Crystal structure of maltose phosphorylase from Lactobacillus brevis: Unexpected evolutionary relationship with glucoamylases

Structure

Volumn 9, Issue 8, 2001, Pages 689-697

  Egloff, Marie Pierre ^a   Uppenberg, Jonas ^b   Haalck, Lutz ^c   van Tilbeurgh, Herman ^a  

^a CNRS   (France)

^b Pharmacia Corporation   (Sweden)

^c UNIVERSITY HOSPITAL MÜNSTER   (Germany)

Author keywords

( )6 barrel; Evolution; Glucoamylase; Maltose phoshorylase; Structure

Indexed keywords

ACID; BACTERIAL ENZYME; CARBOHYDRATE DERIVATIVE; CARBON; CARBOXYLIC ACID DERIVATIVE; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLUTAMIC ACID; MALTOSE PHOSPHORYLASE; PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS AWAMORI; CATALYST; CHEMICAL BOND; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; LACTOBACILLUS BREVIS; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ANALYSIS;

BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; EVOLUTION, MOLECULAR; GLUCAN 1,4-ALPHA-GLUCOSIDASE; GLUCOSE; GLUCOSEPHOSPHATES; GLUCOSYLTRANSFERASES; LACTOBACILLUS; MODELS, MOLECULAR; PHOSPHATES;

ASPERGILLUS AWAMORI; BACTERIA (MICROORGANISMS); LACTOBACILLUS BREVIS;

EID: 0034885657     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00626-8     Document Type: Article

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