Literature DB >> 9257709

Recombinant human glycosylasparaginase catalyzes hydrolysis of L-asparagine.

T Noronkoski1, I B Stoineva, D D Petkov, I Mononen.   

Abstract

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.

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Year:  1997        PMID: 9257709     DOI: 10.1016/s0014-5793(97)00761-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Isoaspartyl dipeptidase activity of plant-type asparaginases.

Authors:  Mahdi Hejazi; Kirill Piotukh; Jens Mattow; Rainer Deutzmann; Rudolf Volkmer-Engert; Wolfgang Lockau
Journal:  Biochem J       Date:  2002-05-15       Impact factor: 3.857

2.  Crystal structure of a mutant glycosylasparaginase shedding light on aspartylglycosaminuria-causing mechanism as well as on hydrolysis of non-chitobiose substrate.

Authors:  Suchita Pande; Damodharan Lakshminarasimhan; Hwai-Chen Guo
Journal:  Mol Genet Metab       Date:  2017-04-19       Impact factor: 4.797

Review 3.  Aspartylglycosaminuria: a review.

Authors:  Maria Arvio; Ilkka Mononen
Journal:  Orphanet J Rare Dis       Date:  2016-12-01       Impact factor: 4.123

4.  Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma.

Authors:  Quentin Coulette; Séverine Lemauf; Dominique Colinet; Geneviève Prévost; Caroline Anselme; Marylène Poirié; Jean-Luc Gatti
Journal:  PLoS One       Date:  2017-07-24       Impact factor: 3.240

  4 in total

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