ALDOTETROSES AND C(3)-MODIFIED ALDOHEXOSES AS SUBSTRATES FOR N-ACETYLNEURAMINIC ACID ALDOLASE - A MODEL FOR THE EXPLANATION OF THE NORMAL AND THE INVERSED STEREOSELECTIVITY
ALDOTETROSES AND C(3)-MODIFIED ALDOHEXOSES AS SUBSTRATES FOR N-ACETYLNEURAMINIC ACID ALDOLASE - A MODEL FOR THE EXPLANATION OF THE NORMAL AND THE INVERSED STEREOSELECTIVITY
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DOI：
10.1021/jo00117a016
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发表时间：
1995-06-16
影响因子：
3.6
通讯作者：
WONG, CH
中科院分区：
文献类型：
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作者：
FITZ, W;SCHWARK, JR;WONG, CH
N-乙酰神经氨酸缩醛酶对四种不同立体异构体的醛固酮具有不同的反应活性。C(3)修饰的D-甘露糖和D-葡萄糖分别不能发生酶促的羟醛加成反应。基于被测化合物的反应性(约58)，提出了一个将底物结构、反应性和在Neu5Ac缩醛酶催化反应中观察到的立体化学结果联系起来的机理方案。在L-红糖和D-苏糖反应中得到的缩合产物分别是具有生物意义的侧链修饰的唾液酸和D-KDO衍生物。
The four stereoisomeric aldotetroses were accepted with different reactivities by N-acetylneuraminic acid aldolase. C(3)-modified D-mannose and D-glucose derivatives, respectively, failed to undergo enzymatic aldol addition. Based on the observed reactivities of the tested compounds (about 58), a mechanistic scheme is proposed which relates substrate structure, reactivity and stereochemical outcome observed in Neu5Ac aldolase-catalyzed reactions. The condensation products obtained in the L-erythrose and D-threose reactions are side-chain modified sialic acid and D-KDO derivatives, respectively, of biological interest.