지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제29권 제9호
- 발행연도
- 2019.1
- 수록면
- 1,375 - 1,382 (8page)
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초록· 키워드
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Phenylalanine hydroxylase from Chromobacterium violaceum (CvPAH) is a monomeric enzyme that converts phenylalanine to tyrosine. It shares high amino acid identity and similar structure with a subunit of human phenylalanine hydroxylase that is a tetramer, resulting in the latent application in medications. In this study, semirational design was applied to CvPAH to improve the catalytic ability based on molecular dynamics simulation analyses. Four Nterminal truncated variants and one single point variant were constructed and characterized. The D267P variant showed a 2.1-fold increased thermal stability compared to the wild type, but lower specific activity was noted compared with the wild type. The specific activity of all truncated variants was a greater than 25% increase compared to the wild type, and these variants showed similar or slightly decreased thermostability with the exception of the N-Δ9 variant. Notably, the N-Δ9 variant exhibited a 1.2-fold increased specific activity, a 1.3-fold increased thermostability and considerably increased catalytic activity under the neutral environment compared with the wild type. These properties of the N-Δ9 variant could advance medical and pharmaceutical applications of CvPAH. Our findings indicate that the N-terminus might modulate substrate binding, and are directives for further modification and functional research of PAH and other enzymes.
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참고문헌 (21)
참고문헌 신청
Muntau AC / 2002 / Tetrahydrobiopterin as an alternative treatment for mild phenylketonuria / N. Engl. J. Med 347:2122~2132
Zhu T / 2017 / The predictive value of genetic analyses in the diagnosis of tetrahydrobiopterin (BH4)-responsiveness in Chinese phenylalanine hydroxylase deficiency patients / Sci. Rep 7:6762
Nakata H / 1979 / Phenylalanine hydroxylase from Chromobacterium violaceum, purification and characterization / J. Biol. Chem 254:1829~1833
Onishi A / 1991 / Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases / J. Biol. Chem 266:18454~18459
Erlandsen H / 2002 / Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases : similar fold, different stability and reaction rates / J. Mol. Biol 320:645~661
Zhu T / 2017 / The predictive value of genetic analyses in the diagnosis of tetrahydrobiopterin (BH4)-responsiveness in Chinese phenylalanine hydroxylase deficiency patients / Sci. Rep 7:6762
Nakata H / 1979 / Phenylalanine hydroxylase from Chromobacterium violaceum, purification and characterization / J. Biol. Chem 254:1829~1833
Onishi A / 1991 / Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases / J. Biol. Chem 266:18454~18459
Erlandsen H / 2002 / Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases : similar fold, different stability and reaction rates / J. Mol. Biol 320:645~661
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