Structure of the complex of adenylate kinase from Escherichia coli with the inhibitor P1,P5-di(adenosine-5′-)pentaphosphate
✍ Scribed by Müller, Christoph W.; Schulz, Georg E.
- Book ID
- 122901908
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 428 KB
- Volume
- 202
- Category
- Article
- ISSN
- 0022-2836
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📜 SIMILAR VOLUMES
A biochemical assay for the measurement of ATP synthesis coupled to electron transport in the presence of adenylate kinase was developed as an alternative to using the conventional Clark-type oxygen electrode. The assay utilizes Pi,p-di-(adenosine-5')-pentaphosphate which is shown to he a competitiv
P1,P5-di(adenosine 5')pentaphosphate (Ap5A) is an excellent inhibitor of human hemolysate adenylate kinase at concentrations near 2 microM and above. At ten times this concentration and in hemolysate enzyme assays under conditions described in this paper it appears not to alter reaction data in the