| Title | Escherichia coli γ-glutamylcysteine synthetase의 아미노산 치환 효과 | ||
| Author | 남용석 · 김중수 · 곽준혁 · 박영인 * · 이세영 | ||
| Address | 고려대학교 농대 농화학과 유전공학과 * | ||
| Bibliography | Korean Journal of Microbiology, 29(5),278-283, 1991 | ||
| DOI | |||
| Key Words | E. coli γ-glutamylcysteine synthetase, alanine^494, serine^495, feedback inhibition site, site-specific mutagensis | ||
| Abstract | Two amino acid residues (Ala^494 and Ser^495) of E. coli γ-glutamylcysteine synthetase have been investigated whether they are the site of feedback inhibition by site specific mutagenesis. Single substitution of serine^495 (S495F), and double substitutions of alanine^494 and serine^495 (A494G-S495F) resulted in the inactivation of the γ-glutamylcysteine synthetase activity. Substitution of alanine^494 with glycine^494 resulted in a higher level of feedback inhibition. These results suggest that serine^495 in γ-glutamylcysteine synthetase is required for its catalytic acitvity and alanine^494 is presumably related to the feeback inhibition site. | ||
| Download PDF | Kor_290503_278-283p1.pdf | ||