- Abstract:
-
A mutant (D165N) of clostridial glutamate dehydrogenase (GDH) in which the catalytic Asp is replaced by Asn surprisingly showed a residual 2% of wild-type activity when purified after expression in Escherichia coli at 37 degrees C. This low-level activity also displayed Michaelis constants for substrates that were remarkably similar to those of the wild-type enzyme. Expression at 8 degrees C gave a mutant enzyme preparation 1000 times less active than the first preparation, but progressively,...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/bi047679u
-
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- Journal:
- Biochemistry
- Volume:
- 44
- Issue:
- 9
- Pages:
- 3636-3643
- Publication date:
- 2005-03-05
- DOI:
- EISSN:
-
1520-4995
- ISSN:
-
0006-2960
- URN:
-
uuid:db5b74b0-d426-4356-ac2d-3a4e11db5879
- Source identifiers:
-
224179
- Local pid:
- pubs:224179
- Copyright date:
- 2005
Journal article
Spontaneous chemical reversion of an active site mutation: deamidation of an asparagine residue replacing the catalytic aspartic acid of glutamate dehydrogenase.
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