High resolution structure and sequence of T. aurantiacus Xylanase I: Implications for the evolution of thermostability in family 10 Xylanases and enzymes with βα-barrel architecture

Proteins: Structure, Function and Genetics

Volumn 36, Issue 3, 1999, Pages 295-306

  Lo Leggio, Leila ^a,b   Kalogiannis, S ^a,c   Bhat, M K ^a   Pickersgill, R W ^a  

^a INSTITUTE OF FOOD RESEARCH   (United Kingdom)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c Hellenic Sugar Industry SA   (Greece)

Author keywords

barrel; Family 10; Glycosyl hydrolase; Thermostability; Xylanase

Indexed keywords

FUNGAL PROTEIN; GLYCOSIDASE; PROLINE; XYLAN ENDO 1,3 BETA XYLOSIDASE;

ARTICLE; CRYSTALLIZATION; DIPOLE; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; FUNGUS; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; X RAY ANALYSIS;

AMINO ACID SEQUENCE; ASCOMYCOTA; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ENZYME STABILITY; EVOLUTION, MOLECULAR; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; XYLAN ENDO-1,3-BETA-XYLOSIDASE; XYLOSIDASES;

FUNGI; THERMOASCUS AURANTIACUS;

EID: 0033567040     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19990815)36:3<295::AID-PROT4>3.0.CO;2-6     Document Type: Article

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