Stereochemistry of the reaction of the inhibitor β-chloroalanine with mercaptoethanol, a β-substitution reaction catalysed by an aminotransferase
Stereochemistry of the reaction of the inhibitor β-chloroalanine with mercaptoethanol, a β-substitution reaction catalysed by an aminotransferase
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抑制剂β-氯丙氨酸与巯基乙醇反应的立体化学，这是转氨酶催化的β-取代反应
DOI：
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发表时间：
2000
期刊：
影响因子：
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通讯作者：
D. W. Young
中科院分区：
文献类型：
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作者：
B. Adams;K. Beresford;S. Whyte;D. W. Young
L-天冬氨酸氨基转移酶是PLP介导的酶的α-家族的成员，通常催化转氨作用，已用于催化酶抑制剂β-氯-L-丙氨酸的立体特异性标记样品与2-巯基乙醇的β-取代反应;产物的立体化学通过独立的合成来指定，表明异常取代反应在立体化学的总体保留下进行，由PLP介导的酶的β-家族的酶催化的反应的通常立体化学结果，所述酶与α-家族的酶具有低同源性
L-Aspartate aminotransferase, a member of the α-family of PLP mediated enzymes, which normally catalyses transamination, has been used to catalyse the β-substitution reaction of stereospecifically labelled samples of the enzyme inhibitor β-chloro-L-alanine with 2-mercaptoethanol; the stereochemistry of the products was assigned by independent synthesis, showing that the abnormal substitution reaction proceeds with overall retention of stereochemistry, the usual stereochemical consequence of reactions catalysed by enzymes of the β-family of PLP mediated enzymes which have low homology with enzymes of the α-family
影响因子：
2.9
作者：
Schneider, TR;Gerhardt, E;Schlichting, I
通讯作者：
Schlichting, I