Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog.

Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog. Research Abstract Details 

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Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog. Abstract Text:

K Sakai,S Kawashima,K Suzuki,K Imahori,

D-Fructose 1,6-bisphosphatase [EC 3.1.3.11, FBPase] is one of the key enzymes in glyconeogenesis and its activity is controlled by various effectors such as substrate, AMP and ATP. To analyze this complex regulation system, we tried an affinity labeling of FBPase with an AMP derivative, since AMP is a potent allosteric inhibitor of this enzyme. The results obtained are as follows. 1. To determine the functional groups which are essential for AMP as an inhibitor, inhibitory activities of some AMP derivatives were examined. These derivatives modified at the purine ring or phosphate group lost the activity while one modified at the ribose ring retained the ability to inhibit FBPase. This shows that an affinity labeling reagent should be an AMP derivative in which the ribose ring is modified. 2. 2',3'-Dialdehyde AMP (dial-AMP) was prepared by periodate oxidation of AMP and was reacted with FBPase. Under appropriate conditions, 1 mol of the reagent was incorporated per mol of enzyme subunit with a concomitant loss of enzyme activity. The reaction was prevented by the presence of AMP but not of ATP. The heat-stability, the kinetic parameters and the UV-absorption spectrum of the modified enzyme were all the same as those of native FBPase in the presence of AMP. Thus it was concluded that the allosteric AMP site in FBPase was modified specifically.

Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog. Publishing Authors By Initials

K Sakai,S Kawashima,K Suzuki,K Imahori,

For similar sulfhydryl compounds research abstracts see: sulfhydryl compounds research

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Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 102

Page Numbers: 377-84

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Aug

YEAR: 1987

Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog. Keywords Mesh Terms:

KEYWORDS: Sulfhydryl Compounds

MESH TERMS: analysis

Chemical & Substance for Abstract: Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog. Information

Substance Name: Fructose-Bisphosphatase

Registry Number: EC 3.1.3.11

Grant and Affiliation Information for Affinity labeling of the allosteric site of fructose 1,6-bisphosphatase with an AMP analog.

AFFILIATION: Department of Biochemistry, Faculty of Medicine, University of Tokyo.

Country: JAPAN

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MEDLINETA: J Biochem

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