Key aromatic residues at subsites + 2 and + 3 of glycoside hydrolase family 31 α-glucosidase contribute to recognition of long-chain substrates

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 1, 2013, Pages 329-335

  Tagami, Takayoshi ^a   Okuyama, Masayuki ^a   Nakai, Hiroyuki ^a   Kim, Young Min ^a   Mori, Haruhide ^a   Taguchi, Kazunori ^b   Svensson, Birte ^c   Kimura, Atsuo ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b NATIONAL AGRICULTURAL RESEARCH CENTER FOR HOKKAIDO REGION   (Japan)

^c TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

Glucosidase; Aromatic residue; Glycoside hydrolase family 31; Subsite affinity; Substrate specificity

Indexed keywords

31 ALPHA GLYCOSIDASE; GLYCOSIDASE; MALTOTRIOSE; PHENYLALANINE; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS NIGER; CONTROLLED STUDY; ENZYME MODIFICATION; ENZYME STRUCTURE; MUTATION; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ALIGNMENT;

ALPHA-GLUCOSIDASES; AMINO ACID SUBSTITUTION; ASPERGILLUS NIGER; FUNGAL PROTEINS; MALTOSE; MUTATION, MISSENSE; OLIGOSACCHARIDES; PHENYLALANINE; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

ASPERGILLUS NIGER; BETA VULGARIS SUBSP. VULGARIS;

EID: 84871716252     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.08.007     Document Type: Article

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