Study on structure and function of enzymes acting on pullulan and related saccharides

This paper describes the study on the structure and function of enzymes hydrolyzing a polysaccharide, pullulan and the related enzymes. The paper is composed of the following three major sections. (1) A thermophilic actinomycete, Thermoactinomyces vulgaris R-47, produces two pullulan hydrolyzing-enz...

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Bibliographic Details
Published in:Journal of Applied Glycoscience 2009, Vol.56(1), pp.29-33
Main Author: Tonozuka, T.(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan))
Format: Article
Language:eng ; jpn
Subjects:
ARTHROBACTER
Arthrobacter globiformis
BIODEGRADACION
BIODEGRADATION
CHEMICAL STRUCTURE
ENZIMAS
ENZYME
ENZYMES
ESCHERICHIA COLI
ESTRUCTURA QUIMICA
GLUCOAMILASA
GLUCOAMYLASE
glucodextranase
GLUCOSIDASA
GLUCOSIDASE
GLUCOSIDASES
isopullulanase
MECANISMOS DE ACCION
MODE D'ACTION
MODE OF ACTION
POLISACARIDOS
POLYHOLOSIDE
POLYSACCHARIDES
pullulan
STRUCTURE CHIMIQUE
THERMOACTINOMYCES
Thermoactinomyces vulgaris
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Summary:This paper describes the study on the structure and function of enzymes hydrolyzing a polysaccharide, pullulan and the related enzymes. The paper is composed of the following three major sections. (1) A thermophilic actinomycete, Thermoactinomyces vulgaris R-47, produces two pullulan hydrolyzing-enzymes, TVA I and TVA II. TVA II forms a dimer, and this is the first observation of a dimeric enzyme in the alpha amylase family. In contrast, TVA I functions as a monomer, and domain N of TVA I is identified as a novel carbohydrate-binding module, CBM 34. (2) The crystal structure and function of the isopullulanase were determined. The isopullulanase forms a unique beta-helix fold, which is not found in other pullulan-hydrolyzing enzymes. (3) A glucoamylase gene was found downstream of the TVA II gene, and the primary structure of this glucoamylase resembled that of glucodextranase. The glucoamylase and related enzymes were further studied, and the crystal structures and functions of Arthrobacter globiformis I 42 glucodextranase (GDase) and Escherichia coli glucosidase, YgjK, have been determined. Although GDase and YgjK scarcely hydrolyzed starch and their substrate specificities were completely different from that of glucoamylase, these enzymes have a common (alpha/alpha)sub(6)-barrel domain like glucoamylase.
ISSN:1344-7882
1880-7291
DOI:10.5458/jag.56.29