SCOPUS 정보 검색 플랫폼

Volumn 164, Issue 4, 2011, Pages 454-463

Investigating the structural and functional effects of mutating Asn glycosylation sites of Horseradish peroxidase to Asp

(3) Asad, Sedigheh a Khajeh, Khosro b Ghaemi, Nasser a

a UNIVERSITY OF TEHRAN (Iran)

b TARBIAT MODARES UNIVERSITY (Iran)

Author keywords

Glycosylation site; H2O2 inactivation; Protein stability; Recombinant horseradish peroxidase; Site directed mutagenesis

Indexed keywords

ACRYLAMIDES; ACTIVE SITE; ASPARAGINE RESIDUE; ASPARTIC ACIDS; BIOCATALYSIS; CATALYTIC ACTIVITY; CONFORMATIONAL CHANGE; DOUBLE MUTATION; H2O2 INACTIVATION; HORSERADISH PEROXIDASE; HYDROPHOBIC PATCH; MUTANT PROTEINS; NON-ADDITIVE; PROTEIN STABILITY; RECOMBINANT HORSERADISH PEROXIDASE; SITE DIRECTED MUTAGENESIS; THERMAL INACTIVATION;

AMIDES; AMINO ACIDS; BIOSENSORS; CATALYST ACTIVITY; ESCHERICHIA COLI; GLYCOSYLATION;

ESTERIFICATION;

4 AMINOPHENAZONE; ACRYLAMIDE; ASPARAGINE; ASPARTIC ACID; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; MUTANT PROTEIN; PHENOL; RECOMBINANT ENZYME;

ARTICLE; BINDING AFFINITY; BIOSENSOR; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME GLYCOSYLATION; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HETEROLOGOUS EXPRESSION; HYDROPHOBICITY; MUTATION; PROKARYOTE; PROTEIN EXPRESSION; STEADY STATE; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; ASPARAGINE; ASPARTIC ACID; CYTOSOL; ESCHERICHIA COLI; GLYCOSYLATION; HORSERADISH PEROXIDASE; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP;

ARMORACIA RUSTICANA; ESCHERICHIA COLI; PROKARYOTA;

EID: 79955807332 PISSN: 02732289 EISSN: None Source Type: Journal
DOI: 10.1007/s12010-010-9147-1 Document Type: Article

Times cited : (19)

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