Earticle

초록

영어

Uncharacterized genes from the mesophilic bacterium Clostridium difficile and hyperthermophilic bacterium Thermotoga maritima that were previously proposed to be ribose-5-phosphate isomerases (RpiBs) were cloned and expressed in Escherichia coli. The RpiBs were
compared to RpiB from the thermophilic bacterium C. thermocellum. The maximal activity of l-talose isomerization was observed at pH 7.5 and 40 °C in C. difficile RpiB, at pH 7.5 and 65 °C in C. thermocellum RpiB, and at pH 8.0 and 70 °C in T. maritima RpiB. C. difficile RpiB exhibited activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as d-ribose, d-allose, l-talose, llyxose, d-gulose, and l-mannose. In contrast, C. thermocellum and T. maritima RpiBs displayed activity only with aldose substrates possessing hydroxyl groups configured the same direction at the C2, C3, and C4 positions, such as the d- and l-forms of ribose, talose, and
allose.

키워드

저자

• Soo-Jin YEOM [ Department of Bioscience and Biotechnology, Konkuk University ]
• Chang-Su PARK [ Department of Bioscience and Biotechnology, Konkuk University ]
• Deok-Kun OH [ Department of Bioscience and Biotechnology, Konkuk University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576