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Gene Review

asnB  -  asparagine synthetase B

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0662, JW0660
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Disease relevance of asnB


High impact information on asnB


Chemical compound and disease context of asnB


Biological context of asnB

  • The nucleotide sequence of asnB and the flanking sequences were determined [1].
  • Transcription analyses revealed that asnB was possibly cotranscribed with a downstream gene, ytnA, while the asnH gene was transcribed as the fourth gene of an operon comprising yxbB, yxbA, yxnB, asnH, and yxaM [3].
  • In contrast, deletion of asnB led to a slow-growth phenotype, even in the presence of asparagine [3].
  • The implication of this model is that the two active sites in AS-B become coordinated only after formation of a beta-aspartyl-AMP intermediate in the synthetase site of the enzyme [7].
  • The site-directed chemical modifier [p-(fluorosulfonyl)benzoyl]adenosine (5'-FSBA) inactivates Escherichia coli asparagine synthetase B activity following pseudo-first-order kinetics, with ATP providing specific protection, with a Kd of 12 microM [8].

Associations of asnB with chemical compounds

  • A purF type glutamine amide transfer domain was identified upon inspection of the amino-terminal amino acid sequence of the asparagine synthetase B protein [1].
  • Nitrogen transfer from LGH to yield aspartic acid beta-monohydroxamate is also catalyzed by AS-B [6].
  • In addition, the kinetic parameters determined for hydroxylamine in AS-B synthetase activity are very similar to those of ammonia [6].
  • While cysteine sulfinic acid did not itself constitute a clinically useful inhibitor of asparagine synthetase B, these results suggested that replacing this linkage by a more stable analogue might lead to a more potent inhibitor [9].
  • Radiolabeled protein is not observed (i) when the wild-type enzyme is incubated with 6-diazo-5-oxo-L-norleucine (DON) prior to reaction with [14C]glutamine or (ii) when the C1A AS-B mutant is incubated with [14C]-L-glutamine [10].


  1. Nucleotide sequence of Escherichia coli asnB and deduced amino acid sequence of asparagine synthetase B. Scofield, M.A., Lewis, W.S., Schuster, S.M. J. Biol. Chem. (1990) [Pubmed]
  2. Transfer RNA-dependent amino acid biosynthesis: an essential route to asparagine formation. Min, B., Pelaschier, J.T., Graham, D.E., Tumbula-Hansen, D., Söll, D. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Three asparagine synthetase genes of Bacillus subtilis. Yoshida, K., Fujita, Y., Ehrlich, S.D. J. Bacteriol. (1999) [Pubmed]
  4. Mutagenesis and chemical rescue indicate residues involved in beta-aspartyl-AMP formation by Escherichia coli asparagine synthetase B. Boehlein, S.K., Walworth, E.S., Richards, N.G., Schuster, S.M. J. Biol. Chem. (1997) [Pubmed]
  5. Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad. Boehlein, S.K., Richards, N.G., Schuster, S.M. J. Biol. Chem. (1994) [Pubmed]
  6. Glutamic acid gamma-monohydroxamate and hydroxylamine are alternate substrates for Escherichia coli asparagine synthetase B. Boehlein, S.K., Schuster, S.M., Richards, N.G. Biochemistry (1996) [Pubmed]
  7. Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli. Tesson, A.R., Soper, T.S., Ciustea, M., Richards, N.G. Arch. Biochem. Biophys. (2003) [Pubmed]
  8. Identification of cysteine-523 in the aspartate binding site of Escherichia coli asparagine synthetase B. Boehlein, S.K., Walworth, E.S., Schuster, S.M. Biochemistry (1997) [Pubmed]
  9. Characterization of inhibitors acting at the synthetase site of Escherichia coli asparagine synthetase B. Boehlein, S.K., Nakatsu, T., Hiratake, J., Thirumoorthy, R., Stewart, J.D., Richards, N.G., Schuster, S.M. Biochemistry (2001) [Pubmed]
  10. Formation and isolation of a covalent intermediate during the glutaminase reaction of a class II amidotransferase. Schnizer, H.G., Boehlein, S.K., Stewart, J.D., Richards, N.G., Schuster, S.M. Biochemistry (1999) [Pubmed]
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