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Information on EC 2.6.1.2 - alanine transaminase and Organism(s) Homo sapiens and UniProt Accession P24298

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     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.2 alanine transaminase
IUBMB Comments
A pyridoxal-phosphate protein. 2-Aminobutanoate can act slowly instead of alanine.
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This record set is specific for:
Homo sapiens
UNIPROT: P24298
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
alanine aminotransferase, alanine transaminase, alat, pyruvate transaminase, glutamic-pyruvic transaminase, glutamate-pyruvate transaminase, alanine-aminotransferase, alaat, l-alanine aminotransferase, c-aat, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alanine aminotransferase
-
-
-
-
alanine-alpha-ketoglutarate aminotransferase
-
-
-
-
alanine-aminotransferase
-
-
alanine-pyruvate aminotransferase
-
-
-
-
ALAT
-
-
aminotransferase, alanine
-
-
-
-
beta-alanine aminotransferase
-
-
-
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
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
-
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 + glyoxylate
pyruvate + glycine
show the reaction diagram
L-glutamate and L-alanine are by far the best amino-group donors
-
-
?
L-glutamate + glyoxylate
2-oxoglutarate + glycine
show the reaction diagram
L-glutamate and L-alanine are by far the best amino-group donors
-
-
?
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
licorice
-
traditional Chinese medicine, competitive, reversible
-
Qingkailing
-
traditional Chinese medicine, noncompetitive, reversible
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.75 - 0.81
glyoxylate
0.19 - 0.22
2-oxoglutarate
21
alanine
-
pH 7.8, 30°C, cytosolic enzyme
5.1 - 10.12
L-alanine
3.22
L-glutamate
-
pH 7.4, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.16
licorice
-
pH 7.5, temperature not specified in the publication
-
1.61
Qingkailing
-
pH 7.5, temperature not specified in the publication
-
1.15
succinic acid
-
pH 7.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.1
pH 7.4, 25°C, L-alanine (10 mM) + glyoxylate
2.5
pH 7.4, 25°C, L-glutamate (10 mM) + glyoxylate
4
-
25°C
60.2
-
25°C
additional information
-
11.2 units/ml
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
-
almost full activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
37
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALAT1_HUMAN
496
0
54637
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
recombinant enzyme
112000 - 118000
-
gel filtration
59000
-
x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
60000
-
x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 59000, calculated, x * 60000, SDS-PAGE, His-tagged protein
PROTEIN VARIANTS
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
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
-
-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
-
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
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37°C, 20 mM Tris-HCl, pH 7.5, 72% loss of activity in first two days
-
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sepharose, partial purification of cytosolic and mitochondrial isoenzymes
-
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed as His6-tagged protein in Escherichia coli cells
expression in Sf9 cell
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is increased during acute hepatitis C virus infection
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Chang, Y.; Ryu, S.; Sung, E.; Jang, Y.
Higher concentrations of alanine aminotransferase within the reference interval predict nonalcoholic fatty liver disease
Clin. Chem.
53
686-692
2007
Homo sapiens
Manually annotated by BRENDA team
Totan, A.; Greabu, M.; Totan, C.; Spinu, T.
Salivary aspartate aminotransferase, alanine aminotransferase and alkaline phosphatase: possible markers in periodontal diseases?
Clin. Chem. Lab. Med.
44
612-615
2006
Homo sapiens
Manually annotated by BRENDA team
Nathwani, R.A.; Pais, S.; Reynolds, T.B.; Kaplowitz, N.
Serum alanine aminotransferase in skeletal muscle diseases
Hepatology
41
380-382
2005
Homo sapiens
Manually annotated by BRENDA team
Kazumi, T.; Kawaguchi, A.; Hirano, T.; Yoshino, G.
Serum alanine aminotransferase is associated with serum adiponectin, C-reactive protein and apolipoprotein B in young healthy men
Horm. Metab. Res.
38
119-124
2006
Homo sapiens
Manually annotated by BRENDA team
Harenberg, J.; Joerg, I.; Weiss, C.
Observations of alanine aminotransferase and aspartate aminotransferase in THRIVE studies treated orally with ximelagatran
Int. J. Toxicol.
25
165-169
2006
Homo sapiens
Manually annotated by BRENDA team
Lopes, E.P.; Gouveia, E.C.; Albuquerque, A.C.; Sette, L.H.; Mello, L.A.; Moreira, R.C.; Coelho, M.R.
Determination of the cut-off value of serum alanine aminotransferase in patients undergoing hemodialysis, to identify biochemical activity in patients with hepatitis C viremia
J. Clin. Virol.
35
298-302
2006
Homo sapiens
Manually annotated by BRENDA team
Prati, D.; Shiffman, M.L.; Diago, M.; Gane, E.; Rajender Reddy, K.; Pockros, P.; Farci, P.; OBrien, C.B.; Lardelli, P.; Blotner, S.; Zeuzem, S.
Viral and metabolic factors influencing alanine aminotransferase activity in patients with chronic hepatitis C
J. Hepatol.
44
679-685
2006
Homo sapiens
Manually annotated by BRENDA team
Dahari, H.; Markatou, M.; Zeremski, M.; Haller, I.; Ribeiro, R.M.; Licholai, T.; Perelson, A.S.; Talal, A.H.
Early ribavirin pharmacokinetics, HCV RNA and alanine aminotransferase kinetics in HIV/HCV co-infected patients during treatment with pegylated interferon and ribavirin
J. Hepatol.
47
23-30
2007
Homo sapiens
Manually annotated by BRENDA team
Oh, S.Y.; Cho, Y.K.; Kang, M.S.; Yoo, T.W.; Park, J.H.; Kim, H.J.; Park, D.I.; Sohn, C.I.; Jeon, W.K.; Kim, B.I.; Son, B.H.; Shin, J.H.
The association between increased alanine aminotransferase activity and metabolic factors in nonalcoholic fatty liver disease
Metab. Clin. Exp.
55
1604-1609
2006
Homo sapiens
Manually annotated by BRENDA team
Khedmat, H.; Fallahian, F.; Abolghasemi, H.; Hajibeigi, B.; Attarchi, Z.; Alaeddini, F.; Holisaz, M.T.; Pourali, M.; Sharifi, S.; Zarei, N.
Serum gamma-glutamyltransferase, alanine aminotransferase, and aspartate aminotransferase activity in Iranian healthy blood donor men
World J. Gastroenterol.
13
889-894
2007
Homo sapiens
Manually annotated by BRENDA team
Liu, L.; Zhong, S.; Yang, R.; Hu, H.; Yu, D.; Zhu, D.; Hua, Z.; Shuldiner, A.R.; Goldstein, R.; Reagan, W.J.; Gong, D.W.
Expression, purification, and initial characterization of human alanine aminotransferase (ALT) isoenzyme 1 and 2 in High-five insect cells
Protein Expr. Purif.
60
225-231
2008
Homo sapiens
Manually annotated by BRENDA team
Gelderblom, H.C.; Zeuzem, S.; Weegink, C.J.; Forestier, N.; Mcnair, L.; Purdy, S.; Dijkgraf, M.g.W.; Jansen, P.L.M.; Reesnik, H.W.
Inflammatory markers neopterin and alanine aminotransferase in HCV patients treated with HCV NS3-4A protease inhibitor telaprevir (VX-950) and/or peginterferon alfa-2a
Scand. J. Gastroenterol.
43
1122-1127
2008
Homo sapiens
Manually annotated by BRENDA team
Mu, X.; Qi, L.; Qiao, J.; Zhang, H.; Ma, H.
Study on alanine aminotransferase kinetics by microchip electrophoresis
Anal. Biochem.
421
499-505
2012
Homo sapiens
Manually annotated by BRENDA team
Donini, S.; Ferrari, M.; Fedeli, C.; Faini, M.; Lamberto, I.; Marletta, A.S.; Mellini, L.; Panini, M.; Percudani, R.; Pollegioni, L.; Caldinelli, L.; Petrucco, S.; Peracchi, A.
Recombinant production of eight human cytosolic aminotransferases and assessment of their potential involvement in glyoxylate metabolism
Biochem. J.
422
265-272
2009
Homo sapiens (P24298)
Manually annotated by BRENDA team
Liu, L.; Chen, Y.; Yang, L.
Inhibition study of alanine aminotransferase enzyme using sequential online capillary electrophoresis analysis
Anal. Biochem.
467
28-30
2014
Homo sapiens
Manually annotated by BRENDA team
Tabuchi, H.; Sugiyama, T.
Cooverexpression of alanine aminotransferase 1 in Chinese hamster ovary cells overexpressing taurine transporter further stimulates metabolism and enhances product yield
Biotechnol. Bioeng.
110
2208-2215
2013
Homo sapiens (P24298)
Manually annotated by BRENDA team
Hajarizadeh, B.; Lamoury, F.M.; Feld, J.J.; Amin, J.; Keoshkerian, E.; Matthews, G.V.; Hellard, M.; Dore, G.J.; Lloyd, A.R.; Grebely, J.; Applegate, T.L.
Alanine aminotransferase, HCV RNA levels and pro-inflammatory and pro-fibrogenic cytokines/chemokines during acute hepatitis C virus infection
Virol. J.
13
32
2016
Homo sapiens
Manually annotated by BRENDA team