Substrate specificity and reaction mechanism of human glycoasparaginase. The N-glycosidic linkage of various glycoasparagines is cleaved through a reaction mechanism similar to L-asparaginase.-Reference-Cited by-同舟云学术

Substrate specificity and reaction mechanism of human glycoasparaginase. The N-glycosidic linkage of various glycoasparagines is cleaved through a reaction mechanism similar to L-asparaginase.

Published:1992-04 Issue:10 Volume:267 Page:6855-6858
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kaartinen V,Mononen T,Laatikainen R,Mononen I

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference20 articles.

1. Enzymatic cleavage of glycopeptides

2. Glycosaparaginase from human leukocytes. Inactivation and covalent modification with diazo-oxonorvaline.

3. Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.

4. 5 L-Asparaginase

5. Structure of peptide from active site region of Escherichia coli L-asparaginase.

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1. Depletion of L-asparagine supply and apoptosis of leukemia cells induced by human glycosylasparaginase;Leukemia;2009-01-22

2. Gliap − a novel untypical l-asparaginase localized to rat brain astrocytes;Journal of Neurochemistry;2003-05-01

3. β-Aspartylpeptides as substrates ofL-asparaginases fromEscherichia coliandErwinia chrysanthemi;FEBS Letters;2002-08-28

4. Glycosylasparaginase Activity Requires the α-Carboxyl Group, but Not the α-Amino Group, on N4-(2-Acetamido- 2-deoxy-β--glucopyranosyl)--asparagine;Archives of Biochemistry and Biophysics;2001-07

5. Glycosylasparaginase Inhibition Studies: Competitive Inhibitors, Transition State Mimics, Noncompetitive Inhibitors;Journal of Enzyme Inhibition;2001-01