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Recombinant human glycosylasparaginase catalyzes hydrolysis of l ‐asparagine
Author(s) -
Noronkoski Tiina,
Stoineva Ivanka B.,
Petkov Dimiter D.,
Mon Ilkka
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00761-8
Subject(s) - asparagine , hydrolysis , amidase , aspartic acid , chemistry , amino acid , biochemistry , recombinant dna , acid hydrolysis , gene
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 K m is 3–4‐fold higher and V max 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.