Pascarella S, Bossa F
Dipartimento di Scienze Biochimiche, Università La Sapienza, Rome, Italy.
Protein Sci. 1994 Apr;3(4):701-5. doi: 10.1002/pro.5560030418.
A multiple sequence alignment among aspartate aminotransferase, dialkylglycine decarboxylase, and serine hydroxymethyltransferase (DAS) was used for profile databank search. The DAS profile could detect similarities to other pyridoxal or pyridoxamine phosphate-dependent enzymes, like several gene products involved in dideoxysugar and deoxyaminosugar synthesis. The alignment among DAS and such gene products shows the conservation of aspartate 222 and lysine 258, which, in aspartate aminotransferase, interacts with the N1 of the coenzyme pyridine ring and forms the internal Schiff base, respectively. The lysine is replaced by histidine in the pyridoxamine phosphate-dependent gene products. The alignment indicates also that the region encompassing the coenzyme binding site is the most conserved.
天冬氨酸转氨酶、二烷基甘氨酸脱羧酶和丝氨酸羟甲基转移酶(DAS)之间的多序列比对用于数据库搜索。DAS图谱可检测到与其他磷酸吡哆醛或磷酸吡哆胺依赖性酶的相似性,例如参与双脱氧糖和脱氧氨基糖合成的几种基因产物。DAS与这些基因产物之间的比对显示,天冬氨酸222和赖氨酸258保守,在天冬氨酸转氨酶中,它们分别与辅酶吡啶环的N1相互作用并形成内部席夫碱。在磷酸吡哆胺依赖性基因产物中,赖氨酸被组氨酸取代。比对还表明,包含辅酶结合位点的区域是最保守的。