Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli.

Article Details

Citation

Bennett CD, Rodkey JA, Sondey JM, Hirschmann R

Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli.

Biochemistry. 1978 Apr 4;17(7):1328-37.

PubMed ID
350268 [ View in PubMed
]
Abstract

The determination of the amino acid sequence of the enzyme dihydrofolate reductase (5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase, EC 1.5.1.3) from a mutant of Escherichia coli B is described. The 159 residues were positioned by automatic Edman degradation of the whole protein, of the reduced and alkylated cyanogen bromide fragments, and of selected tryptic, chymotryptic, and thermolytic digestion products. An N-bromosuccinimide produced fragment of the largest cyanogen bromide peptide was also used in the sequence determination.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Dihydrofolate reductaseP0ABQ4Details