Characterization of prolyl oligopeptidase from hyperthermophilic archaeon Thermococcus sp NA1
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Title
- Characterization of prolyl oligopeptidase from hyperthermophilic archaeon Thermococcus sp NA1
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Author(s)
- Lee, Hyun Sook; Kim, Yun Jae; Cho, Yona; Kim, Sang-Jin; Lee, Jung-Hyun; Kang, Sung Gyun
- KIOST Author(s)
- Lee, Hyun Sook(이현숙); Kim, Yun Jae(김윤재); Lee, Jung Hyun(이정현); Kang, Sung Gyun(강성균)
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Alternative Author(s)
- 이현숙; 김윤재; 조요나; 김상진; 이정현; 강성균
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Publication Year
- 2007-03
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Abstract
- The prolyl oligopeptidase TNA1_POP was found to be encoded in the genome of the hyperthermophilic archaeon Thermococcus sp. NA1 and showed high similarities to its archaeal homologs (76-83%). The enzyme was found to be a single polypeptide composed of 616 amino acids with conserved signature domains. A recombinant TNA1_POP expressed in Escherichia coli was capable of hydrolyzing succinyl-Ala-Pro-p-nitroanilide (Sue-Ala-Pro-pNA) with temperature and pH optimums of 80 degrees C and 7, respectively. TNA1_POP activity appeared to be significantly activated by pre-incubation at 80 degrees C and 90 degrees C with the optimum temperature unchanged. The heat-activated enzyme exhibited a k(cat), approximately twofold higher than that of the unheated enzyme, however, both enzymes showed the same K-m TNA1_POP was thermostable at 80 degrees C retaining 80% of its heat-activated activity even after 23 h, but it lost its enzymatic activity at 90 degrees C with a half-life of 3 h. The loss of the enzymatic activity at 90 degrees C seemed to be caused by the autodegradation of the enzyme, not by thermal denaturation, as supported by circular dichroism spectropolarimetry. Autodegradation fragments ranging from 2 to 18 kDa were mapped by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry.
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ISSN
- 1389-1723
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/4727
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DOI
- 10.1263/jbb.103.221
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Bibliographic Citation
- JOURNAL OF BIOSCIENCE AND BIOENGINEERING, v.103, no.3, pp.221 - 228, 2007
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Publisher
- SOC BIOSCIENCE BIOENGINEERING JAPAN
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Subject
- PYROCOCCUS-FURIOSUS; ACTIVE-SITE; CLEAVING ENZYME; ENDOPEPTIDASE; PEPTIDASES; CLONING; CELLS; SEQUENCE; SPECIFICITY; EXPRESSION
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Keywords
- prolyl oligopeptidase; hyperthermophile; archaea; Thermococcus; autodegradation
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Type
- Article
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Language
- English
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Document Type
- Article
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