Functional consequence of substitutions at residue 171 in human galactose-1-phosphate uridylyltransferase
Functional consequence of substitutions at residue 171 in human galactose-1-phosphate uridylyltransferase
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DOI：
10.1074/jbc.m001053200
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发表时间：
2000-07-28
影响因子：
4.8
通讯作者：
Fridovich-Keil, JL
中科院分区：
文献类型：
--
作者：
Crews, C;Wilkinson, KD;Fridovich-Keil, JL
Impairment of the human enzyme galactose-l-phosphate uridylyltransferase (hGALT) results in the potentially lethal disorder classic galactosemia. Although a variety of naturally occurring mutations have been identified in patient alleles, few have been well characterized. We have explored the functional significance of a common patient mutation, F171S, using a strategy of conservative substitution at the defined residue followed by expression of the wild-type and, alternatively, substituted proteins in a null-background strain of yeast, As expected from patient studies, the F171S-hGALT protein demonstrated
