Information on EC 2.6.1.2 - alanine transaminase

Word Map on EC 2.6.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
2.6.1.2
-
RECOMMENDED NAME
GeneOntology No.
alanine transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
-
anaerobic energy metabolism (invertebrates, cytosol)
-
-
Arginine biosynthesis
-
-
C4 photosynthetic carbon assimilation cycle, NAD-ME type
-
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
-
Carbon fixation in photosynthetic organisms
-
-
L-alanine biosynthesis II
-
-
L-alanine degradation II (to D-lactate)
-
-
L-alanine degradation III
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
alanine metabolism
-
-
C4 and CAM-carbon fixation
-
-
SYSTEMATIC NAME
IUBMB Comments
L-alanine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly instead of alanine.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-86-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Bugang
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
dolphin
-
-
Manually annotated by BRENDA team
Leptosphaeria michotii
fungi
-
-
Manually annotated by BRENDA team
six isoforms with different pH-optima
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Dongjin
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PAO2
-
-
Manually annotated by BRENDA team
-
-
-
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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
bifunctional cystine C-S lyase, EC 4.4.1.8, and alanine aminotransferase
-
-
Manually annotated by BRENDA team
soil fungus
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
aspartate + 2-oxoglutarate
malate + L-glutamate
show the reaction diagram
14% of activity with glutamate and pyruvate
-
?
aspartate + pyruvate
malate + alanine
show the reaction diagram
10% of activity with alanine and 2-oxoglutarate
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
?
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
glycine + 2-oxoglutarate
glyoxylate + glutamate
show the reaction diagram
-
24% of activity with DL-alanine
-
?
glyoxylate + alanine
glycine + pyruvate
show the reaction diagram
glyoxylate + glutamate
glycine + 2-oxoglutarate
show the reaction diagram
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 + glyoxylate
pyruvate + glycine
show the reaction diagram
L-glutamate and L-alanine are by far the best amino-group donors
-
-
?
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
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-glutamate + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
L-glutamate and L-alanine are by far the best amino-group donors
-
-
?
L-leucine + 2-oxoglutarate
2-oxo-4-methylpentanoate + L-glutamate
show the reaction diagram
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
-
-
?
L-tyrosine + 2-oxoglutarate
2-deamino-2-oxotyrosine + L-glutamate
show the reaction diagram
-
12-14% of the activity with L-alanine
-
-
?
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
show the reaction diagram
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
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
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
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
additional information
-
anaerobically induced isoform does not require the presence of pyridoxal 5'-phosphate to retain its activity
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(aminooxy)acetate
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%
Ag+
-
-
Al3+
-
-
Aminooxyacetate
aminooxyacetic acid
-
2.5 mM, complete inhibition
beta-chloro-L-alanine
-
-
Citric acid
-
-
Co2+
-
-
cycloserine
D-alanine
-
competitive vs. L-alanine
DL-2-aminobutanoate
-
-
-
EDTA
-
-
Fumaric acid
-
-
Glutarate
HgCl2
hydroxylamine
Isonicotinic hydrazide
-
-
L-ascorbic acid
-
2 mM, 25% inhibition
L-Cycloserine
-
-
licorice
-
traditional Chinese medicine, competitive, reversible
-
malate
-
5 mM, 25% inhibition
Maleate
Maleic acid
-
-
o-phenanthroline
-
weak
oxalic acid
-
-
p-chloromercuribenzoate
p-hydroxymercuribenzoate
Phenelzine
-
monoamine oxidase inhibitor used as antidepressant/antipanic drug, maximum inhibition, i.e. 32%, of brain alanine aminotransferase at 15 mg/kg
phenylhydrazine
-
-
Qingkailing
-
traditional Chinese medicine, noncompetitive, reversible
-
Semicarbazide
succinate
-
competitive inhibitor
succinic acid
-
competitive, reversible
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0058 - 5
2-oxoglutarate
0.51
4-aminobutanoate
-
pH 8.8, 37C, cosubstrate 2-oxoglutarate
0.25 - 21
alanine
3.9 - 7.6
beta-Alanine
8.3
DL-alanine
-
pH 8.6, 37C
0.55 - 32
glutamate
0.75 - 0.9
glyoxylate
0.21 - 30.3
L-alanine
0.1 - 13
L-glutamate
0.022 - 18.6
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 170
2-oxoglutarate
0.08 - 170
L-alanine
0.17 - 136
L-glutamate
0.17 - 136
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22290 - 24640
2-oxoglutarate
34
22290 - 24640
L-alanine
103
19630 - 20510
L-glutamate
41
19630 - 20510
pyruvate
31
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00034 - 0.00064
Aminooxyacetate
1.16
licorice
-
pH 7.5, temperature not specified in the publication
-
1.61
Qingkailing
-
pH 7.5, temperature not specified in the publication
-
17
succinate
-
pH 8.6, 37C
1.15
succinic acid
-
pH 7.5, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069
(aminooxy)acetate
Hordeum vulgare
-
25C, pH 8.0
0.15
beta-chloro-L-alanine
Brevibacterium flavum
-
pH 8.0, temperature not specified in the publication
0.119
cycloserine
Hordeum vulgare
-
25C, pH 8.0
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.12
-
enzyme from cell lysate
0.75
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30C
1.39
-
-
1.6
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
2.1
-
pH 7.4, 25C, L-alanine (10 mM) + glyoxylate
2.5
-
pH 7.4, 25C, L-glutamate (10 mM) + glyoxylate
3.52
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30C
3.55
-
-
4.5
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
-
native enzyme
213
-
-
229.8
-
after purification
243
-
recombinant enzyme
360
Leptosphaeria michotii
-
-
594
-
forward reaction
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
-
6.5 - 7.5
-
forward and reverse reaction
6.5 - 7.8
-
native and recombinant enzyme
7.3
-
assay at
7.5 - 8.5
-
-
8 - 8.3
-
with alanine and 2-oxoglutarate
8.2
-
isoform in eggs
8.3
-
in borate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 9.5
-
active over whole range
5.5 - 9.5
-
approx. 70% of maximal activity at pH 5.5, approx. 50% of maximal activity at pH 9.5
5.5 - 8.2
-
native and recombinant enzyme
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
6.5 - 7.5
-
-
7 - 9
more than 70% of maximum activity
7 - 7.5
-
rapid decrease of activity below pH 7 and above pH 7.5
7.9 - 8.4
-
highest activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
above 95C, native and recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 55
-
strong decrease above
30 - 95
-
native and recombinant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
isoform AlaAT II, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
broad expression in the head, wings, legs, thorax and abdomen; high transcript level
Manually annotated by BRENDA team
-
three isoforms with different pH-optima
Manually annotated by BRENDA team
specific expression
Manually annotated by BRENDA team
-
stroma
Manually annotated by BRENDA team
broad expression in the head, wings, legs, thorax and abdomen
Manually annotated by BRENDA team
-
highest activity, two isoforms with different pH-optima
Manually annotated by BRENDA team
-
increase in alanine aminotransferase activity during lactation and weaning when compared to virgin rats
Manually annotated by BRENDA team
-
highest expression found
Manually annotated by BRENDA team
predominantly expressed in developing seeds during active starch synthesis
Manually annotated by BRENDA team
-
mitochondrial enzyme
Manually annotated by BRENDA team
broad expression in the head, wings, legs, thorax and abdomen
Manually annotated by BRENDA team
broad expression in the head, wings, legs, thorax and abdomen
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18300
-
gel filtration
18370
-
isoform AlaAT I, gel filtration
46000
-
2 * 46000, SDS-PAGE
48000
-
2 * 48000, SDS-PAGE
52000
-
2 * 52000, SDS-PAGE
53000
-
enzyme containing a His- and a T5-tag, SDS-PAGE
54820
-
calculated from sequence of cDNA
55100
-
LC mass spectrometry
55500
2 * 55500, gel filtration
57000
-
recombinant enzyme
57900
-
SDS-PAGE
59000
-
x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
60000
-
x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
61300
-
SDS-PAGE
65000
-
1 * 65000
75000
-
1 * 75000, SDS-PAGE
80000
-
gel filtration
92000
-
-
93400
-
gel filtration
97000
-
gel filtration
99000
-
gel filtration
100000
-
gel filtration
101000
-
SDS-PAGE
102000
-
gel filtration
105000
-
gel filtration
110000
Leptosphaeria michotii
-
-
111000
gel filtration; PAGE
112000 - 118000
112000
-
sucrose density gradient centrifugation
112200
-
x * 17700, isoform AlaAT I, x * 112200, isoform AlaAT II, SDS-PAGE
114800
-
isoform AlaAT II, gel filtration
115000
-
gel filtration
118000
-
sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
strong loss of activity below
636720
7 - 9
70% of activity remaining at pH values of 7 and 9
673585
7.5
-
40C, 30 min, 50% loss of activity
636724
8.5 - 9.5
-
more stable at alkaline pH than at neutral pH
636724
9
-
40C, 30 min, 5% loss of activity
636724
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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
-
K+ or L-alanine stabilizes
-
pyridoxal 5'-phosphate, L-alanine or 2-oxoglutarate protects against heat inactivation
-
uneffected by repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10% glycerol, half-life of 2 weeks
-
-20C, 20 mM Tris-HCl, pH 7.5, freezing is worse than storage at 4C or 25C
-
-20C, 50 mM potassium phosphate buffer, pH 7.5, 5 mM 2-mercaptoethanol, 5% glycerol, stable for at least 5 weeks
-
-20C, stable for several months
-
-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
-
-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
-
0-5C, 50 mM potassium phosphate buffer, pH 7.5, 5 mM 2-mercaptoethanol, 5% glycerol, stable for 2 weeks
-
0C, stable for several h in solution
-
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, 12 days, 57% residual activity
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
-
4C, 80% saturated solution of ammonium sulfate, 10 days, 40% loss of activity
-
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-cellulose, 3 isoforms
-
ammonium sulfate, DEAE-Sephadex, Sephadex G-200, partial purification
-
ammonium sulfate, DEAE-Sepharose, partial purification of cytosolic and mitochondrial isoenzymes
-
ammonium sulfate, hydroxylapatite, preparative electrophoresis
-
ammonium sulfate, Sephadex G-150, DEAE-Sephadex, partial purification
-
anaerobically induced isoform, ammonium sulfate, gel filtration, Q-Sepharose, Mono P, Mono Q
-
DEAE-Sephadex
-
Dowex 50WX8 200-400 mesh chromatography
-
heat treatment, ammonium sulfate, DEAE-cellulose, isoelectric focusing, Sephadex G-150, hydroxylapatite, DEAE-cellulose
-
heat treatment, ammonium sulfate, DEAE-Sepharose, hydroxylapatite, Sephacryl S-200
-
HisTrap HP column chromatography
-
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
-
recombinant enzyme
-
Sephadex G-150 column chromatography, DEAE-Sephadex A-25 column chromatography, and hydroxyapatite column chromatography
-
Sephadex G-150, DEAE-cellulose, ammonium sulfate, isoelectric focusing
-
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 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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana
-
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli strain BL21gold(DE3)
-
expression as His-tagged protein
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
expression in Sf9 cell
-
expression in Sf9 cells; expression in Sf9 cells
overexpressed as His6-tagged protein in Escherichia coli cells
-
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 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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
L214F
mutation observed in short dormancy barley
additional information
-
a mutant strain is severely hampered in polyamine utilization, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Show AA Sequence (1893 entries)
Please use the Sequence Search for a specific query.
Show Disease (7568 entries)
Longer loading times are possible.