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Literature summary for 1.14.18.1 extracted from

  • Branza-Nichita, N.; Negroiu, G.; Petrescu, A.J.; Garman, E.F.; Platt, F.M.; Wormald, M.R.; Dwek, R.A.; Petrescu, S.M.
    Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control (2000), J. Biol. Chem., 275, 8169-8175.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type, N86Q, N111Q, N337Q, N371Q and several double and triple mutant enzymes derived from this single mutants in CHO cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
N111Q mutation in potential N-glycosylation site, 95% of wild-type L-dopa oxidase activity Homo sapiens
N111Q/N337Q mutations in potential N-glycosylation site, 95% of wild-type L-dopa oxidase activity Homo sapiens
N111Q/N337Q/N371Q mutations in potential N-glycosylation site, no L-dopa oxidase activity Homo sapiens
N111Q/N371Q mutations in potential N-glycosylation site, 59% of wild-type L-dopa oxidase activity Homo sapiens
N337Q mutation in potential N-glycosylation site, 93% of wild-type L-dopa oxidase activity Homo sapiens
N337Q/N3711Q mutations in potential N-glycosylation site, 37% of wild-type L-dopa oxidase activity Homo sapiens
N371Q mutation in potential N-glycosylation site, 64% of wild-type L-dopa oxidase activity Homo sapiens
N86Q mutation in potential N-glycosylation site, 70% of wild-type L-dopa oxidase activity Homo sapiens
N86Q/N111Q mutations in potential N-glycosylation site, 68% of wild-type L-dopa oxidase activity Homo sapiens
N86Q/N111Q/N337Q mutations in potential N-glycosylation site, no L-dopa oxidase activity Homo sapiens
N86Q/N111Q/N337Q/N371Q mutations in potential N-glycosylation site, no L-dopa oxidase activity Homo sapiens
N86Q/N111Q/N371Q mutations in potential N-glycosylation site, no L-dopa oxidase activity Homo sapiens
N86Q/N337Q mutations in potential N-glycosylation site, 35% of wild-type L-dopa oxidase activity Homo sapiens
N86Q/N337Q/N371Q mutations in potential N-glycosylation site, no L-dopa oxidase activity Homo sapiens
N86Q/N371Q mutations in potential N-glycosylation site, 30% of wild-type L-dopa oxidase activity, contains at least 3 times less copper than wild-type Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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