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Recombinant human glycosylasparaginase catalyzes hydrolysis of L-asparagine.

Glycosylasparaginase is a lysosomal amidase involved in the degradation of glycoproteins. Recombinant human glycosylasparaginase is capable of catalyzing the hydrolysis of the amino acid L-asparagine to L-aspartic acid and ammonia. For the hydrolysis of L-asparagine the Km is 3-4-fold higher and Vmax 1/5 of that for glycoasparagines suggesting that the full catalytic potential of glycosylasparaginase is not used in the hydrolysis of the free amino acid. L-Asparagine competitively inhibits the hydrolysis of aspartylglucosamine indicating that both the amino acid and glycoasparagine are interacting with the same active site of the enzyme. The hydrolytic mechanism of L-asparagine and glycoasparagines will be discussed.[1]

References

  1. Recombinant human glycosylasparaginase catalyzes hydrolysis of L-asparagine. Noronkoski, T., Stoineva, I.B., Petkov, D.D., Mononen, I. FEBS Lett. (1997) [Pubmed]
 
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