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Adenosine di‐, tri‐ and tetraphosphopyridoxals modify the same lysyl residue at the ATP‐binding site in adenylate kinase
Author(s) -
Yagami Tatsurou,
Tagaya Mitsuo,
Fukui Toshio
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81137-2
Subject(s) - adenylate kinase , binding site , chemistry , adenosine , residue (chemistry) , adenosine kinase , biochemistry , adenosine triphosphate , enzyme , microbiology and biotechnology , biology , adenosine deaminase
Adenosine diphosphopyridoxal modifies Lys‐21 in adenylate kinase which is located in a glycine‐rich loop [(1987) J. Biol. Chem. 262, 8257–8261]. We presently report that adenosine tri‐ and tetraphosphopyridoxals modify the same lysyl residue more rapidly than the diphospho compound does. However, susceptibilities of the Schiff bases between the labels and the lysyl residue to sodium borohydride considerably differ in the modifications with the three reagents. These observations seem to be ascribable to the mobility of the ε‐amino group of Lys‐21 in the active‐site region of the enzyme.