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The amino acid sequence of the trimethoprim resistant di hydro folate reductase ec 1.5.1.3 specified in escherichia coli by r plasmid r 67


Journal of Biological Chemistry 254(21): 10857-10861
The amino acid sequence of the trimethoprim resistant di hydro folate reductase ec 1.5.1.3 specified in escherichia coli by r plasmid r 67
The amino acid sequence of a trimethoprim-resistant dihydrofolate reductase (EC 1.5.1.3.) specified by the R-plasmid R67 is described. The sequence was deduced from automatic and manual sequence analysis of the intact protein, the fragments produced by CNBr cleavage and peptides derived from the largest CNBr fragment by digestion with trypsin. Staphylococcus aureus V8 protease, chymotrypsin and Lysobacter enzymogenes .alpha.-lytic protease. The complete sequence comprises 78 residues in a single polypeptide chain of MW 8444. No evidence of heterogeneity was obtained, indicating that all subunits of the native enzyme are identical. Comparison of the sequence with that of all known dihydrofolate reductases shows no significant sequence homology.


Accession: 006599393



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