Reaction stereochemistry of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine

Eriko Nango; Fumitaka Kudo; Tadashi Eguchi; Katsumi Kakinuma

doi:10.1246/cl.2003.438

Reaction stereochemistry of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine

Eriko Nango, Fumitaka Kudo, Tadashi Eguchi, Katsumi Kakinuma

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

The reaction stereochemistry of 2-deoxy-scyllo-inosose (DOI) synthase (DOIS) derived from butirosin-producing Bacillus circulans, the key starter enzyme of 2-deoxystreptamine biosynthesis, was closely analyzed by use of the purified recombinant DOIS. The stereochemical pathway of the DOIS reaction is common in the aminoglycoside-producing Bacillus and Streptomyces, but is distinct from a related dehydroquinate synthase reaction in the shikimate pathway. Evolutionary relationship between these enzymes is also discussed.

Original language	English
Pages (from-to)	438-439
Number of pages	2
Journal	Chemistry Letters
Volume	32
Issue number	5
DOIs	https://doi.org/10.1246/cl.2003.438
Publication status	Published - 2003 May 5
Externally published	Yes

ASJC Scopus subject areas

Chemistry(all)

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abstract = "The reaction stereochemistry of 2-deoxy-scyllo-inosose (DOI) synthase (DOIS) derived from butirosin-producing Bacillus circulans, the key starter enzyme of 2-deoxystreptamine biosynthesis, was closely analyzed by use of the purified recombinant DOIS. The stereochemical pathway of the DOIS reaction is common in the aminoglycoside-producing Bacillus and Streptomyces, but is distinct from a related dehydroquinate synthase reaction in the shikimate pathway. Evolutionary relationship between these enzymes is also discussed.",

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AU - Nango, Eriko

AU - Kudo, Fumitaka

AU - Eguchi, Tadashi

AU - Kakinuma, Katsumi

PY - 2003/5/5

Y1 - 2003/5/5

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AB - The reaction stereochemistry of 2-deoxy-scyllo-inosose (DOI) synthase (DOIS) derived from butirosin-producing Bacillus circulans, the key starter enzyme of 2-deoxystreptamine biosynthesis, was closely analyzed by use of the purified recombinant DOIS. The stereochemical pathway of the DOIS reaction is common in the aminoglycoside-producing Bacillus and Streptomyces, but is distinct from a related dehydroquinate synthase reaction in the shikimate pathway. Evolutionary relationship between these enzymes is also discussed.

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Reaction stereochemistry of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine

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