Interaction of muscle glycogen phosphorylase b reconstituted from apoenzyme and analogs of pyridoxal-5'-phosphate with specific ligands

被引：0

作者：

Chebotareva, NA ^{[1
]}

Sugrobova, NP ^{[1
]}

Bulanova, LN ^{[1
]}

Poznanskaya, AA ^{[1
]}

Kurganov, BI ^{[1
]}

Gunar, VI ^{[1
]}

机构：

[1] RUSSIAN ACAD SCI,BAKH INST BIOCHEM,MOSCOW 117071,RUSSIA

来源：

BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL | 1996年 / 38卷 / 05期

关键词：

glycogen phosphorylase b; reconstitution with PLP; self-association; inhibition by FMN; analogs of PLP;

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphorylase b from rabbit skeletal muscles was reconstituted with analogs of PLP containing residues -CH2-CH2-COOH, trans-CH=CH-COOH or -C=COOH at position 5. Replacing native coenzyme in the phosphorylase molecule with any PLP analog tested leads to the decrease in the enzyme affinity for the allosteric inhibitor, FMN. Phosphorylase b reconstituted with analogs of PLP shows the greater ability for association in tetramers in the presence of 1 mM AMP than native enzyme.

引用

页码：1033 / 1040

页数：8

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