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Dolichol kinases from yeast, nematode and human can replace each other and exchange their domains cr...

Dolichol kinases from yeast, nematode and human can replace each other and exchange their domains cr...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_3125995086

Dolichol kinases from yeast, nematode and human can replace each other and exchange their domains creating active chimeric enzymes in yeast

About this item

Full title

Dolichol kinases from yeast, nematode and human can replace each other and exchange their domains creating active chimeric enzymes in yeast

Publisher

United States: Public Library of Science

Journal title

PloS one, 2024-11, Vol.19 (11), p.e0313330

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Protein glycosylation is a fundamental modification crucial for numerous intra- and extracellular functions in all eukaryotes. The phosphorylated dolichol (Dol-P) is utilized in N-linked protein glycosylation and other glycosylation pathways. Dolichol kinase (DK) plays a key role in catalyzing the phosphorylation of dolichol. The glycosylation patt...

Alternative Titles

Full title

Dolichol kinases from yeast, nematode and human can replace each other and exchange their domains creating active chimeric enzymes in yeast

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_3125995086

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_3125995086

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0313330

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