THE CRYSTALLOGRAPHIC STRUCTURE OF A HUMAN DIHYDROPTERIDINE REDUCTASE NADH BINARY COMPLEX EXPRESSED IN ESCHERICHIA-COLI BY A CDNA CONSTRUCTED FROM ITS RAT HOMOLOG

Authors
SU Y VARUGHESE KI XUONG NH BRAY TL ROCHE DJ WHITELEY JM
Citation
Y. Su et al., THE CRYSTALLOGRAPHIC STRUCTURE OF A HUMAN DIHYDROPTERIDINE REDUCTASE NADH BINARY COMPLEX EXPRESSED IN ESCHERICHIA-COLI BY A CDNA CONSTRUCTED FROM ITS RAT HOMOLOG, The Journal of biological chemistry, 268(36), 1993, pp. 26836-26841
Citations number
31
Categorie Soggetti
Biology
Journal title
The Journal of biological chemistry → ACNP
ISSN journal
00219258
Volume
268
Issue
36
Year of publication
1993
Pages
26836 - 26841
Database
ISI
SICI code
0021-9258(1993)268:36<26836:TCSOAH>2.0.ZU;2-A
Abstract
A human dihydropteridine reductase (EC 1.6.99.10) has been created fro m a rat cDNA clone by a single five-oligonucleotide mutagenesis reacti on and expressed in good yield in Escherichia coli. The enzyme has bee n purified to homogeneity, and kinetic identity to the naturally occur ring enzyme has been proven. Crystallization has also been achieved, a nd the crystal structure was solved using 2.5 angstrom data that was r efined to an R value of 16.9%. The structure described in this report represents the first complete structural characterization of this impo rtant human enzyme.