Earticle

초록

영어

Human cystathionine gamma-lyase (hCGL) is a PLP dependent
enzyme that catalyzes the cleavage reaction of L-cystathionine to Lcysteine
and 2-ketobutyrate. hCGL also uses L-cysteine as a substrate
to produce hydrogen sulfide (H2S). The hCGL/H2S system has been
shown to play an important role in regulating cellular functions in
different systems. In the present study, we found a novel reaction of
hCGL that directly converting seleno-L-methionine (SeMet) into
methylselenol, 2-ketobutyrate, and NH3. The hCGL gene was cloned
into a pET-28 vector which incorporating a TEV cleavable N-terminal His-tag fusion. hCGL was purified by a His-bind column chromatography followed by TEV protease cleavage. Authentic methylselenol was prepared by reduction of dimethyldiselenide with sodium tetrahydroborate. The gaseous product of the enzymatic reaction with SeMet was determined by making the 2, 4-dinitrophenyl derivative, subjecting it to analysis by GC/MS spectrometry. GC/MS data was identical to that of authentic 2, 4-dinitrophenyl-methylselenol. 2-ketobutyrate was also detected by the MBTH method. These results suggested that hCGL is a critical enzyme charging SeMet metabolism.

키워드

저자

• Kwang-Hwan JHEE [ Dept. of Applied Chemistry, Kumoh National Institute of Technology,Gumi, 730-701. ]
• Hyun-Nam CHO [ Dept. of Applied Chemistry, Kumoh National Institute of Technology,Gumi, 730-701. ]
• Seun-Ah YANG [ The Center for Traditional Microorganism Resources, Keimyung University, ]
• In-Seon LEE [ The Center for Traditional Microorganism Resources, Keimyung University, ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576