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Volumn 277, Issue 6, 2002, Pages 4166-4175

Mutational analysis of duck δ2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase

(3) Sampaleanu, Liliana M a Yu, Bomina b Lynne Howell, P a

a HOSPITAL FOR SICK CHILDREN RESEARCH INSTITUTE (Canada)

b UNIVERSITY OF TORONTO (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; MUTAGENESIS;

FUMARATE MOIETY;

ENZYMES;

ARGININE; ARGININOSUCCINATE LYASE; ASPARAGINE; ASPARTIC ACID; CITRULLINE; CRYSTALLIN; FUMARIC ACID; HISTIDINE; LYSINE; SERINE; THREONINE; WATER;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; ARGININOSUCCINATE LYASE; BINDING SITES; CATALYSIS; CIRCULAR DICHROISM; CRYSTALLINS; DUCKS; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

ANAS SP.; AVES;

EID: 0037040187 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M107465200 Document Type: Article

Times cited : (30)

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