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Literature summary for 6.3.5.4 extracted from

  • Boehlein, S.K.; Rosa-Rodriguez, J.G.; Schuster, S.M.; Richards, N.G.J.
    Catalytic activity of the N-terminal domain of Escherichia coli asparagine synthetase B can be reengineered by single-point mutation (1997), J. Am. Chem. Soc., 119, 5785-5791.
No PubMed abstract available
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Protein Variants

Protein Variants Comment Organism
N74D replacement of the catalytically important residue Asn-74 by Asp, N74D, in the N-terminal domain of Escherichia coli Asn synthetase B confers nitrile hydratase activity upon the mutant enzyme. While wild-type As-B can efficiently catalyze the hydrolysis of Gln to Glu, the N74D As-B mutant exhibits very low glutaminase activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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 wild-type enzyme and mutant N74S
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Escherichia coli
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 Asn synthetase B
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Asp + L-Gln
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 Escherichia coli AMP + diphosphate + Asn + Glu
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 ?
additional information the N74D As-B mutant exhibits very low glutaminase activity Escherichia coli ?
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 ?