一种原核苯丙氨酸解氨酶的生化特性
Biochemical characterization of a prokaryotic phenylalanine ammonia lyase.
作者信息
Xiang Longkuan, Moore Bradley S
机构信息
College of Pharmacy, University of Arizona, Tucson, Arizona 85721-0207, USA.
出版信息
J Bacteriol. 2005 Jun;187(12):4286-9. doi: 10.1128/JB.187.12.4286-4289.2005.
Abstract
The committed biosynthetic reaction to benzoyl-coenzyme A in the marine bacterium "Streptomyces maritimus" is carried out by the novel prokaryotic phenylalanine ammonia lyase (PAL) EncP, which converts the primary amino acid L-phenylalanine to trans-cinnamic acid. Recombinant EncP is specific for L-phenylalanine and shares many biochemical features with eukaryotic PALs, which are substantially larger proteins by approximately 200 amino acid residues.
摘要
海洋细菌“海链霉菌”中对苯甲酰辅酶A的特定生物合成反应是由新型原核苯丙氨酸解氨酶（PAL）EncP进行的，它将初级氨基酸L-苯丙氨酸转化为反式肉桂酸。重组EncP对L-苯丙氨酸具有特异性，并且与真核PAL具有许多生化特征，真核PAL的蛋白质要大得多，大约多200个氨基酸残基。
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