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softwareStructure of the phosphoribosylglycinamide formimidoyltransferase catalytic
domain of Escherichia coli dihydrofolate reductase. A deletion mutant of Escherichia coli
dihydrofolate reductase (DHFR) lacking eight amino acids near the C terminus of theprotein was constructed and characterized. The mutant protein has properties similar to
those of wild type DHFR, including turnover rate and heat stability. However, the mutant
DHFR cannot catalyze the thymidylate formation reaction of de novo pyrimidine
biosynthesis. Thus, the eight residues near the C terminus of wild-type DHFR are required

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for activity. The mutant protein contains an intact catalytic domain. The catalytic domain ofthe mutant DHFR was isolated and purified using the proline-dependent protease bacilluslicheniformis P60. The catalytic domain of the mutant DHFR has the same physicalproperties as that of wild-type DHFR, and its subunit structure is indistinguishable from thatof wild-type DHFR by polyacrylamide gel electrophoresis, gel filtration, andultracentrifugation. The catalytic domain of the mutant DHFR was digested withchymotrypsin and the sequences of the fragments were determined. The partial peptide map
shows that the amino-terminal amino acid sequence of the catalytic domain of the mutant
DHFR is the same as that of wild-type DHFR. The sequences of two other peptides werealso the same as those of the corresponding peptides of wild-type DHFR. The carboxylterminal sequences were determined from the amino-terminal sequences and thechromatographic and electrophoretic behavior of the fragments of the catalytic domain of
the mutant DHFR. The amino-terminal sequences of three peptides from the catalytic
domain of the mutant DHFR were the same as those of the corresponding peptides of wildtype DHFR,
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