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Literature summary for 2.7.3.3 extracted from

  • Binder, M.; Mahler, V.; Hayek, B.; Sperr, W.R.; Scholler, M.; Prozell, S.; Wiedermann, G.; Valent, P.; Valenta, R.; Duchene, M.
    Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen (2001), J. Immunol., 167, 5470-5477.
    View publication on PubMed

Application

Application Comment Organism
medicine the recombinant enzyme may be used to identify a group of polysensitized indoor allergic patients and for immunotheraphy of theses individuals Plodia interpunctella

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli as a histidine-tagged protein Plodia interpunctella

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-Arg Plodia interpunctella the enzyme is involved in the storage of the high-energy phosphate reserve phosphoarginine ADP + Nomega-phospho-L-Arg
-
?

Organism

Organism UniProt Comment Textmining
Plodia interpunctella
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Plodia interpunctella

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Arg
-
Plodia interpunctella ADP + Nomega-phospho-L-Arg
-
?
ATP + L-Arg the enzyme is involved in the storage of the high-energy phosphate reserve phosphoarginine Plodia interpunctella ADP + Nomega-phospho-L-Arg
-
?