A single free cysteine residue and bisulfide bond contribute to the thermostability of Aspergillus saitoi 1,2-α-mannosidase

Bioscience, Biotechnology and Biochemistry

Volumn 69, Issue 11, 2005, Pages 2101-2108

  Tatara, Yota ^a   Yoshida, Takashi ^b   Ichishima, Eiji ^a  

^a SOKA UNIVERSITY   (Japan)

^b HIROSAKI UNIVERSITY   (Japan)

Author keywords

Cysteine; Free thiol group; Hydrophobic interaction; Mannosidase; Thermostability

Indexed keywords

CHEMICAL BONDS; ENZYMES; HYDROPHILICITY; HYDROPHOBICITY; MUTAGENESIS; NITROGEN COMPOUNDS;

CYSTEINE; FREE THIOL GROUP; HYDROPHOBIC INTERACTION; MANNOSIDASE; THERMOSTABILITY;

PROTEINS;

CYSTEINE; DISULFIDE; MANNOSIDASE; MANNOSYL OLIGOSACCHARIDE 1,2 ALPHA MANNOSIDASE; MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE;

ARTICLE; ASPERGILLUS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; HEAT; HYDROPHOBICITY; KINETICS; METABOLISM; PROTEIN DENATURATION; SITE DIRECTED MUTAGENESIS;

ASPERGILLUS; CYSTEINE; DISULFIDES; ENZYME STABILITY; HEAT; HYDROPHOBICITY; KINETICS; MANNOSIDASES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION;

ASPERGILLUS; ASPERGILLUS SAITOI;

EID: 28244499526     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.69.2101     Document Type: Article

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