The entire biosynthetic gene cluster for Tautomycetin (TMC), a potent T-cell immunosuppressive compound that are superior to cyclosporine A both in vitro and in vivo. TMC produced by soil microorganism Streptomyces sp. CK4412 has earlier been investigated, cloned and sequenced[1]. TMC has a unique structure, containing an ester bond linkage between a terminal cyclic anhydride moiety and a linear polyketide chain bearing an unusual terminal alkene. Here we propose two putative genes which participate a pathway to synthesize both dialkylmaleic anhydride moiety and terminal alkene as dehydratase enzyme. Within the TMC biosynthetic gene cluster, we found two putative dehydratase enzyme tmcM and tmcQ. A 1.5Kb gene tmcM and 1.4kb gene tmcQ both are located downstream of the PKS tmcB gene. In silico database comparisons revealed that TmcM function as L-carnitine dehydratase and another putative dehydratase enzyme TmcQ is a member of the MmgE/PrpD protein family. New TMC analogues characterized from inactivation of two genes, tmcM and tmcQ in Streptomyces sp. CK4412, resulting from this it constructed mutant strains △tmcM and △tmcQ respectively. The importance of the function by TmcM and TmcQ will be further studied.
키워드
StreptomycesTautomycetinDehydratase
저자
Hye-Mi YOON [ Department of Biological Engineering, Inha University, Incheon 402-751, Korea. ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다
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