Schulz G E, Schiltz E, Tomasselli A G, Frank R, Brune M, Wittinghofer A, Schirmer R H
Eur J Biochem. 1986 Nov 17;161(1):127-32. doi: 10.1111/j.1432-1033.1986.tb10132.x.
The sequences of five distantly related adenylate kinases have been aligned. The local conservation of amino acids is discussed in the light of the known three-dimensional structure of one of the enzymes, the cytosolic isoenzyme 1 (AK1) from porcine muscle. The similarity profile outlines clearly the active site in the cleft of the spatial structure of AK1. The alignment reveals further that the enzyme family can be subdivided into small and large variants according to the presence or absence of a particular segment of about 30 residues in the middle of the chain. The extra segments of the large variants are strongly conserved.
已对五种亲缘关系较远的腺苷酸激酶序列进行了比对。根据其中一种酶(猪肌肉胞质同工酶1,即AK1)的已知三维结构,讨论了氨基酸的局部保守性。相似性图谱清晰地勾勒出了AK1空间结构裂隙中的活性位点。比对结果还显示,根据链中间约30个残基的特定片段的有无,该酶家族可细分为小变体和大变体。大变体的额外片段高度保守。