2.6.1.1: aspartate transaminase

This is an abbreviated version!
For detailed information about aspartate transaminase, go to the full flat file.

Reaction

Synonyms

2-oxoglutarate-glutamate aminotransferase, AAT, AAT-2, AAT-3, AAT3, aatA, AATase, aatB3, all2340, alr1039, alr2765, alr4853, aminotransferase, aspartate, aoa/coa, AsAT, Asp AT, aspartate alpha-ketoglutarate transaminase, aspartate aminotransferase, aspartate aminotransferase 1, aspartate aminotransferase A, aspartate AT, aspartate transaminase, aspartate, 2-oxoglutarate aminotransferase, aspartate-2-oxoglutarate transaminase, aspartate/(R)-cysteate:2-oxoglutarate aminotransferase, aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase, aspartate:2-oxoglutarate amino-transferase, aspartate:2-oxoglutarate aminotransferase, aspartic acid aminotransferase, aspartic aminotransferase, aspartyl aminotransferase, AspAT, AspATSs, aspB, aspC, AspT, AST, AST-Bb, AtPAT, bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase, C-S lyase, CAA1, cAST, Cgl0240, class Ibeta AAT, EcAspAT, GL50803_91056, glutamate oxaloacetate transaminase, glutamate oxaloacetate transaminase 1, glutamate-oxalacetate aminotransferase, glutamate-oxalate transaminase, glutamate-oxaloacetate transaminase 1, glutamic oxalic transaminase, glutamic oxaloacetic transaminase, glutamic-aspartic aminotransferase, glutamic-aspartic transaminase, glutamic-oxalacetic transaminase, glutamic-oxaloacetic transaminase, GOT, GOT (enzyme), GOT1, GOT1L1, GOT2, KAT IV, L-aspartate aminotransferase, L-aspartate transaminase, L-aspartate-2-ketoglutarate aminotransferase, L-aspartate-2-oxoglutarate aminotransferase, L-aspartate-2-oxoglutarate-transaminase, L-aspartate-alpha-ketoglutarate transaminase, L-aspartate:2-oxoglutarate aminotransferase, L-aspartateartate aminotransferase, L-aspartic aminotransferase, L-AspAT, mitAAT, More, oxaloacetate transferase, oxaloacetate-aspartate aminotransferase, Pat, PfAspAT, plastid aspartate aminotransferase, prephenate aminotransferase, protein TT0402, PT-AAT, Rv3722c, Sar2028, SsAspAT, Tb11.02.2740, transaminase A

ECTree

     2 Transferases

         2.6 Transferring nitrogenous groups

             2.6.1 Transaminases

                2.6.1.1 aspartate transaminase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
8	Activating Compound
15300	AA Sequence
11	Application
1	CAS Registry Number
44	Cloned(Commentary)
102	Cofactor
39	Crystallization (Commentary)
4727	Disease/ Diagnostics
7	Expression
18	General Information
13	General Stability
59	IC50 Value
159	Inhibitors
40	kcat/KM [mM/s]
52	Ki Value [mM]
260	KM Value [mM]
171	Localization
10	Metals/Ions
107	Molecular Weight [Da]
139	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
881	Organism
59	Pathway
333	PDB ID
75	pH Optimum
16	pH Range
6	pH Stability
28	pI Value
1	Posttranslational Modification
63	Protein Variants
87	Purification (Commentary)
24	Reaction
1	Reaction Type
233	Reference
12	Renatured (Commentary)
144	Source Tissue
107	Specific Activity [micromol/min/mg]
13	Storage Stability
401	Substrates and Products (Substrate)
90	Subunits
320	Synonyms
1	Systematic Name
50	Temperature Optimum [°C]
8	Temperature Range [°C]
51	Temperature Stability [°C]
72	Turnover Number [1/s]

Application

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Application on EC 2.6.1.1 - aspartate transaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Application Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

biotechnology

Sus scrofa

-

an enzymatic method for the synthesis of the amino acid Phe is developed. AAT from porcine heart is immobilized by covalent attachment and entrapment, and the resulting immobilized preparations are compared to the soluble enzyme both in terms of stability and reaction efficiency

721515

medicine

6 entries

synthesis

4 entries

medicine

Mus musculus

-

the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells

715070

medicine

Oryctolagus cuniculus

-

the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells

715070

medicine

Rattus norvegicus

P00507

the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells

715070

medicine

Homo sapiens

P17174

following doxorubicin administration, triple-negative breast cancer cells, which do not express the estrogen receptor, the progesterone receptor, and the human epidermal growth factor receptor, acquire metabolic alteration, causing increased glutamine flux for the synthesis of aspartate which can be converted into oxaloacetate by GOT1. Subsequently, this oxaloacetate is converted into malate and then pyruvate, maintaining the NADP+/NADPH ratio which neutralizes doxorubicin-induced oxidative stress. Repression of GOT1 results in doxorubicin-induced formation of reactive oxygen species, thereby increasing doxorubicin sensitivity

737616

medicine

Mus musculus BALB/cCrSlc

-

the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells

-

medicine

Oryctolagus cuniculus New Zealand White

-

the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells

-

synthesis

Escherichia coli

-

mutant enzyme R292E/L18H can use L-lysine as inexpensive amino donor for the production of L-homophenylalanine. The low solubility of product L-homophenylalanine and spontaneous cyclization of 2-keto-6-aminocaproate drive the reaction completely towards production of L-homophenylalanine

658335

synthesis

Homo sapiens

P00505

codon-optimized expression in Escherichia coli with His6-tag and purification. The enzyme activity of purified aspartate aminotransferase reaches 150000 U/l. The preparation shows high stability during long-term storage at -20ºC

738861

synthesis

Escherichia coli

A0A140ND68

expression in 2-phenylethanol producing strain Saccharomyces cerevisiae YS58, and use of the strain for the coproduction of 2-phenylethanol and L-homophenylalanine via a fermentation process. The L-homophenylalanine productivity of the recombinant Saccharomyces cerevisiae improves by 78.9% in comparison to the wild-type. High yields of 43.7 mM L-homophenylalanine and 32.4 mM 2-phenylethanol are achieved

738727

synthesis

Escherichia coli BL21-DE3

-

expression in 2-phenylethanol producing strain Saccharomyces cerevisiae YS58, and use of the strain for the coproduction of 2-phenylethanol and L-homophenylalanine via a fermentation process. The L-homophenylalanine productivity of the recombinant Saccharomyces cerevisiae improves by 78.9% in comparison to the wild-type. High yields of 43.7 mM L-homophenylalanine and 32.4 mM 2-phenylethanol are achieved

-