Two-fold repeated (βα)4 half-barrels may provide a molecular tool for dual substrate specificity

EMBO Reports

Volumn 6, Issue 2, 2005, Pages 134-139

  Kuper, Jochen ^a   Doenges, Catharina ^b   Wilmanns, Matthias ^a  

^a DESY   (Germany)

^b UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Evolution of ( )8 barrels; Phosphoribosyl isomerase; Tryptophan and histidine biosynthesis

Indexed keywords

BACTERIAL PROTEIN; BETA,ALPHA4 HALF BARREL PROTEIN; ISOMERASE; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; HELICASE;

ARTICLE; BACTERIAL GENOME; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; GENETIC CODE; ISOMERIZATION; MOLECULAR GENETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; STEADY STATE; STREPTOMYCES COELICOLOR; AMINO ACID SEQUENCE; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; ISOLATION AND PURIFICATION; PROTEIN TERTIARY STRUCTURE;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLIZATION; DNA HELICASES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; STREPTOMYCES COELICOLOR; SUBSTRATE SPECIFICITY;

EID: 14644416029     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.embor.7400330     Document Type: Article

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