Atypical transient state kinetics of recombinant human dihydrofolate reductase produced by hysteretic behavior

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Atypical transient state kinetics of recombinant human dihydrofolate reductase produced by hysteretic behavior. Comparison with dihydrofolate reductases from other sources.

The transient state kinetics of catalysis for dihydrofolate reductase (DHFR) from several enzyme sources including highly purified recombinant human enzyme (rHDHFR) have been examined. Like DHFR from Escherichia coli, the enzyme from Lactobacillus casei, and isoenzyme 2 from Streptococcus faecium exhibit a slow increase in activity upon addition of substrates to enzyme. No slow hysteresis of th...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1989

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)81659-9