New class of IMP cyclohydrolases in Methanococcus jannaschii

被引:18
作者
Graupner, M [1 ]
Xu, HM [1 ]
White, RH [1 ]
机构
[1] Virginia Polytech Inst & State Univ, Dept Biochem 0308, Blacksburg, VA 24061 USA
关键词
D O I
10.1128/JB.184.5.1471-1473.2002
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The enzyme responsible for observed IMP cyclohydrolase activity in Methanococcus jannaschii was purified and sequenced: its genetic locus was found to correspond to gene MJ0626. The MJ0626 gene was cloned, and its protein product was expressed in Escherichia coli and shown to catalyze the cyclization of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP. The enzyme has no sequence similarity to known enzymes, and its catalytic properties appear distinct from any characterized IMP cyclohydrolase. The purO gene for the enzyme is currently found only in the domain Archaea.
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页码:1471 / 1473
页数:3
相关论文
共 15 条
[11]   RADIOASSAY OF BIFUNCTIONAL 5-AMINOIMIDAZOLE-4-CARBOXAMIDE RIBOTIDE TRANSFORMYLASE-IMP CYCLOHYDROLASE BY THIN-LAYER CHROMATOGRAPHY [J].
SZABADOS, E ;
CHRISTOPHERSON, RI .
ANALYTICAL BIOCHEMISTRY, 1994, 221 (02) :401-404
[12]   STRUCTURES OF THE MODIFIED FOLATES IN THE THERMOPHILIC ARCHAEBACTERIA PYROCOCCUS-FURIOSUS [J].
WHITE, RH .
BIOCHEMISTRY, 1993, 32 (03) :745-753
[13]   DISTRIBUTION OF FOLATES AND MODIFIED FOLATES IN EXTREMELY THERMOPHILIC BACTERIA [J].
WHITE, RH .
JOURNAL OF BACTERIOLOGY, 1991, 173 (06) :1987-1991
[14]   Purine biosynthesis in the domain Archaea without folates or modified folates [J].
White, RH .
JOURNAL OF BACTERIOLOGY, 1997, 179 (10) :3374-3377