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Heterologous expression of peptidyl-Lys metallopeptidase of
Armillaria mellea
and mutagenic analysis of the recombinant peptidase
Anders Sebastian Rosenkrans Ødum, Søren Østergaard, Inga Nørby,
Morten Peter Meldal
, Kjeld Olesen
Department of Chemistry
1
Citation (Scopus)
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Dive into the research topics of 'Heterologous expression of peptidyl-Lys metallopeptidase of
Armillaria mellea
and mutagenic analysis of the recombinant peptidase'. Together they form a unique fingerprint.
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Biochemistry, Genetics and Molecular Biology
Heterologous Expression
100%
Metalloproteinase
100%
Armillaria
100%
Arginine
100%
Peptidase
100%
Metalloendopeptidase
100%
Protease
66%
Wild Type
66%
Lysine
33%
Enzyme Specificity
33%
Site-Directed Mutagenesis
33%
Mutagenesis
33%
Molecular Model
33%
Komagataella pastoris
33%
Immunology and Microbiology
Heterologous Expression
100%
Arginine
100%
Armillaria
100%
Wild Type
66%
Mutagenesis
33%
Enzyme Specificity
33%
Molecular Model
33%
Komagataella pastoris
33%
Site Directed Mutagenesis
33%
Lysine
33%
Pharmacology, Toxicology and Pharmaceutical Science
Peptidase
100%
Metalloproteinase
100%
Arginine
100%
Proteinase
66%
Site-Directed Mutagenesis
33%
Mutagenesis
33%
Lysine
33%
Substrate Specificity
33%
Komagataella pastoris
33%
Keyphrases
Armillaria Mellea
100%
Lys-N
100%