Spontaneous Chemical Reversion of an Active Site Mutation: Deamidation of an Asparagine Residue Replacing the Catalytic Aspartic Acid of Glutamate Dehydrogenase-Reference-Cited by-同舟云学术

Spontaneous Chemical Reversion of an Active Site Mutation: Deamidation of an Asparagine Residue Replacing the Catalytic Aspartic Acid of Glutamate Dehydrogenase

Published:2005-02-10 Issue:9 Volume:44 Page:3636-3643
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Paradisi Francesca¹,Dean Jonathan L. E.¹,Geoghegan Kieran F.¹,Engel Paul C.¹

Affiliation:

1. Department of Biochemistry, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland, Kennedy Institute of Rheumatology Division, Faculty of Medicine, Imperial College, London W6 8LH, England, and Pfizer Global Research and Development, Groton, Connecticut 06340

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi047679u

Reference26 articles.

1. The Effect of Pyridoxal Phosphate Modification on the Catalytic and Regulatory Properties of Bovine Liver Glutamate Dehydrogenase

2. Inactivation of Bovine Glutamate Dehydrogenase by Carbamyl Phosphate and Cyanate

3. A peptide containing a reactive lysyl group from ox liver glutamate dehydrogenase

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