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Mutation of Cysteine-115 to Alanine in Nicotiana glutinosa Ornithine Decarboxylase Reduces Enzyme Activity
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  • Mutation of Cysteine-115 to Alanine in Nicotiana glutinosa Ornithine Decarboxylase Reduces Enzyme Activity
  • Mutation of Cysteine-115 to Alanine in Nicotiana glutinosa Ornithine Decarboxylase Reduces Enzyme Activity
저자명
Lee. Yong-Sun,Cho. Young-Dong
간행물명
Journal of biochemistry and molecular biology
권/호정보
2001년|34권 5호|pp.472-477 (6 pages)
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생화학분자생물학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

Ornithine decarboxylase (ODC, EC 4.1.1.17) is the first and key enzyme in eukaryotic polyamine biosynthesis. The cDNA encoding ornithine decarboxylase from Nicotiana glutinosa was cloned ($GeBank^{TM}$ AF 323910) and expressed in E. coli. Site directed mutagenesis were performed on several highly conserved cysteine residues. Among the mutants, C115A showed significant changes in the kinetic properties. The $K_m$ value of the C115A mutant was $1790;{mu}M$, which was 3-fold higher than that of the wild-type ODC. There was a dramatic decrease in the $k_{cat}$, values of the C115A mutant, compared to that of the wild-type ODC, which had a $k_{cat}$ value of $77.75;s^{-1}$. C115A caused a shift in the optimal pH from 8.0 to 8.4. Considering these results, we suggest that cys-115 is involved in the catalytic activity of N. glutinosa ODC.