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Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control.

Abstract:

Tyrosinase is a copper-containing enzyme that regulates melanin biosynthesis in mammals. Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation. To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants. W...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.275.11.8169

Authors


Branza-Nichita, N More by this author
Negroiu, G More by this author
Petrescu, AJ More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Pharmacology
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Journal:
The Journal of biological chemistry
Volume:
275
Issue:
11
Pages:
8169-8175
Publication date:
2000-03-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:724a4c93-f2e9-454e-9397-7b04b27cfc3e
Source identifiers:
99854
Local pid:
pubs:99854

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