Human salivary α-amylase Trp58 situated at subsite -2 is critical for enzyme activity

European Journal of Biochemistry

Volumn 271, Issue 12, 2004, Pages 2517-2529

  Ramasubbu, Narayanan ^a   Ragunath, Chandran ^a   Mishra, Prasunkumar J ^a   Thomas, Leonard M ^b   Gyémánt, Gyöngyi ^c   Kandra, Lili ^c  

^a UNIVERSITY OF MEDICINE AND DENTISTRY OF NEW JERSEY   (United States)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^c UNIVERSITY OF DEBRECEN   (Hungary)

Author keywords

Crystal structure; Oligosaccharide hydrolysis; Salivary amylase; Site directed mutagenesis; Subsite engineering

Indexed keywords

ACARBOSE; ALANINE; AMYLASE; GLUCOSE; LEUCINE; MALTOSE; OLIGOSACCHARIDE; STARCH; TRYPTOPHAN; TYROSINE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; DENSITY; ELECTRON; ENZYME ACTIVITY; GLYCOSYLATION; HYDROLYSIS; KINETICS; NONHUMAN; PRIORITY JOURNAL; SALIVA; WILD TYPE;

ALPHA-AMYLASE; BINDING SITES; GLYCOSIDES; HUMANS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; OLIGOSACCHARIDES; PROTEIN STRUCTURE, SECONDARY; SALIVA; TRYPTOPHAN;

FELIS CATUS;

EID: 3042554260     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04182.x     Document Type: Article

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