Open AccessThe Amino‐Acid Sequence of the Dihydrofolate Reductase of a Trimethoprim‐Resistant Strain of Escherichia coli
Author(s) -
STONE David,
PHILLIPS Anthony W.,
BURCHALL James J.
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11284.x
Subject(s) - dihydrofolate reductase , escherichia coli , protease , peptide sequence , lytic cycle , biochemistry , sequence (biology) , strain (injury) , amino acid , biology , lysine , trimethoprim , staphylococcus aureus , enzyme , chemistry , bacteria , genetics , antibiotics , gene , virus , anatomy
The determination of the amino acid sequence of the dihydrofolate reductase from Escherichia coli RT500 is described. The sequence, comprising 159 residues, has been derived from automatic sequencing of the intact protein in conjunction with manual sequencing of lysine‐blocked tryptic peptides, Staphylococcus aureus protease peptides, and α‐lytic protease peptides. Comparison of the sequence with that of the dihydrofolate reductase from a methotrexate‐resistant strain of E. coli (MB1428) shows that 145 of the residues are identical. The distribution of the differences along the length of the molecule is discussed.