The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase

EMBO Journal

Volumn 16, Issue 1, 1997, Pages 1-14

  Watson, K A ^a   Schinzel, R ^b   Palm, D ^b   Johnson, L N ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

Bacteria; maltodextrin; Phosphorylase; Regulation; X ray structure

Indexed keywords

BACTERIAL ENZYME; DIMER; GLYCOGEN PHOSPHORYLASE; MALTODEXTRIN; PHOSPHORYLASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

EID: 0031014875     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.1.1     Document Type: Article

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