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The comparative amino acid sequences, substrate specificities and gene or cDNA nucleotide sequences of some prokaryote and eukaryote amidinotransferases: implications for evolution
Authors:Ajay Bedekar  Robert M Zink  David H Sherman  Theresa V Line  John F Van Pilsum
Institution:aDepartment of Biochemistry, The Medical School, 4–225 Millard Hall, 435 Delaware St. S.E., University of Minnesota, Minneapolis, Minnesota 55455-0347, USA;bBell Museum, 100 Ecology Building, University of Minnesota, St. Paul, MN 55108, USA;cDepartment of Microbiology and Biological Process Technology Institute, 240 Gortner Laboratory, 1479 Gortner Avenue, University of Minnesota, St. Paul, Minnesota 55108-0122, USA
Abstract:The amino acid sequences of the amidinotransferases and the nucleotide sequences of their genes or cDNA from four Streptomyces species (seven genes) and from the kidneys of rat, pig, human and human pancreas were compared. The overall amino acid and nucleotide sequences of the prokaryotes and eukaryotes were very similar and further, three regions were identified that were highly identical. Evidence is presented that there is virtually zero chance that the overall and high identity regions of the amino acid sequence similarities and the overall nucleotide sequence similarities between Streptomyces and mammals represent random match. Both rat and lamprey amidinotransferases were able to use inosamine phosphate, the amidine group acceptor of Streptomyces. We have concluded that the structure and function of the amidinotransferases and their genes has been highly conserved through evolution from prokaryotes to eukaryotes. The evolution has occurred with: (1) a high degree of retention of nucleotide and amino acid sequences; (2) a high degree of retention of the primitive Streptomyces guanine+cytosine (G+C) third codon position composition in certain high identity regions of the eukaryote cDNA; (3) a decrease in the specificities for the amidine group acceptors; and (4) most of the mutations silent in the regions suggested to code for active sites in the enzymes.
Keywords:Amidinotransferases  Homo sapiens  Petromyzon marinus  Rattus norvegicus  Streptomyces  Sus scrofa
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