Adenosine di‐, tri‐ and tetraphosphopyridoxals modify the same lysyl residue at the ATP‐binding site in adenylate kinase

FEBS Letters

Yagami, Tatsurou¹  Tagaya, Mitsuo¹  Fukui, Toshio¹ 

[1]Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567, Japan

关键词: Adenylate kinase;    Nucleotide-binding protein;    Affinity label;    Adenosine polyphosphopyridoxal;    Glycine-rich region;    Induced fit;    AP2-PL;    adenosine diphosphopyridoxal;    AP3-PL;    adenosine triphosphopyridoxal;    AP4-PL;    adenosine tetraphosphopyridoxal;   

DOI  :  10.1016/0014-5793(88)81137-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown