Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe52 → Ala and Phe52 → Asn mutants

FEBS Letters

Volumn 585, Issue 3, 2011, Pages 499-504

  Wildberger, Patricia ^a   Luley Goedl, Christiane ^a   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

Aromatic stacking; Cation interaction; GH 13; Glycoside hydrolase; Glycosyltransferase; Oxocarbenium ion; Sucrose phosphorylase

Indexed keywords

ALANINE; AROMATIC AMINO ACID; ASPARAGINE; CATION; CHEMICAL COMPOUND; OXOCARBENIUM; PHENYLALANINE; PHOSPHORYLASE; SUCROSE PHOSPHORYLASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME GLYCOSYLATION; ENZYME STABILITY; GLUCOSE TRANSPORT; HYDROLYSIS; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BIOCATALYSIS; CATALYTIC DOMAIN; GLUCOSE; GLUCOSYLTRANSFERASES; KINETICS; LEUCONOSTOC; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PHENYLALANINE; PROTEIN BINDING; RECOMBINANT PROTEINS;

LEUCONOSTOC MESENTEROIDES;

EID: 79551502426     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.12.041     Document Type: Article

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