Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization

• Published in: The Journal of biological chemistry Vol. 259; no. 4; pp. 2113 - 2123
• Main Authors: Renosto, F, Seubert, P A, Segel, I H
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.02.1984; American Society for Biochemistry and Molecular Biology
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; fungi; Kinetics; Macromolecular Substances; Mathematics; Molecular Weight; Penicillium - enzymology; Penicillium chrysogenum - enzymology; Phosphotransferases (Alcohol Group Acceptor); Phosphotransferases - isolation & purification; Phosphotransferases - metabolism; Transferases; Fungi; Adenylylsulfate kinase; Purification; Enzyme; Kinetics; Fungi Imperfecti; Thallophyta; Penicillium chrysogenum

Adenosine 5'-phosphosulfate (APS) kinase, the second enzyme in the pathway of inorganic sulfate assimilation, was purified to near homogeneity from mycelium of the filamentous fungus, Penicillium chrysogenum. The enzyme has a native molecular weight of 59,000-60,000 and is composed of two 30,00...