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Glycobiology Advance Access originally published online on October 19, 2006
Glycobiology 2007 17(2):119-126; doi:10.1093/glycob/cwl060
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© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Biosynthesis of dTDP-6-deoxy-ß-D-allose, biochemical characterization of dTDP-4-keto-6-deoxyglucose reductase (GerKI) from Streptomyces sp. KCTC 0041BP

Ta Thi Thu Thuy2, Kwangkyoung Liou2, Tae-jin Oh2, Dea Hee Kim3, Doo Hyun Nam4, Jin Cheol Yoo5 and Jae Kyung Sohng1,2

2 Department of Pharmaceutical Engineering, Institute of Biomolecule Reconstruction (iBR), SunMoon University, 100, Kalsan-ri, Tangjeong-myeon, Asansi, Chungnam 336-708, South Korea
3 GeneChem Inc., 59-1, Jang-Dong, Yusong-Gu, Daejon 305-390, South Korea
4 Department of Pharmacy, Yeungnam University, Kyongsan, Kyungbuk 712-749, South Korea
5 Department of Pharmacy, Chosun University, Kwangju 501-759, South Korea

1 To whom correspondence should be addressed; Tel: +82 41-530-2246; Fax: +82 41-544-2919; e-mail: sohng{at}sunmoon.ac.kr

Received on March 14, 2006; revised on September 28, 2006; accepted on October 10, 2006

dTDP-6-deoxy-D-allose, an unusual deoxysugar, has been identified as an intermediate in the mycinose biosynthetic pathway of several macrolide antibiotics. In order to characterize the biosynthesis of this deoxysugar, we have cloned and heterologously overexpressed gerK1 in Escherichia coli BL21 (DE3) cells. This gene encodes for a protein with the putative function of a dTDP-4-keto-6-deoxyglucose reductase, which appears to be involved in the dihydrochalcomycin (GERI-155) biosynthesis evidenced by Streptomyces sp KCTC 0041BP. Our results revealed that GerK1 exhibited a specific reductive effect on the 4-keto carbon of dTDP-4-keto-6-deoxy-D-allose, with the hydroxyl group in an axial configuration at the C3 position only. The enzyme catalyzed the conversion of dTDP-4-keto-6-deoxyglucose to dTDP-6-deoxy-ß-D-allose, according to the results of an in vitro coupled enzyme assay, in the presence of GerF (dTDP-4-keto-6-deoxyglucose 3-epimerase). The product was isolated, and its stereochemistry was determined via nuclear magnetic resonance analysis.

Key words: deoxysugar biosynthesis / dTDP-6-deoxy-D-allose / dTDP-4-keto-6-deoxyglucose reductase / Streptomyces

None declared.


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