Journal article icon

Journal article

Spontaneous chemical reversion of an active site mutation: deamidation of an asparagine residue replacing the catalytic aspartic acid of glutamate dehydrogenase.

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

Actions


Access Document


Publisher copy:
10.1021/bi047679u

Authors


Paradisi, F More by this author
Geoghegan, KF More by this author
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

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP