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Dihydroneopterin triphosphate epimerase of Escherichia coli: purification, genetic cloning, and expression.


ABSTRACT: The enzyme catalyzing the epimerization at position 2' of dihydroneopterin triphosphate was purified by a factor of about 10,000 from cell extract of Escherichia coli. The cognate gene was cloned, sequenced, expressed, and mapped to kb 2427 on the E. coli chromosome.

SUBMITTER: Haussmann C 

PROVIDER: S-EPMC178780 | biostudies-other | 1997 Feb

REPOSITORIES: biostudies-other

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Dihydroneopterin triphosphate epimerase of Escherichia coli: purification, genetic cloning, and expression.

Haussmann C C   Rohdich F F   Lottspeich F F   Eberhardt S S   Scheuring J J   Mackamul S S   Bacher A A  

Journal of bacteriology 19970201 3


The enzyme catalyzing the epimerization at position 2' of dihydroneopterin triphosphate was purified by a factor of about 10,000 from cell extract of Escherichia coli. The cognate gene was cloned, sequenced, expressed, and mapped to kb 2427 on the E. coli chromosome. ...[more]

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