Substrate analysis of homoserine acyltransferase from Bacillus cereus.
Substrate analysis of homoserine acyltransferase from Bacillus cereus.
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DOI：
10.1016/j.bbrc.2007.07.044
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发表时间：
2007-09
影响因子：
3.1
通讯作者：
Katharine Ziegler;M. Yusupov;B. Bishop;T. Born
中科院分区：
文献类型：
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作者：
Katharine Ziegler;M. Yusupov;B. Bishop;T. Born
被称为高丝氨酸琥珀酰转移酶的酶家族内的底物特异性是可变的，一些生物体利用琥珀酰辅酶A，而其他生物体利用乙酰辅酶A。在这项研究中，它表明，从蜡状芽孢杆菌的酶使用乙酰辅酶A作为其酰基供体，但其催化速率显着低于其他HTS家族成员。BcHTS被碘乙酰胺和焦碳酸二乙酯灭活，并且该酶可以被琥珀酰辅酶A的存在部分保护免于灭活。这导致的结论是，BcHTS可以结合乙酰辅酶A和琥珀酰辅酶A，并表明它可能代表之间的琥珀酸转移HTS家族成员和乙酸转移HTS家族成员的中间体。B。然而，蜡状酶不能拯救缺乏功能性琥珀酰转移酶的大肠杆菌菌株的生长。
Substrate specificity within the family of enzymes designated as homoserine transsuccinylases is variable, with some organisms utilizing succinyl-CoA and other organisms utilizing acetyl-CoA. In this study it is shown that the enzyme from Bacillus cereus uses acetyl-CoA as its acyl donor, but its catalytic rate is significantly lower than other HTS family members. BcHTS is inactivated by both iodoacetamide and diethyl pyrocarbonate and the enzyme can be partially protected from inactivation by the presence of succinyl-CoA. This leads to the conclusion that BcHTS can bind both acetyl-CoA and succinyl-CoA and suggests that it may represent an intermediate between the succinate-transferring HTS family members and the acetate-transferring HTS family members. The B. cereus enzyme was unable to rescue growth of an Escherichia coli strain lacking a functional transsuccinylase, however.