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Enzyme Nomenclature
Information on EC 2.6.1.2 - alanine transaminase
for references in articles please use BRENDA:EC2.6.1.2
Word Map on EC 2.6.1.2
- 2.6.1.2
- injury
- bilirubin
- necrosis
- cholesterol
- lactate
-
hepatotoxicity
- viral
- triglyceride
- creatinine
- fibrosis
- hepatocytes
- urea
- inflammation
- cirrhosis
- superoxide
- malondialdehyde
-
interferon
-
enrol
- diabetes
-
hepatoprotective
- steatosis
- wistar
- bile
-
gamma-glutamyl
-
virological
-
tetrachloride
- gsh
- ccl4
-
reperfusion
-
nonalcoholic
-
anti-hcv
-
hbeag
- transpeptidase
- nafld
-
portal
- seroconversion
- cholestasis
-
prothrombin
- ribavirin
-
ccl4-induced
- steatohepatitis
-
transaminases
- acetaminophen
- gamma-glutamyltransferase
-
aminotransferases
- jaundice
- lamivudine
- viremia
-
waist
-
corpuscular
- medicine
- synthesis
- agriculture
- analysis
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.6.1.2
-
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RECOMMENDED NAME
GeneOntology No.
alanine transaminase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
tomato, 2 alanine aminotransferases, soluble and Triton X-100 extractable
-
-
bifunctional cystine C-S lyase, EC 4.4.1.8, and alanine aminotransferase
-
-
-
636717, 636722, 636729, 673124, 673126, 673914, 673921, 674076, 675072, 675182, 675788, 677259, 721277, 737435
-
-
high alanine aminotransferase activity is a marker of risk for type 2 diabetis
-
-
isoform Pyd4, involved in both beta-alanine and gamma-aminobutanoic acid transamination
UniProt
isoform derived from yeast-like symbionts of Sogatella furcifera
X5DUP7
UniProt
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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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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 SUBSTRATES
NATURAL PRODUCTS
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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INHIBITORS
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
X5DCE6, X5DUP7
broad expression in the head, wings, legs, thorax and abdomen; high transcript level
X5DCE6, X5DUP7
broad expression in the head, wings, legs, thorax and abdomen
-
increase in alanine aminotransferase activity during lactation and weaning when compared to virgin rats
predominantly expressed in developing seeds during active starch synthesis
X5DCE6, X5DUP7
broad expression in the head, wings, legs, thorax and abdomen
X5DCE6, X5DUP7
broad expression in the head, wings, legs, thorax and abdomen
additional information
additional information
X5DCE6
only trace amounts of transcripts are detected in the heads, wings, legs and thoraces
additional information
X5DUP7
only trace amounts of transcripts are detected in the heads, wings, legs and thoraces
additional information
-
expressed in all plant tissues, with relatively low levels in the latex and pedicel
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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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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SUBUNITS
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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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
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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
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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
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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
X5DCE6, X5DUP7
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
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hypoxia induces transcript levels for AlaAT1 but not AlaAT2. Hypoxia induces AlaAT1 earlier in roots than in shoots
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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)
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nitrogen deprivation results in reduced transcript levels for AlaAT. The effect is more pronounced for AlaAT1
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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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
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a mutant strain is severely hampered in polyamine utilization, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
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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
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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
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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
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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
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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
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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
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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
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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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