Structures of chitobiase mutants complexed with the substrate di-N-acetyl-D-glucosamine: The catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540

Journal of Molecular Biology

Volumn 300, Issue 3, 2000, Pages 611-617

  Prag, G ^a   Papanikolau, Y ^b   Tavlas, G ^b   Vorgias, C E ^c   Petratos, K ^b   Oppenheim, A B ^a  

^a HEBREW UNIVERSITY   (Israel)

^b INSTITUTE OF MOLECULAR BIOLOGY AND BIOTECHNOLOGY   (Greece)

^c UNIVERSITY OF ATHENS   (Greece)

Author keywords

Catalytic mechanism; Crystal structure; Hexosaminidase; Serratia marcescens; N acetylhexosaminidase

Indexed keywords

ASPARTIC ACID; BETA N ACETYLHEXOSAMINIDASE; GLUCOSAMINE DERIVATIVE; GLUTAMIC ACID; MUTANT PROTEIN; N ACETYLGLUCOSAMINE;

ARTICLE; BASE PAIRING; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT; SERRATIA MARCESCENS; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

EID: 0034647424     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3906     Document Type: Article

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