TY - JOUR
T1 - Calcineurin hydrolysis of para-nitrophenyl phosphorothioate
AU - Spannaus-Martin, Donna J.
AU - Martin, Bruce L.
PY - 2004/4/1
Y1 - 2004/4/1
N2 - para-Nitrophenyl phosphorothioate (pNPT) was hydrolyzed by calcineurin at initial rates slightly, but comparable to rates for para-nitrophenyl phosphate (pNPP). Kinetic characterization yielded higher estimates for both Km and Vmax compared to pNPP. Metal ion activation of phosphorothioate hydrolysis was more promiscuous. Unlike the hydrolysis of with pNPP, Ca 2+, Mg2+, and Ba2+ activated calcineurin as well as Mn2+.
AB - para-Nitrophenyl phosphorothioate (pNPT) was hydrolyzed by calcineurin at initial rates slightly, but comparable to rates for para-nitrophenyl phosphate (pNPP). Kinetic characterization yielded higher estimates for both Km and Vmax compared to pNPP. Metal ion activation of phosphorothioate hydrolysis was more promiscuous. Unlike the hydrolysis of with pNPP, Ca 2+, Mg2+, and Ba2+ activated calcineurin as well as Mn2+.
KW - Calcineurin
KW - Metal-activated enzyme
KW - Substrate analog
KW - Substrate specificity
UR - http://www.scopus.com/inward/record.url?scp=1942521048&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=1942521048&partnerID=8YFLogxK
U2 - 10.2174/0929866043478338
DO - 10.2174/0929866043478338
M3 - Article
C2 - 15078203
AN - SCOPUS:1942521048
SN - 0929-8665
VL - 11
SP - 149
EP - 155
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
IS - 2
ER -