The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM.

Fröhlich, K U; Fries, H W; Peters, J M; Mecke, D

Fröhlich, K U; Fries, H W; Peters, J M; Mecke, D.

Affiliation

Fröhlich KU; Physiologisch-chemisches Institut, Tübingen, Germany.

Biochim Biophys Acta ; 1253(1): 25-32, 1995 Nov 15.

Article in En | MEDLINE | ID: mdl-7492595

Subject(s)

Adenosine Triphosphatases/metabolism; Cell Cycle Proteins/metabolism; Fungal Proteins/metabolism; Saccharomyces cerevisiae/enzymology; Adenosine Diphosphate/pharmacology; Adenosine Triphosphatases/antagonists & inhibitors; Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/ultrastructure; Adenosine Triphosphate/pharmacology; Allosteric Regulation; Cell Cycle Proteins/antagonists & inhibitors; Cell Cycle Proteins/chemistry; Cell Cycle Proteins/ultrastructure; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors/pharmacology; Ethylmaleimide/pharmacology; Fungal Proteins/chemistry; Fungal Proteins/ultrastructure; Kinetics; Microscopy, Electron; NAD/pharmacology; Saccharomyces cerevisiae Proteins; Valosin Containing Protein

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Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae / Fungal Proteins / Adenosine Triphosphatases / Cell Cycle Proteins Language: En Journal: Biochim Biophys Acta Year: 1995 Document type: Article Affiliation country: Germany Country of publication: Netherlands

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