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Bovine kidney low molecular weight acid phosphatase: FMN‐dependent kinetics
Author(s) -
Granjeiro José M.,
Ferreira Carmen V.,
Jucá Marilena B.,
Taga Eulázio M.,
Aoyama Hiroshi
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700202291
Subject(s) - flavin mononucleotide , chemistry , guanosine , hydrolysis , phosphate , kinetics , flavin group , molecular mass , acid phosphatase , biochemistry , enzyme , physics , quantum mechanics
A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0. Distinct activation energy values were obtained for p‐nitrophenyl phosphate‐ (45.44 kJ mol‐1) and flavin mononucleotide‐ (28.60 kJ mol‐1) hydrolysis reactions. The FMN hydrolysis was strongly inhibited by Cu2+ and pCMB, but activated by guanosine. Pyridoxal‐phosphate and vanadate were competitive inhibitors for the FMN‐dependent reaction.