Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations.

Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations. Research Abstract Details 

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Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations. Abstract Text:

Y Nakajima,K Nakamura,

The most reactive single thiol group of rabbit skeletal muscle phosphofructokinase per protomer was modified with the following thiol reagents: iodoacetamide, iodoacetate, 2-hydroxyethyl disulfide, 3,3'-dithiodipropionate, and glutathione disulfide. As a result of the modification, there was increase in not only the apparent activation constants of activating monovalent cations, NH4+ (about 3-, 9-, 12-, 20-, and 30-fold, respectively) and K+ (about 3-, 10-, 15-, 17-, and 20-fold, respectively), but also the apparent Km for ATP (about 3-, 10-, 15-, 100-, and 20-fold, respectively) without any significant change in maximum velocity or apparent Km for fructose 6-phosphate in the presence of high concentrations of NH4+. These results suggest that modification of the thiol group destabilizes the enzyme-monovalent cation-MgATP complex proposed by Suelter [Science (1970) 168, 789-795], causing an apparent loss in catalytic activity.

Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations. Publishing Authors By Initials

Y Nakajima,K Nakamura,

For similar sulfhydryl compounds research abstracts see: sulfhydryl compounds research

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Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 109

Page Numbers: 251-5

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1991

Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations. Keywords Mesh Terms:

KEYWORDS: Sulfhydryl Compounds

MESH TERMS: chemistry

Chemical & Substance for Abstract: Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations. Information

Substance Name: Phosphofructokinase-1

Registry Number: EC 2.7.1.11

Grant and Affiliation Information for Chemical modification of the most reactive thiol group of rabbit skeletal muscle phosphofructokinase, to reduce its affinity toward substrate ATP and activating monovalent cations.

AFFILIATION: Department of Biochemistry, Kitasato University School of Medicine, Kanagawa.

Country: JAPAN

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MEDLINETA: J Biochem

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