Quantitative analysis of the action of Taka-amylase A on maltotriose.

Quantitative analysis of the action of Taka-amylase A on maltotriose. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Quantitative analysis of the action of Taka-amylase A on maltotriose. Abstract Text:

T Suganuma,M Ohnishi,R Matsuno,K Hiromi,

The action of Taka-amylase A from Asp. oryzae was studied quantitatively by the product analysis method using unlabeled maltotriose and maltotriose labeled at the reducing end as substrates. It was found that the ratio of the unlabeled products, maltose (G2) and glucose (G1) exceeded unity, and that the ratio of the labeled products, G2/G1 was strongly dependent on the initial substrate concentrations. The results can only be explained by a transglycosylation or condensation mechanism or both. Analysis of maltose labeled at the nonreducing or reducing end reveal that the ratio of the transglycosylation to the condensation mechanism was about 20:1 with about 80 mM maltotriose. A computer simulation was made on a reaction scheme involving the termolecular-shifted complex, transglycosylation and condensation besides hydrolysis, by using reported subsite affinities as modified by the authors. The simulation reproduced the experimental results satisfactorily.

Quantitative analysis of the action of Taka-amylase A on maltotriose. Publishing Authors By Initials

T Suganuma,M Ohnishi,R Matsuno,K Hiromi,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research

PUBMED ID PMID:

MEDLINE DATE:

Quantitative analysis of the action of Taka-amylase A on maltotriose. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 80

Page Numbers: 645-8

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1976

Quantitative analysis of the action of Taka-amylase A on maltotriose. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Quantitative analysis of the action of Taka-amylase A on maltotriose. Keywords Mesh Terms:

KEYWORDS: Protein Binding

MESH TERMS: metabolism

Chemical & Substance for Abstract: Quantitative analysis of the action of Taka-amylase A on maltotriose. Information

Substance Name: Amylases

Registry Number: EC 3.2.1.-

Grant and Affiliation Information for Quantitative analysis of the action of Taka-amylase A on maltotriose.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Quantitative analysis of the action of Taka-amylase A on maltotriose Related Publications

• A method for the deductive and unique determination of the values of three parameters involved in fractional functions applicable to relaxation kinetics.
• A study of the mechanism of action of Taka-amylase A1 on linear oligosaccharides by product analysis and computer simulation.
• Determination of the best-fit values of kinetic parameters of the Michaelis-Menten equation by the method of least squares with the Taylor expansion.
• Difference-spectrophotometry of the interaction of cycloheptaamylose with saccharifying alpha-amylase from Bacillus subtilis.
• Direct fluorometric determination of a dissociation constant as low as 10(-10) M for the subtilisin BPN'--protein proteinase inhibitor (Streptomyces subtilisin inhibitor) complex by a single photon counting technique.
• Elementary processes in the interaction of serine protease with a possible transition state analog. Subtillisin-benzeneboronic acid system.
• Inhibition by analogues of the hydrolysis of phenyl alpha-maltoside catalyzed by saccharifying alpha-amylase from Bacillus subtilis.
• Interaction of Asp. melleus Semi-alkaline protease with benzeneboronic acid.
• Interaction of alpha-chymotrypsin and a protein proteinase inhibitor, Streptomyces subtilisin inhibitor. The formation of ternary complex of Streptomyces subtilisin inhibitor, alpha-chymotrypsin, and proflavine.
• Interaction of cyclodextrins with fluorescent probes and its application to kinetic studies of amylase.
• Kinetic studies on the aerobic oxidation of reduced human ceruloplasmin.
• Kinetic study of lysozyme ethylene glycol chitin interaction.
• Kinetics of selective acylation of sn-glycerol 3-phosphate in the synthesis of phospholipid molecular species.
• Quantitative analysis of the action of Taka-amylase A on maltotriose.
• Reaction mechanism of saccharifying alpha-amylase from B. subtilis with maltose as a substrate.
• Spectrophotometric identification of the purple complex as an intermediate of the reaction of D-amino-acid oxidase using stopped-flow technique.
• Static and kinetic studies by fluorometry on the interaction between gluconolactone and glucoamylase from Rh. niveus.
• Stopped-flow studies on the chemical modification with N-bromosuccinimide of model compounds of tryptophan residues.
• Studies on the binding between acid proteinases and aliphatic alcohols with dyes as probes.
• Studies on the subsite structure of amylases. I. Interaction of glucoamylase with substrate and analogues studied by difference-spectrophotometry.
• Studies on the subsite structure of amylases. II. Difference-spectrophotometric studies on the interaction of maltotriose with liquefying alpha-amylase from Bacillus subtilis.
• Studies on the subsite structure of amylases. III. Inhibition by gluconolactone of the hydrolysis of maltodextrin catalyzed by glucoamylase from Rhizopus niveus.
• Studies on the subsite structure of amylases. IV. Tryptophan residues of glucoamylase from Rhizopus niveus studied by chemical modification with N-bromosuccinimide.
• TFIIH controls developmentally-regulated cell cycle progression as a holocomplex.
• Temperature-jump studies on benzeneboronic acid-serine protease interactions. Subtilisin and alpha-chymotrypsin.
• The effects of chemical modification by N-bromosuccinimide of saccharifying alpha-amylase from Bacillus subtilis on various substrates.
• The interaction of a tyrosyl residue and carboxyl groups in the specific interaction between Streptomyces subtilisin inhibitor and subtilisin BPN'. A chemical modification study.
• The role of tryptophan residues of bacterial liquefying alpha-amylase and Taka-amylase A in the enzymatic hydrolysis of linear substrates.
• The role of tyrosine residue of bacterial liquefying alpha-amylase in the enzymatic hydrolysis of linear substrates as studied by chemical modification with acetic anhydride.
• Tryptophan residues of saccharifying alpha-amylase from Bacillus subtilis. A kinetic discrimination of states of tryptophan residues using N-bromosuccinimide.