Stopped-flow studies of human aldose reductase reveal which enzyme form predominates during steady-state turnover in either reaction direction.
Stopped-flow studies of human aldose reductase reveal which enzyme form predominates during steady-state turnover in either reaction direction.
复制标题
人醛糖还原酶的停流研究揭示了在任一反应方向的稳态周转期间哪种酶形式占主导地位。
DOI：
10.1007/978-1-4615-1965-2_29
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发表时间：
1995
影响因子：
--
通讯作者：
Lai,CJ
中科院分区：
文献类型：
--
作者：
Grimshaw,CE;Lai,CJ
自从法国研究小组（Rondeau等人，1992）和贝勒研究小组（Wilson等人，1992），以及华盛顿大学医学院BioCryst制药公司（Borhani等人，1992）和Quiocho博士实验室（Wilson等人，1993）对醛糖还原酶（ALR2）的三维结构进行了研究以来，醛糖还原酶领域的进展相当迅速。最近，贝勒、布兰代斯和惠蒂尔研究所的研究人员共同努力，确定了氨基酸残基的活性位点群及其在催化机制中的可能作用（Harrison等人，1994；Bohren等人，1994）。
Progress in the aldo-keto reductase field has been quite rapid since the solution of the 3-dimensional structure of aldose reductase (ALR2) by the French group (Rondeau et al., 1992) and the Baylor group (Wilson et al., 1992), with additional contributions from Washington University School of Medicine with BioCryst Pharmaceuticals (Borhani et al., 1992) and with Dr. Quiocho’s laboratory (Wilson et al., 1993). Most recently, a definitive assignment of the active site constellation of amino acid residues and their likely roles in the catalytic mechanism was established by the collaborative efforts of researchers at Baylor, Brandeis and The Whittier Institute (Harrison et al., 1994; Bohren et al., 1994).