Abstract：
:The kinetics of the native glycogen phosphorylase b from rabbit skeletal muscle and of the enzyme specifically deiminated by peptidylarginine deiminase have been studied. One arginine residue per phosphorylase b monomer is transformed into citrulline after 3 h of incubation with peptidylarginine deiminase. The maximal velocity of the enzymatic reaction for the modified phosphorylase b is 7-20% higher than that for the native enzyme. Deiminated phosphorylase b, like the native enzyme, shows a positive kinetic cooperativity with respect to glucose-1-phosphate. The affinity of the modified phosphorylase b for the allosteric activator AMP is one order of magnitude higher than that of the native enzyme. Deimination caused a pronounced reduction of the values of [I]0.5 for FMN and glucose, but the sensitivity of the deiminated enzyme to glucose-6-phosphate is much lower than that of the native phosphorylase b. Deiminated phosphorylase b, unlike the native enzyme, shows the positive cooperativity for FMN binding. Deiminated phosphorylase b, unlike the native enzyme, shows less capability to form tetramers in the presence of AMP as compared to the native enzyme.
journal_name
Biochimiejournal_title
Biochimieauthors
Eronina TB,Livanova NB,Chebotareva NA,Kurganov BI,Luo S,Graves DJdoi
10.1016/0300-9084(96)82188-2subject
Has Abstractpub_date
1996-01-01 00:00:00pages
253-8issue
4eissn
0300-9084issn
1638-6183pii
0300-9084(96)82188-2journal_volume
78pub_type
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