Biosynthesis of 2-Deoxystreptamine by Three Crucial Enzymes in Streptomyces fradiae NBRC 12773 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2005-12

AUTHORS

Fumitaka Kudo, Yasuhito Yamamoto, Kenichi Yokoyama, Tadashi Eguchi, Katsumi Kakinuma

ABSTRACT

NeoA, B, and C encoded in the neomycin biosynthetic gene cluster have been enzymatically confirmed to be responsible to the formation of 2-deoxystreptamine (DOS) in Streptomyces fradiae. NeoC was functionally characterized as 2-deoxy-scyllo-inosose synthase, which catalyzes the carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose. Further, NeoA appeared to catalyze the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD(P)+ forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI). Consequently, NeoA was characterized as 2-deoxy-scyllo-inosamine dehydrogenase. Finally, amino-DOI produced by NeoA from DOIA was transformed into DOS by NeoB. Since NeoB (Neo6) was also reported to be L-glutamine:2-deoxy-scyllo-inosose aminotransferase, all the enzymes in the DOS biosynthesis were characterized for the first time. More... »

PAGES

ja2005104

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ja.2005.104

DOI

http://dx.doi.org/10.1038/ja.2005.104

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1009439571

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16506694


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