Journal article icon

Journal article

Chemical rescue of the catalytically disabled clostridial glutamate dehydrogenase mutant D165S by fluoride ion.

Abstract:

The catalytically disabled Asp165-->Ser mutant of clostridial glutamate dehydrogenase shows 100000-fold less activity than the wild-type (WT) enzyme in a standard glutamate oxidation assay and 1000-fold less activity in the reductive-amination reaction. The large reduction in the rate has been attributed to removal of the negative charge and the postulated proton-donor capacity of the aspartate carboxyl group. However, fluoride ion (1 M NaF) causes a 1000-fold activation of the mutant enzy...

Expand abstract

Actions


Access Document


Publisher copy:
10.1042/0264-6021:3400555

Authors


Hayden, BM More by this author
Martin, SR More by this author
Journal:
The Biochemical journal
Volume:
340 ( Pt 2)
Issue:
2
Pages:
555-560
Publication date:
1999-06-05
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:faf290b9-8be4-48b1-9cfe-3fdb41d07676
Source identifiers:
430182
Local pid:
pubs:430182

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