Glutamic acid gamma-monohydroxamate and hydroxylamine are alternate substrates for Escherichia coli asparagine synthetase B

Biochemistry
S K BoehleinN G Richards

Abstract

Escherichia coli asparagine synthetase B (AS-B) catalyzes the synthesis of asparagine from aspartic acid and glutamine in an ATP-dependent reaction. The ability of this enzyme to employ hydroxylamine and L-glutamic acid gamma-monohydroxamate (LGH) as alternative substrates in place of ammonia and L-glutamine, respectively, has been investigated. The enzyme is able to function as an amidohydrolase, liberating hydroxylamine from LGH with high catalytic efficiency, as measured by k(cat)/K(M). In addition, the kinetic parameters determined for hydroxylamine in AS-B synthetase activity are very similar to those of ammonia. Nitrogen transfer from LGH to yield aspartic acid beta-monohydroxamate is also catalyzed by AS-B. While such an observation has been made for a few members of the trpG amidotransferase family, our results appear to be the first demonstration that nitrogen transfer can occur from glutamine analogs in a purF amidotransferase. However, k(cat)/K(M) for the ATP-dependent transfer of hydroxylamine from LGH to aspartic acid is reduced 3-fold relative to that for glutamine-dependent asparagine synthesis. Further, the AS-B mutant in which asparagine is replaced by alanine (N74A) can also use hydroxylamine as an alternate s...Continue Reading

References

May 1, 1992·Quarterly Reviews of Biophysics·D Shortle
May 5, 1986·Journal of Molecular Biology·F W Studier, B A Moffatt
Jun 20, 1965·Journal of the American Chemical Society·J R WHITAKER, M L BENDER

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Citations

Apr 23, 2003·Archives of Biochemistry and Biophysics·Alan R TessonN G J Richards
Jul 8, 2000·Journal of Inorganic Biochemistry·I GoldwaserY Shechter
Oct 30, 2004·European Journal of Biochemistry·Faylene A Lunn, Stephen L Bearne
Apr 9, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·X HuangJ W Keillor
Sep 28, 1998·Biochemistry·S K BoehleinS M Schuster

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