Amino-Acid Sequence of Dihydrofolate Reductase from a Methotrexate-resistant Mutant of Streptococcus faecium and Identification of Methionine Residues at the Inhibitor Binding Site
- 1 August 1974
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 71 (8) , 3001-3005
- https://doi.org/10.1073/pnas.71.8.3001
Abstract
The amino-acid sequence of dihydrofolate reductase (7,8-dihydrofolate:NADP(+) oxidoreductase, EC 1.5.1.4) from S. faecium var Durans strain A is reported, and methionine residues 28 and 50 are shown to be protected by the inhibitor aminopterin from carboxymethylation by iodoacetate which occurs in absence of the inhibitor. Comparison of the sequence with that of the Escherichia coli reductase reveals two domains of considerable homology, one (the N-terminal region) presumably concerned with dihydrofolate and inhibitor binding and the other with dinucleotide binding. No significant sequence homology was found between larger dehydrogenases and the dihydrofolate reductases, which must, therefore, have evolved from a different ancestral protein.Keywords
This publication has 19 references indexed in Scilit:
- COMPARATIVE BIOCHEMISTRY OF DIHYDROFOLATE REDUCTASEAnnals of the New York Academy of Sciences, 1971
- Immunochemistry of sperm whale of myoglobin. IX. Specific interaction of peptides obtained by cleavage at arginine peptide bondsBiochemistry, 1971
- The amino acid sequence of T4 phage lysozyme. IV. Dilute acid hydrolysis and the order of tryptic peptides.1970
- An evaluation of the relatedness of proteins based on comparison of amino acid sequencesJournal of Molecular Biology, 1970
- Amino acid sequence of bovine carboxypeptidase A. II. Tryptic and chymotryptic peptides of the cyanogen bromide fragment F111Biochemistry, 1969
- Amino acid sequence of bovine carboxypeptidase A. III. Specificity of peptide-bond cleavage by thermolysin and the complete sequence of the cyanogen bromide fragment F111Biochemistry, 1969
- Dihydrofolate reductase of Streptococcus faicium. II. Purification and some properties of two dihydrofolate reductases from the amethopterin-resistant mutant Streptococcus faecium var. Durans strain A.1968
- Critical evaluation of the selective tritiation method of determining C-terminal amino acids and its application to luteinizing hormoneBiochemistry, 1968
- Anwendung der dünnschichtchromatographie zur sequenzanalyse von peptiden : Mitt. Untersuchungen über den abbau von peptiden mit phenylisothiocyanatJournal of Chromatography A, 1966
- DIHYDROFOLATE REDUCTASE OF STREPTOCOCCUS FAECALIS .1. PURIFICATION AND SOME PROPERTIES OF REDUCTASE FROM WILD STRAIN AND FROM STRAIN A1966