| Literature DB >> 8262916 |
Y Su1, K I Varughese, N H Xuong, T L Bray, D J Roche, J M Whiteley.
Abstract
A human dihydropteridine reductase (EC 1.6.99.10) has been created from a rat cDNA clone by a single five-oligonucleotide mutagenesis reaction and expressed in good yield in Escherichia coli. The enzyme has been purified to homogeneity, and kinetic identity to the naturally occurring enzyme has been proven. Crystallization has also been achieved, and the crystal structure was solved using 2.5 A data that was refined to an R value of 16.9%. The structure described in this report represents the first complete structural characterization of this important human enzyme.Entities:
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Year: 1993 PMID： 8262916 DOI： 10.2210/pdb1hdr/pdb
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157