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Binding of vanadium (IV) to the phosphatase calcineurin
Author(s) -
Parra-Diaz Dennisse,
Wei Qun,
Lee Ernest Y.C.,
Echegoyen Luis,
Puett David
Publication year - 1995
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(95)01245-2
Subject(s) - chemistry , vanadium , calcineurin , phosphatase , enzyme , calmodulin , electron paramagnetic resonance , serine , binding site , vanadate , biochemistry , inorganic chemistry , nuclear magnetic resonance , medicine , physics , surgery , transplantation
X‐band electron spin resonance spectroscopy was used to study the binding of vanadium (IV), or vanadyl, to the brain serine/threonine phosphatase‐2B, calcineurin. Spectra were determined on frozen solutions of vanadyl and calcineurin at pH 7.4 in the presence of 20% (v/v) glycerol. The binding of vanadyl to the enzyme was established, and the data suggested the presence of two classes of sites, the higher affinity class of which contained two binding sites for vanadyl. The calcium‐binding B subunit of the heterodimeric protein was also shown to bind vanadyl. The holoprotein appeared to be stabilized by vanadyl, and vanadyl enhanced enzymatic activity when assayed with or without calmodulin in the absence of calcium.