Glucose-6-phosphate dehydrogenase in cell free extracts of Zymomonas mobilis

Sly L.I. and Doelle H.W. (1968) Glucose-6-phosphate dehydrogenase in cell free extracts of Zymomonas mobilis. Archiv für Mikrobiologie, 63 3: 197-213. doi:10.1007/BF00412836


Author Sly L.I.
Doelle H.W.
Title Glucose-6-phosphate dehydrogenase in cell free extracts of Zymomonas mobilis
Journal name Archiv für Mikrobiologie   Check publisher's open access policy
ISSN 0302-8933
Publication date 1968
Sub-type Article (original research)
DOI 10.1007/BF00412836
Volume 63
Issue 3
Start page 197
End page 213
Total pages 17
Publisher Springer-Verlag
Subject 2404 Microbiology
2700 Medicine
Abstract Glucose-6-phosphate dehydrogenase activity in cell free extracts o Zymomonas mobilis showed marked differences when compared with the corresponding enzyme of Escherichia coli. It exhibited 3 times higher activity and the reaction rate over 10 min gave linearity only up to a cell free protein concentration of 0.15 mg protein. This different behaviour was not a function of environmental growth conditions of the culture nor of the nine different assay methods employed. A constant relationship existed between the specific G-6-P dehydrogenase protein and the total protein concentration in the cell free extract. The enzyme was stable for at least 5 h at 4°C in Tris-NaCl-MgCl2-buffer. An investigation of the properties of G-6-P dehydrogenase from Z. mobilis revealed a pH optimum of 8.7 with a rapid decline towards the acidic and a small decrease towards the alkaline side. The Km values were 5×10-4m for glucose-6-phosphate and 3.6×10-5m NADP+. The addition of 1×10-2m MgCl2 produced optimal activity but higher concentrations inhibited the enzyme reaction. These results were discussed with those from other sources and found to be unique for Zymomonas mobilis.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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