Muñoz Ma Enriqueta, Ponce Elizabeth
Facultad de Ciencias Quíicas e Ingenierí, Universidad Autónoma de Baja California, Av. Tecnológico s/n, Mesa de Otay, B.C., Tijuana, Mexico C.P. 22390.
Comp Biochem Physiol B Biochem Mol Biol. 2003 Jun;135(2):197-218. doi: 10.1016/s1096-4959(03)00081-2.
Pyruvate kinase (PK) is a key enzyme for the glycolytic pathway and carbon metabolism in general. On the basis of the relevance and enormous diverse properties of this enzyme, this paper describes the results of a current and extensive review that determines the sites of conservation and/or difference in PK sequences, and the differences in the functional and regulatory properties of the enzymes. An alignment and analysis of 50 PK sequences from different sources and a phylogenetic tree are presented. This analysis was performed with reference to crystallographically characterized PK principally from E. coli, cat and rabbit muscle. A number of attributes of the enzyme that make it of particular interest in biomedicine and industry are also discussed.
丙酮酸激酶(PK)是糖酵解途径以及一般碳代谢的关键酶。基于该酶的相关性和极其多样的特性,本文描述了一项当前广泛综述的结果,该综述确定了PK序列中的保守位点和/或差异位点,以及这些酶在功能和调节特性方面的差异。文中呈现了来自不同来源的50个PK序列的比对和分析结果以及一棵系统发育树。该分析主要参考了来自大肠杆菌、猫和兔肌肉的经晶体学表征的PK。还讨论了该酶在生物医学和工业领域中备受关注的一些特性。