In:
FEBS Letters, Wiley, Vol. 459, No. 3 ( 1999-10-15), p. 319-322
Abstract:
Here we show that in extrahepatic methionine adenosyltransferase replacement of a single amino acid (glycine 120) by cysteine is sufficient to create a functional nitric oxide binding site without affecting the kinetic properties of the enzyme. When wild‐type and mutant methionine adenosyltransferase were incubated with S ‐nitrosoglutathione the activity of the wild‐type remained unchanged whereas the activity of the mutant enzyme decreased markedly. The mutant enzyme was found to be S ‐nitrosylated upon incubation with the nitric oxide donor. Treatment of the S ‐nitrosylated mutant enzyme with glutathione removed most of the S ‐nitrosothiol groups and restored the activity to control values. In conclusion, our results suggest that functional S ‐nitrosylation sites can develop from existing structures without drastic or large‐scale amino acid replacements.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(99)01267-3
Language:
English
Publisher:
Wiley
Publication Date:
1999
detail.hit.zdb_id:
1460391-3
SSG:
12
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