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 K m is 3–4-fold higher and V...
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Published in | FEBS letters Vol. 412; no. 1; pp. 149 - 152 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier B.V
21.07.1997
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(97)00761-8 |