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Literature summary for 2.3.2.8 extracted from

  • Saha, S.; Wang, J.; Buckley, B.; Wang, Q.; Lilly, B.; Chernov, M.; Kashina, A.
    Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis (2012), Biochem. Pharmacol., 83, 866-873.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
aurothioglucose complete inhibition at 0.003 mM Mus musculus
Disulfiram complete inhibition at 0.003 mM Mus musculus
merbromin
-
Mus musculus
Reactive blue 2
-
Mus musculus
suramin complete inhibition at 0.001 mM Mus musculus
Tannic acid complete inhibition at 0.001 mM Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginyl-tRNAArg + bovine serum albumin
-
Mus musculus tRNAArg + L-arginyl-[bovine serum albumin]
-
?
L-arginyl-tRNAAsp + beta-actin
-
Mus musculus tRNAAsp + L-arginyl-[beta-actin]
-
?

Synonyms

Synonyms Comment Organism
Ate1
-
Mus musculus

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00028
-
in 50 mM HEPES pH 7.5, 25 mM KCl, 15 mM MgCl2, 0.1 mM dithiothreitol, at 37°C Mus musculus Tannic acid
0.00034
-
in 50 mM HEPES pH 7.5, 25 mM KCl, 15 mM MgCl2, 0.1 mM dithiothreitol, at 37°C Mus musculus merbromin
0.00043
-
in 50 mM HEPES pH 7.5, 25 mM KCl, 15 mM MgCl2, 0.1 mM dithiothreitol, at 37°C Mus musculus suramin
0.00097
-
in 50 mM HEPES pH 7.5, 25 mM KCl, 15 mM MgCl2, 0.1 mM dithiothreitol, at 37°C Mus musculus Reactive blue 2

General Information

General Information Comment Organism
malfunction impairments of arginyltransferase ATE1 are implicated in congenital heart defects, obesity, cancer, and neurodegeneration Mus musculus
physiological function posttranslational arginylation mediated by arginyltransferase (ATE1) is an emerging major regulator of embryogenesis and cell physiology Mus musculus