Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.6.1.1 - aspartate transaminase and Organism(s) Homo sapiens and UniProt Accession P00505

for references in articles please use BRENDA:EC2.6.1.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.1 aspartate transaminase
IUBMB Comments
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis , some EC 2.6.1.57 activity can be found in this enzyme from other sources ; indeed the enzymes are identical in Trichomonas vaginalis .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P00505
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
aspartate transaminase, asat, glutamic oxaloacetic transaminase, glutamate oxaloacetate transaminase, glutamic-oxaloacetic transaminase, asp at, aspat, aspartate at, glutamic-oxalacetic transaminase, aat-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-oxoglutarate-glutamate aminotransferase
-
-
-
-
aminotransferase, aspartate
-
-
-
-
AsAT
-
-
aspartate alpha-ketoglutarate transaminase
-
-
-
-
aspartate aminotransferase
aspartate aminotransferase 1
-
aspartate transaminase
-
-
aspartate-2-oxoglutarate transaminase
-
-
-
-
aspartate:2-oxoglutarate aminotransferase
-
-
-
-
aspartic acid aminotransferase
-
-
-
-
aspartic aminotransferase
-
-
-
-
aspartyl aminotransferase
-
-
-
-
AspAT
-
-
AspT
-
-
-
-
glutamate oxaloacetate transaminase
-
-
-
-
glutamate oxaloacetate transaminase 1
-
glutamate-oxalacetate aminotransferase
-
-
-
-
glutamate-oxalate transaminase
-
-
-
-
glutamate-oxaloacetate transaminase 1
-
glutamic oxalic transaminase
-
-
-
-
glutamic-aspartic aminotransferase
-
-
-
-
glutamic-aspartic transaminase
-
-
-
-
glutamic-oxalacetic transaminase
-
-
-
-
glutamic-oxaloacetic transaminase
-
-
-
-
GOT (enzyme)
-
-
-
-
L-aspartate transaminase
-
-
-
-
L-aspartate-2-ketoglutarate aminotransferase
-
-
-
-
L-aspartate-2-oxoglutarate aminotransferase
-
-
-
-
L-aspartate-2-oxoglutarate-transaminase
-
-
-
-
L-aspartate-alpha-ketoglutarate transaminase
-
-
-
-
L-aspartic aminotransferase
-
-
-
-
mitAAT
-
-
oxaloacetate transferase
-
-
-
-
oxaloacetate-aspartate aminotransferase
-
-
-
-
transaminase A
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis [7], some EC 2.6.1.57 activity can be found in this enzyme from other sources [8]; indeed the enzymes are identical in Trichomonas vaginalis [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9000-97-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
L-kynurenine + ?
kynurenic acid + ?
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-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(2,4-dichlorophenyl)-3-[2-(1H-indol-3-yl)ethyl]urea
-
1-(4-chlorophenyl)-3-[2-(1H-indol-3-yl)ethyl]urea
-
1-biphenyl-2-yl-3-[2-(1H-indol-3-yl)ethyl]urea
-
1-[2-(1H-indol-3-yl)ethyl]-3-phenylurea
-
1-[2-(1H-indol-3-yl)ethyl]-3-[3-(trifluoromethyl)phenyl]urea
-
1-[2-(1H-indol-3-yl)ethyl]-3-[4-(trifluoromethyl)phenyl]urea
-
4-(1H-indazol-4-yl)-N-phenylpiperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-(2-methylphenyl)piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-(3-methylphenyl)piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-(3-phenoxyphenyl)piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-(4-methylphenyl)piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-(propan-2-yl)piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-(pyridazin-4-yl)piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-(pyridin-3-yl)piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-(pyrimidin-5-yl)piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-[2-(trifluoromethyl)phenyl]piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-[3-(methylcarbamoyl)phenyl]piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-[3-(trifluoromethyl)phenyl]piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-[4-(methylcarbamoyl)phenyl]piperazine-1-carboxamide
-
4-(1H-indol-4-yl)-N-[4-(trifluoromethyl)phenyl]piperazine-1-carboxamide
-
4-(3-methoxyphenyl)-N-phenylpiperazine-1-carboxamide
-
4-(5-methyl-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
-
4-(6-chloro-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
-
4-(6-methyl-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
-
4-(7-chloro-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
-
4-(7-methyl-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
-
4-(methylsulfonyl)-N-phenylpiperazine-1-carboxamide
-
4-acetyl-N-phenylpiperazine-1-carboxamide
-
Maleate
-
78% inhibition of cytosolic isozyme at 4 mM, competitive to 2-oxoglutarate
N,4-diphenylpiperazine-1-carboxamide
-
N-(1,3-benzothiazol-5-yl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
-
N-(2,4-dichlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
-
N-(2-chlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
-
N-(3,5-dichlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
-
N-(3-chlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
-
N-(4-benzoylphenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
-
N-(4-chlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
-
N-phenyl-4-(propan-2-yl)piperazine-1-carboxamide
-
N-phenyl-4-(pyridin-4-yl)piperazine-1-carboxamide
-
N-phenyl-4-(quinolin-5-yl)piperazine-1-carboxamide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
rosiglitazone
-
10 nM, stimulates activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.06
2-oxoglutarate
-
cytosolic isozyme, pH 6.8, 37°C
22.5
L-aspartate
-
cytosolic isozyme, pH 6.8, 37°C
additional information
additional information
-
kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.72
Maleate
-
cytosolic isozyme, pH 6.8, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
1-(2,4-dichlorophenyl)-3-[2-(1H-indol-3-yl)ethyl]urea
Homo sapiens
at 37°C, pH not specified in the publication
0.036
1-(4-chlorophenyl)-3-[2-(1H-indol-3-yl)ethyl]urea
Homo sapiens
at 37°C, pH not specified in the publication
0.034
1-biphenyl-2-yl-3-[2-(1H-indol-3-yl)ethyl]urea
Homo sapiens
at 37°C, pH not specified in the publication
0.1
1-[2-(1H-indol-3-yl)ethyl]-3-phenylurea
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.062
1-[2-(1H-indol-3-yl)ethyl]-3-[3-(trifluoromethyl)phenyl]urea
Homo sapiens
at 37°C, pH not specified in the publication
0.039
1-[2-(1H-indol-3-yl)ethyl]-3-[4-(trifluoromethyl)phenyl]urea
Homo sapiens
at 37°C, pH not specified in the publication
0.1
4-(1H-indazol-4-yl)-N-phenylpiperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-(2-methylphenyl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-(3-methylphenyl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.039
4-(1H-indol-4-yl)-N-(3-phenoxyphenyl)piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-(4-methylphenyl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-(propan-2-yl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-(pyridazin-4-yl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-(pyridin-3-yl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-(pyrimidin-5-yl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.0113 - 0.085
4-(1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
0.1
4-(1H-indol-4-yl)-N-[2-(trifluoromethyl)phenyl]piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-[3-(methylcarbamoyl)phenyl]piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.014
4-(1H-indol-4-yl)-N-[3-(trifluoromethyl)phenyl]piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.1
4-(1H-indol-4-yl)-N-[4-(methylcarbamoyl)phenyl]piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.016
4-(1H-indol-4-yl)-N-[4-(trifluoromethyl)phenyl]piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.1
4-(3-methoxyphenyl)-N-phenylpiperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(5-methyl-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.046
4-(6-chloro-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.1
4-(6-methyl-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-(7-chloro-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.041
4-(7-methyl-1H-indol-4-yl)-N-phenylpiperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.1
4-(methylsulfonyl)-N-phenylpiperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
4-acetyl-N-phenylpiperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
N,4-diphenylpiperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.076
N-(1,3-benzothiazol-5-yl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.056
N-(2,4-dichlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.1
N-(2-chlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.022
N-(3,5-dichlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.052
N-(3-chlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.043
N-(4-benzoylphenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.0082
N-(4-chlorophenyl)-4-(1H-indol-4-yl)piperazine-1-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.1
N-phenyl-4-(propan-2-yl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
N-phenyl-4-(pyridin-4-yl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
0.1
N-phenyl-4-(quinolin-5-yl)piperazine-1-carboxamide
Homo sapiens
IC50 above 0.1 mM, at 37°C, pH not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
cytosolic isozyme
7.5
assay at, coupled assay with malate dehydrogenase
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 7.2
-
cytosolic isozyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at, coupled assay with malate dehydrogenase
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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?
AATM_HUMAN
430
0
47518
Swiss-Prot
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.99 A resolution, space group P1, with unit-cell parameters a = 56.7, b = 76.1, c = 94.2 A, alpha =78.0, beta =85.6, gamma = 78.4°
sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol 3350 5% (w/v) Cymal, and 0.1 M sodium acetate trihydrate (pH 4.5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S256A
the mutant shows 3.51% activity compared to the wild type enzyme
T110A
the mutant shows 2.45% activity compared to the wild type enzyme
T110A/S256A
inactive
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol, 64 weeks, less than 3% loss of activity
4°C, partially purified cytosolic isozyme, stable for 1 month, gradual decrease of activity afterwards
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Sephacryl S-200 gel filtration
isoenzyme mitAAT DEAE-Sepharose column chromatography
-
partial, 404fold, cytosolic isozyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli One Shot BL21 (DE3) cells
overexpressed as His6-tagged protein in Escherichia coli cells. The production of the protein corresponding to the gene GOT1L1 encounters several problems: upon induction, multiple overexpressed protein species are detected in the cell lysate, and none of them could be purified by metal-affinity chromatography
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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
medicine
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vessal, M.; Taher, M.
Partial purification and kinetic properties of human placental cytosolic aspartate transaminase
Comp. Biochem. Physiol. B
110
431-437
1995
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
Paknejad, M.; Emtiaz, S.; Khoobyari, M.M.; Gharb, M.T.; Yazdi, M.T.
Analysis of aspartate aminotransferase and alkaline phosphatase in crevicular fluid from implants with and without peri-implantitis
Implant Dent.
15
62-69
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
Tordjman, J.; Leroyer, S.; Chauvet, G.; Quette, J.; Chauvet, C.; Tomkiewicz, C.; Chapron, C.; Barouki, R.; Forest, C.; Aggerbeck, M.; Antoine, B.
Cytosolic aspartate aminotransferase: A new partner in adipocyte glyceroneogenesis and an atypical target of thiazolidinedione
J. Biol. Chem.
282
23591-23602
2007
Homo sapiens
Manually annotated by BRENDA team
Guidetti, P.; Amori, L.; Sapko, M.T.; Okuno, E.; Schwarcz, R.
Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain
J. Neurochem.
102
103-111
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Chang, M.L.; Yang, C.W.; Chen, J.C.; Ho, Y.P.; Pan, M.J.; Lin, C.H.; Lin, D.Y.
Disproportional exaggerated aspartate transaminase is a useful prognostic parameter in late leptospirosis
World J. Gastroenterol.
11
5553-5556
2005
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
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 (Q8NHS2)
Manually annotated by BRENDA team
Yang, Y.
Enhancing doxorubicin efficacy through inhibition of aspartate transaminase in triple-negative breast cancer cells
Biochem. Biophys. Res. Commun.
473
1295-1300
2016
Homo sapiens (P17174), Homo sapiens
Manually annotated by BRENDA team
Jiang, X.; Wang, J.; Chang, H.; Zhou, Y.
Recombinant expression, purification and crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase
Biosci. Trends
10
79-84
2016
Homo sapiens (P00505)
Manually annotated by BRENDA team
Zou, L.; Zhao, H.; Wang, D.; Wang, M.; Zhang, C.; Xiao, F.
Expression and purification of a functional recombinant aspartate aminotransferase (AST) from Escherichia coli
J. Microbiol. Biotechnol.
24
998-1003
2014
Homo sapiens (P00505)
Manually annotated by BRENDA team
Holt, M.C.; Assar, Z.; Beheshti Zavareh, R.; Lin, L.; Anglin, J.; Mashadova, O.; Haldar, D.; Mullarky, E.; Kremer, D.M.; Cantley, L.C.; Kimmelman, A.C.; Stein, A.J.; Lairson, L.L.; Lyssiotis, C.A.
Biochemical characterization and structure-based mutational analysis provide insight into the binding and mechanism of action of novel aspartate aminotransferase inhibitors
Biochemistry
57
6604-6614
2018
Homo sapiens (P17174)
Manually annotated by BRENDA team
Anglin, J.; Zavareh, R.B.; Sander, P.N.; Haldar, D.; Mullarky, E.; Cantley, L.C.; Kimmelman, A.C.; Lyssiotis, C.A.; Lairson, L.L.
Discovery and optimization of aspartate aminotransferase 1 inhibitors to target redox balance in pancreatic ductal adenocarcinoma
Bioorg. Med. Chem. Lett.
28
2675-2678
2018
Homo sapiens (P17174)
Manually annotated by BRENDA team