Stretching exercises - flexibility in dihydrofolate reductase catalysis
被引:93
作者:
Miller, GP
论文数: 0引用数: 0
h-index: 0
机构:
Penn State Univ, Dept Chem, University Pk, PA 16802 USAPenn State Univ, Dept Chem, University Pk, PA 16802 USA
Miller, GP
[1
]
Benkovic, SJ
论文数: 0引用数: 0
h-index: 0
机构:
Penn State Univ, Dept Chem, University Pk, PA 16802 USAPenn State Univ, Dept Chem, University Pk, PA 16802 USA
Benkovic, SJ
[1
]
机构:
[1] Penn State Univ, Dept Chem, University Pk, PA 16802 USA
来源:
CHEMISTRY & BIOLOGY
|
1998年
/
5卷
/
05期
关键词:
D O I:
10.1016/S1074-5521(98)90616-0
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
As an enzyme, dihydrofolate reductase performs two tasks: transformation of its substrate dihydrofolate or folate to tetrahydrofolate, using NADPH as a cofactor, and regeneration of the enzyme for a subsequent round of catalysis. Studies discussed in this review highlight the role of conformational flexibility in both of these enzymatic functions.