Structural and functional role of his 67 residue in subtilisin E = 서브틸리신 E 에서 His 67 잔기의 구조및 기능적 역할

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His 67 residue is highly conserved among subtilisin family and changed to Arg in mammalian subtilisin-like proteins. To elucdate the structural and functional role of His 67 residue in subtilisin E, site-directed mutagenesis was carried out. Three mutants of subtilisin E with Ala 67, Glu 67 and Gly 67 were obtained. Each mutant was characterized in terms of proteolytic activity. Compared with wild type, proteolytic activity for Ala 67 mutant was about 30\%. Glu 67 and Gly 67 mutant did not show any detectable proteolytic activity on Nsuccinyl- L- Ala- L- Ala- L- Pro- L- Phe- p- nitroanilide but developed hallow zones onto the skim-milk plate. It is expected that His 67 residue in subtilisin E influences on catalytic efficiency.
Advisors
Byun, Si-Myung변시명
Description
한국과학기술원 : 생물공학과,
Publisher
한국과학기술원
Issue Date
1992
Identifier
60366/325007 / 000901376
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물공학과, 1992.2, [ vii, 42 p. ]

Keywords

부위 특이 돌연변이

URI
http://hdl.handle.net/10203/27750
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=60366&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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