Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: Thermostability and 1.8 Å resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate

Journal of Molecular Biology

Volumn 326, Issue 1, 2003, Pages 203-216

  Van Boxstael, Sigrid ^a   Cunin, Raymond ^a   Khan, Shakil ^a,c   Maes, Dominique ^b  

^a VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^c Bangladesh Atomic Energy Commission   (Bangladesh)

Author keywords

Crystal structure; Hyperthermophilic aspartate transcarbamylase; P. abyssi; Thermostability

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; HOLOENZYME; PHOSPHATE; SPARFOSIC ACID;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME PURIFICATION; ESCHERICHIA COLI; HIGH TEMPERATURE; NONHUMAN; PRIORITY JOURNAL; PYROCOCCUS ABYSSI; THERMOSTABILITY;

ARCHAEA; ESCHERICHIA COLI; PYROCOCCUS; PYROCOCCUS ABYSSI;

EID: 0037423708     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01228-7     Document Type: Article

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