Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase.

Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase. Research Abstract Details 

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Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase. Abstract Text:

S Onodera,H Matsui,S Chiba,

The substrate specificity of rabbit liver acid alpha-glucosidase was investigated. The enzyme showed a wide specificity for various substrates, and hydrolyzed alpha-glucans such as glycogen and soluble starch. The k0 values (s-1) for maltose, kojibiose, nigerose, isomaltose, phenyl alpha-glucoside, panose, phenyl alpha-maltoside, soluble starch, beta-limit dextrin, amylopectin, shellfish glycogen, and rabbit liver glycogen were estimated to be 94.8, 18.8, 143, 3.6, 11.8, 27.8, 115, 99.2, 155, 83.5, 126, and 108, and the Km values (concentration of non-reducing terminal) for these substrates were 2.1, 1.8, 7.5, 36, 5.4, 1.9, 1.2, 0.90, 9.1, 1.0, 16, and 13 mM, respectively. Isomaltose and phenyl alpha-glucoside were unfavorable as substrates. The acid alpha-glucosidase is characterized by a relatively high activity toward glycogen. The k0 values (s-1) for maltotriose, -tetraose, -pentaose, -hexaose, -heptaose, and -octaose, and maltodextrin (n = 17) were 140, 140, 131, 132, 134, 132, and 74.3, and the Km values, 2.1, 1.8, 1.9, 3.4, 5.0, 4.9, 4.9 and 2.6 mM, respectively. Based on the rate parameters for the series of maltooligosaccharides, the subsite affinities (Ais) in the active site were evaluated as 0.54 (A1), 5.34 (A2), and 0.34 (A3) kcal/mol for subsites 1, 2, and 3, respectively. These three subsites were considered to be predominantly responsible for the binding of substrates to the active site.

Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase. Publishing Authors By Initials

S Onodera,H Matsui,S Chiba,

For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: glucosidases: alpha-glucosidases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: glucosidases: alpha-glucosidases research

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Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 116

Page Numbers: 7-11

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1994

Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase. Keywords Mesh Terms:

KEYWORDS: alpha-Glucosidases

MESH TERMS: metabolism

Chemical & Substance for Abstract: Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase. Information

Substance Name: alpha-Glucosidases

Registry Number: EC 3.2.1.20

Grant and Affiliation Information for Substrate specificity and subsite affinities of rabbit liver acid alpha-glucosidase.

AFFILIATION: Department of Bioscience and Chemistry, Faculty of Agriculture, Hokkaido University.

Country: JAPAN

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MEDLINETA: J Biochem

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