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
- 발행연도
- 2012.1
- 수록면
- 452 - 457 (6page)
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Diketoreductase (DKR) from Acinetobacter baylyi contains two tryptophan residues at positions 149 and 222. Trp-149 and Trp-222 are located along the entry path of substrate into active site and at the dimer interface of DKR, respectively. Single and double substitutions of these positions were generated to probe the roles of tryptophan residues. After replacing Trp with Ala and Phe, biochemical and biophysical characteristics of the mutants were thoroughly investigated. Enzyme activity and substrate binding affinity of W149A and W149F were remarkably decreased, suggesting that Trp-149 regulates the position of substrate at the binding site. Meanwhile, enzyme activity of W222F was increased by 1.7-fold while W222A was completely inactive. In addition to lower thermostability of Trp-222 mutants, molecular modeling of the mutants revealed that Trp-222 is vital to protein folding and dimerization of the enzyme. [BMB Reports 2012; 45(8): 452-457]
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참고문헌 (22)
참고문헌 신청
Allocati, N. / 2005 / Contribution of the two conserved tryptophan residues to the catalytic and structural properties of Proteus mirabilis glutathione S-transferase B1-1 /
Balchin, D. / 2010 / Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1 / Biochim. Biophy
Bourbon-Freie, A. / 2009 / Trp-107 and trp-253 account for the increasedsteady state fluorescence that accompanies the conformationalchange in human pancreatic triglyceride
Burley, S. K. / 1985 / Aromatic-aromatic interaction: a mechanism of protein structure stabilization / Science 229 : 23 ~ 28
Hong, H. / 2007 / Role of aromatic side chains in the folding and thermodynamic stability of integral
Balchin, D. / 2010 / Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1 / Biochim. Biophy
Bourbon-Freie, A. / 2009 / Trp-107 and trp-253 account for the increasedsteady state fluorescence that accompanies the conformationalchange in human pancreatic triglyceride
Burley, S. K. / 1985 / Aromatic-aromatic interaction: a mechanism of protein structure stabilization / Science 229 : 23 ~ 28
Hong, H. / 2007 / Role of aromatic side chains in the folding and thermodynamic stability of integral
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