A New Arylsulfate Sulfotransferase Involved in Liponucleoside Antibiotic Biosynthesis in Streptomycetes

• Published in: The Journal of biological chemistry Vol. 285; no. 17; pp. 12684 - 12694
• Main Authors: Kaysser, Leonard, Eitel, Kornelia, Tanino, Tetsuya, Siebenberg, Stefanie, Matsuda, Akira, Ichikawa, Satoshi, Gust, Bertolt
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 23.04.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Anti-Bacterial Agents - biosynthesis; Anti-Bacterial Agents - chemistry; Antibiotics; Arylsulfotransferase - biosynthesis; Arylsulfotransferase - chemistry; Arylsulfotransferase - genetics; Arylsulfotransferase - isolation & purification; Caprazamycins; Catalysis; Cloning, Molecular; Enzyme Inhibitors; Enzyme Mechanisms; Enzymology; Liposidomycins; Microbiology; Nucleosides - biosynthesis; Nucleosides - chemistry; Recombinant Proteins - biosynthesis; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification; Sequence Homology, Amino Acid; Site-directed Mutagenesis; Streptomyces; Streptomyces coelicolor - enzymology; Streptomyces coelicolor - genetics; Streptomycetes; Substrate Specificity; Sulfotransferase; Enzyme Mechanisms; Site-directed Mutagenesis; Caprazamycins; Enzyme Inhibitors; Liposidomycins; Antibiotics; Streptomycetes; Sulfotransferase

Sulfotransferases are involved in a variety of physiological processes and typically use 3′-phosphoadenosine 5′-phosphosulfate (PAPS) as the sulfate donor substrate. In contrast, microbial arylsulfate sulfotransferases (ASSTs) are PAPS-independent and utilize arylsulfates as sulfate donors. Yet, the...