## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a βFull Textβ option. The original article is trackable v
Primary structure of E. coli dihydrofolate reductase
β Scribed by BENNETT, CARL D.
- Book ID
- 109693674
- Publisher
- Nature Publishing Group
- Year
- 1974
- Tongue
- English
- Weight
- 250 KB
- Volume
- 252
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/252511c0
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Two site-specific mutations of dihydrofolate reductase from Escherichiu coli based on the x-ray crystallographic structure were constructed. The first mutation (His-45 + Gln) is aimed at assessing the interaction between the imidazole moiety and the pyrophosphate backbone of NADPH. The second (Thr-1
The dihydrofolate reductase gene of Saccharornyces cerevisiae has been isolated by selection of trimethoprim resistant Escherichia coli transformed with a gene bank of yeast DNA in plasmid pBR322. From a 9.2 kilobase pair BamHI DNA fragment this gene has been localized to a 1.76 kb fragment, the res
Trimethoprim inhibits dihydrofolate reductase. Mutations conferring trimethorpim-resistance on E coli K12 result in either an altered reductase with decreased affinity for the drug, or in 2-30 fold higher levels of the enzyme. Studies of the latter class of mutants indicate that dihydrofolate reduct