Open AccessStructural relationships in the adenylate kinase family
Author(s) -
SCHULZ Georg E.,
SCHILTZ Emile,
TOMASSELLI Alfredo G.,
FRANK Rainer,
BRUNE Martin,
WITTINGHOFER Alfred,
SCHIRMER R. Heiner
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb10132.x
Subject(s) - adenylate kinase , isozyme , enzyme , structural similarity , biology , similarity (geometry) , biochemistry , cytosol , active site , kinase , amino acid , genetics , computer science , artificial intelligence , image (mathematics)
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.