Information on EC 2.6.1.2 - alanine transaminase and Organism(s) Homo sapiens

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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
2.6.1.2
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RECOMMENDED NAME
GeneOntology No.
alanine transaminase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anaerobic energy metabolism (invertebrates, cytosol)
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C4 photosynthetic carbon assimilation cycle, NAD-ME type
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C4 photosynthetic carbon assimilation cycle, PEPCK type
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L-alanine biosynthesis II
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L-alanine degradation II (to D-lactate)
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L-alanine degradation III
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alanine metabolism
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C4 and CAM-carbon fixation
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Arginine biosynthesis
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Alanine, aspartate and glutamate metabolism
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Carbon fixation in photosynthetic organisms
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Metabolic pathways
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Microbial metabolism in diverse environments
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-86-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
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
L-alanine + glyoxylate
pyruvate + glycine
show the reaction diagram
L-glutamate and L-alanine are by far the best amino-group donors
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-
?
L-glutamate + glyoxylate
2-oxoglutaramate + glycine
show the reaction diagram
L-glutamate and L-alanine are by far the best amino-group donors
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-
?
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
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
licorice
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traditional Chinese medicine, competitive, reversible
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Qingkailing
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traditional Chinese medicine, noncompetitive, reversible
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succinic acid
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competitive, reversible
vigabatrin
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 0.22
2-oxoglutarate
21
alanine
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pH 7.8, 30°C, cytosolic enzyme
0.75 - 0.81
glyoxylate
5.1 - 10.12
L-alanine
3.22
L-glutamate
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pH 7.4, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.16
licorice
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pH 7.5, temperature not specified in the publication
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1.61
Qingkailing
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pH 7.5, temperature not specified in the publication
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1.15
succinic acid
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pH 7.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.1
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pH 7.4, 25°C, L-alanine (10 mM) + glyoxylate
2.5
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pH 7.4, 25°C, L-glutamate (10 mM) + glyoxylate
4
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25°C
60.2
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25°C
additional information
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11.2 units/ml
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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almost full activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Q8TD30
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
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recombinant enzyme
59000
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x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
60000
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x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
112000 - 118000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM Tris-HCl, pH 7.5, freezing is worse than storage at 4°C or 25°C
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-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
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-80°C, 20 mM Tris-HCl, pH 7.5, stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
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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
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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
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37°C, 20 mM Tris-HCl, pH 7.5, 50% loss of activity in 24 h, and complete loss of activity within one week
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37°C, 20 mM Tris-HCl, pH 7.5, 72% loss of activity in first two days
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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
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4°C, 20 mM Tris-HCl, pH 7.5, stable for at least 20 days. Addition of 25% glycerol preserves most of the activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sepharose, partial purification of cytosolic and mitochondrial isoenzymes
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recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Sf9 cell
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overexpressed as His6-tagged protein in Escherichia coli cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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