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Disulfide-bond formation in the H+-pyrophosphatase of Streptomyces coelicolor and its implications for redox control and enzyme structure
- Source :
-
FEBS Letters . Jul2005, Vol. 579 Issue 17, p3625-3631. 7p. - Publication Year :
- 2005
-
Abstract
- Abstract: Redox control of disulfide-bond formation in the H+-pyrophosphatase of Streptomyces coelicolor was investigated using cysteine mutants expressed in Escherichia coli. The wild-type enzyme, but not a cysteine-less mutant, was reversibly inactivated by oxidation. To determine the residues involved in oxidative inactivation, different cysteine residues were replaced. Analysis with a cysteine-modifying reagent revealed that the formation of a disulfide bond between cysteines 253 and 621 was responsible for enzyme inactivation. This result suggests that residues in different cytoplasmic loops are close to each other in the tertiary structure. Both cysteine residues are conserved in K+-independent (type II) H+-pyrophosphatases. [Copyright &y& Elsevier]
- Subjects :
- *ADENOSINE triphosphatase
*ENZYME analysis
*ENTEROBACTERIACEAE
*ESCHERICHIA coli
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 579
- Issue :
- 17
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 18094609
- Full Text :
- https://doi.org/10.1016/j.febslet.2005.05.045