyme activity of AlaAT
-
enzyme is highly expressed in fifth-instar nymphs, followed by male adults,female adults, third and fourth instars; enzyme is highly expressed in male adults, followed by fourth- and first-instar nymphs, and is lowly expressed in fifth-, third-, second-instar nymphs, and in female adults
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
-
hypoxia induces transcript levels for AlaAT1 but not AlaAT2. Hypoxia induces AlaAT1 earlier in roots than in shoots
-
in response to temperature changes, AlaAT levels reach a peak after 12 h in 10°C water and after 48 h in 30°Cwater, 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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
-
sequential online capillary electrophoresis assay to study enzyme inhibitors. Evolution of the inhibition reaction can be achieved by automatically and simultaneously monitoring the substrate consumption and product formation as a function of reaction time
medicine
synthesis
-
for synthesis of monoclonal antibodies in Chinese hamster ovary cells, cooverexpression of alanine aminotransferase in a taurine transporter-overexpressing host cell line gives a higher monoclonal anitbody yield in a shorter culture period. Forced cooverexpression of taurine transporter TAUT and ALT1 in results in a higher proliferation, with an ideal balance between cell viability and productivity
agriculture
-
expression of AlaAT variants from diverse sources and different subcellular locations, in the wild-type Arabidopsis thaliana Col-0 background and alaat1, alaat2 knockout background under various conditions. Both the physical and physiological properties of AlaAT over-expressing transgenic plants demonstrate significant differences between plants expressing the different AlaAT enzymes under different external conditions. Plants over-expressing Mus musculus AlaAT1 and Hordeum vulgare AlaAT constitutively show increased leaf area.Pyrococcus furiosus AlaAT over-expressing cells take-up external leucine and alanine more effectively
agriculture
-
expression of AlaAT variants from diverse sources and different subcellular locations, in the wild-type Arabidopsis thaliana Col-0 background and alaat1, alaat2 knockout background under various conditions. Both the physical and physiological properties of AlaAT over-expressing transgenic plants demonstrate significant differences between plants expressing the different AlaAT enzymes under different external conditions. Plants over-expressing Mus musculus AlaAT1 and Hordeum vulgare AlaAT constitutively show increased leaf area.Pyrococcus furiosus AlaAT over-expressing cells take-up external leucine and alanine more effectively
agriculture
-
expression of AlaAT variants from diverse sources and different subcellular locations, in the wild-type Arabidopsis thaliana Col-0 background and alaat1, alaat2 knockout background under various conditions. Both the physical and physiological properties of AlaAT over-expressing transgenic plants demonstrate significant differences between plants expressing the different AlaAT enzymes under different external conditions. Plants over-expressing Mus musculus AlaAT1 and Hordeum vulgare AlaAT constitutively show increased leaf area.Pyrococcus furiosus AlaAT over-expressing cells take-up external leucine and alanine more effectively
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
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abou-Zeid, A.M.; Jerebzoff, S.; Jerebzoff-Quintin, S.
Alanine aminotransferase in Leptosphaeria michotii. Isolation, properties and cyclic variations of its activity in relation to polypeptide level
Physiol. Plant.
82
401-408
1991
Leptosphaeria michotii
-
brenda
Nakamura, M.; Horie, Y.
Partial purification and properties of alanine and aspartate aminotransferases in the midgut of the silkworm, Bombyx mori (Lepidoptera:Bombycidae)
Appl. Entomol. Zool.
21
236-243
1986
Bombyx mori
-
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Purification and properties of L-alanine 2-oxoglutarate aminotransferase of bovine erythrocytes stroma
Indian J. Biochem. Biophys.
22
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1985
Bos taurus
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Ruscak, M.; Orlicky, J.; Zubor, V.; Hager, H.
Alanine aminotransferase in bovine brain: purification and properties
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39
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1982
Bos taurus
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Mane, S.D.; Mehrotra, K.N.
Alanine aminotransferase: properties and distribution in the desert locust, Schistocerca gregaria
Insect Biochem.
7
419-426
1977
Schistocerca gregaria
-
brenda
Owen, T.G.; Hochachka, P.W.
Purification and properties of dolphin muscle aspartate and alanine transaminases and thier possible roles in the energy metabolism of diving mammals
Biochem. J.
143
541-553
1974
Lagenorhynchus obliquidens
brenda
Noguchi, T.; Takada, Y.; Kido, R.
Glutamate-glyoxylate aminotransferase in rat liver cytosol. Purification, properties and identity with alanine-2-oxoglutarate aminotransferase
Hoppe-Seyler's Z. Physiol. Chem.
358
1533-1542
1977
Canis lupus familiaris, Felis catus, Homo sapiens, Rattus norvegicus
brenda
Eze, L.C.; Echetebu, C.O.
Some properties of aspartate and alanine aminotransferases from Trichoderma virie
J. Gen. Microbiol.
120
523-527
1980
Trichoderma viride
-
brenda
Hatch, M.D.
Separation and properties of leaf aspartate aminotransferase and alanine aminotransferase isoenzymes operative in the C4 pathway of photosynthesis
Arch. Biochem. Biophys.
156
207-214
1973
Atriplex spongiosa
brenda
Rech, J.; Crouzet, J.
Partial purification and initial studies of the tomato L-alanine:2-oxoglutarate aminotransferase
Biochim. Biophys. Acta
350
392-399
1974
Solanum lycopersicum
brenda
De Rosa, G.; Burk, T.L.; Swick, R.W.
Isolation and characterization of mitochondrial alanine aminotransferase from porcine tissue
Biochim. Biophys. Acta
567
116-124
1979
Sus scrofa
brenda
Gubern, G.; Imperial, S.; Busquets, M.; Cortes, A.
Partial characterization of the alanine aminotransferase isoenzymes from human liver
Biochem. Soc. Trans.
18
1288-1289
1990
Homo sapiens
brenda
Lain-Guelbenzu, B.; Cardenas, J.; Munoz-Blanco, J.
Purification and properties of L-alanine aminotransferase from Chlamydomonas reinhardtii
Eur. J. Biochem.
202
881-887
1991
Chlamydomonas reinhardtii
brenda
Umemura, I.; Yanagiya, K.; Komatsubara, S.; Sato, T.; Tosa, T.
Purification and some properties of alanine aminotransferase from Candida maltosa
Biosci. Biotechnol. Biochem.
58
283-287
1994
Candida maltosa
brenda
Son, D.; Jo, J.; Sugiyama, T.
Purification and characterization of alanine aminotransferase from Panicum miliaceum leaves
Arch. Biochem. Biophys.
289
262-266
1991
Panicum miliaceum
brenda
Good, A.G.; Muench, D.G.
Purification and characterization of an anaerobically induced alanine aminotransferase from barley roots
Plant Physiol.
99
1520-1525
1992
Hordeum vulgare
brenda
Tamaki, N.; Aoyama, H.; Kubo, K.; Ikeda, T.; Hama, T.
Purification and properties of beta-alanine aminotransferase from rabbit liver
J. Biochem.
92
1009-1017
1982
Oryctolagus cuniculus
brenda
Desantiago, S.; Aleman, G.; Hernandez-Montes, H.
Alanine aminotransferase activity in mammary tissue, muscle and liver of dam rat during lactation and weaning
Arch. Med. Res.
27
443-448
1996
Rattus norvegicus
brenda
Richens, A.; McEwan, J.R.; Deybach, J.C.; Mumford, J.P.
Evidence for both in vivo and in vitro interaction between vigabatrin and alanine transaminase
Br. J. Clin. Pharmacol.
43
163-168
1997
Homo sapiens
brenda
Orzechowski, S.; Socha-Hanc, J.; Paszkowski, A.
Purification and properties of alanine aminotransferase from maize (Zea mays L.) leaves
Acta Physiol. Plant.
21
323-330
1999
Zea mays
-
brenda
Orzechowski, S.; Socha-Hanc, J.; Paszkowski, A.
Alanine aminotransferase and glycine aminotransferase from maize (Zea mays L.) leaves
Acta Biochim. Pol.
46
447-457
1999
Zea mays
brenda
Blasco, J.; Puppo, J.
Effect of heavy metals (Cu, Cd and Pb) on aspartate and alanine aminotransferase in Ruditapes philippinarum (Mollusca: Bivalvia)
Comp. Biochem. Physiol. C
122
253-263
1999
Ruditapes philippinarum
brenda
Ward, D.E.; Kengen, S.W.; van Der Oost, J.; de Vos, W.M.
Purification and characterization of the alanine aminotransferase from the hyperthermophilic Archaeon pyrococcus furiosus and its role in alanine production
J. Bacteriol.
182
2559-2566
2000
Pyrococcus furiosus, Pyrococcus furiosus (Q9P9M8)
brenda
Tanay, V.A.; Parent, M.B.; Wong, J.T.; Paslawski, T.; Martin, I.L.; Baker, G.B.
Effects of the antidepressant/antipanic drug phenelzine on alanine and alanine transaminase in rat brain
Cell. Mol. Neurobiol.
21
325-339
2001
Rattus norvegicus
brenda
Vozarova, B.; Stefan, N.; Lindsay, R.S.; Saremi, A.; Pratley, R.E.; Bogardus, C.; Tataranni, P.A.
High alanine aminotransferase is associated with decreased hepatic insulin sensitivity and predicts the development of type 2 diabetes
Diabetes
51
1889-1895
2002
Homo sapiens
brenda
Samsonova, M.V.; Min'kova, N.O.; Lapteva, T.I.; Mikodina, E.V.; Filippovich, Y.B.
Aspartate and alanine aminotransferases in early development of the keta
Russ. J. Dev. Biol.
34
14-18
2003
Oncorhynchus keta
-
brenda
Xuan, G.S.; Oh, S.W.; Choi, E.Y.
Development of an electrochemical immunosensor for alanine aminotransferase
Biosens. Bioelectron.
19
365-371
2003
Homo sapiens
brenda
Matthews, C.C.; Zielke, H.R.; Parks, D.A.; Fishman, P.S.
Glutamate-pyruvate transaminase protects against glutamate toxicity in hippocampal slices
Brain Res.
978
59-64
2003
Rattus norvegicus
brenda
Srivastava, A.S.; Oohara, I.; Suzuki, T.; Shenouda, S.; Singh, S.N.; Chauhan, D.P.; Carrier, E.
Purification and properties of cytosolic alanine aminotransferase from the liver of two freshwater fish, Clarias batrachus and Labeo rohita
Comp. Biochem. Physiol. B
137
197-207
2004
Clarias batrachus, Labeo rohita
brenda
Vedavathi, M.; Girish, K.S.; Kumar, M.K.
Isolation and characterization of cytosolic alanine aminotransferase isoforms from starved rat liver
Mol. Cell. Biochem.
267
13-23
2004
Rattus norvegicus
brenda
Petlevski, R.; Hadzija, M.; Bajalo, J.L.; Juretic, D.
Effect of acarbose on alanine aminotransferase and aspartate aminotransferase activities in the liver of control and diabetic CBA mice
Acta Pharm.
56
87-93
2006
Mus musculus
brenda
Vedavathi, M.; Girish, K.S.; Kumar, M.K.
A novel low molecular weight alanine aminotransferase from fasted rat liver
Biochemistry
71
S105-S112
2006
Rattus norvegicus
-
brenda
Ingram, C.U.; Bommer, M.; Smith, M.E.; Dalby, P.A.; Ward, J.M.; Hailes, H.C.; Lye, G.J.
One-pot synthesis of amino-alcohols using a de-novo transketolase and beta-alanine:pyruvate transaminase pathway in Escherichia coli
Biotechnol. Bioeng.