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AF049: ATP:guanido phosphotransferase
Biochemical properties
ATP:guanido phosphotransferases are a family of structurally and functionally related enzymes that reversibly catalyze the transfer of phosphate between ATP and various phosphogens. The substrate binding site is located in the cleft between N and C-terminal domains [1].
Allergens from this family
Allergenic members of this family are arginine kinases. These are minor allergens from crustaceans, mites, and insects [2, 3].
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References
- Strong SJ, Ellington WR:
Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues.
Biochim Biophys Acta 1995, 1246, 197-200. [PubMed]
- Pedrosa M, Boyano-Martinez T, Garcia-Ara C, Quirce S:
Shellfish Allergy: a Comprehensive Review.
Clin Rev Allergy Immunol 2015, 49, 203-16. [PubMed] [Full Text]
- Binder M, Mahler V, Hayek B, Sperr WR, 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.
J Immunol 2001, 167, 5470-7. [PubMed]
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Links to Pfam
Family-defining Pfam domains (at least one of these domains is present in each family member):
Pfam domain |
Pfam clan |
PF00217
|
ATP:guanido phosphotransferase, C-terminal catalytic domain
|
CL0286
|
gamma-glutamylcysteine synthetase/glutamine synthetase clan
|
PF02807
|
ATP:guanido phosphotransferase, N-terminal domain
|
- | |
Links to Wikipedia
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