The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds

Journal of Molecular Biology

Volumn 301, Issue 2, 2000, Pages 433-450

  Toth, Eric A ^a   Worby, Carolyn ^b   Dixon, Jack E ^b   Goedken, Eric R ^c   Marqusee, Susan ^c   Yeates, Todd O ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Autism; Lyase; Purine biosynthesis; Thermal stability; elimination

Indexed keywords

ADENYLOSUCCINATE LYASE; BACTERIAL ENZYME; PURINE;

ARCHAEBACTERIUM; ARTICLE; BIOSYNTHESIS; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME STRUCTURE; GENE MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PURINE SYNTHESIS; THERMOSTABILITY;

ARCHAEA; BACTERIA (MICROORGANISMS); PYROBACULUM AEROPHILUM; THERMOTOGA MARITIMA;

EID: 0034636987     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3970     Document Type: Article

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