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Titolo:
Amylolytic enzymes: Molecular aspects of their properties
Autore:
Horvathova, V; Janecek, S; Sturdik, E;
Indirizzi:
Slovak Acad Sci, Inst Mol Biol, Bratislava 84251, Slovakia Slovak Acad Sci Bratislava Slovakia 84251 ol, Bratislava 84251, Slovakia Univ SS Constantine & Methodius, Fac Nat Sci, Dept Biotechnol, Trnava 91701, Slovakia Univ SS Constantine & Methodius Trnava Slovakia 91701 va 91701, Slovakia Slovak Univ Technol, Fac Chem Technol, Dept Biochem Technol, Bratislava 81237, Slovakia Slovak Univ Technol Bratislava Slovakia 81237 Bratislava 81237, Slovakia
Titolo Testata:
GENERAL PHYSIOLOGY AND BIOPHYSICS
fascicolo: 1, volume: 20, anno: 2001,
pagine: 7 - 32
SICI:
0231-5882(200103)20:1<7:AEMAOT>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
STARCH-BINDING DOMAIN; PANCREATIC ALPHA-AMYLASE; SOYBEAN BETA-AMYLASE; X-RAY STRUCTURE; BACILLUS-CIRCULANS STRAIN-251; SITE-DIRECTED MUTAGENESIS; AMINO-ACID-RESIDUES; AWAMORI VAR X100; THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1; CATALYTIC (BETA/ALPHA)(8)-BARREL DOMAIN;
Keywords:
amylase; catalytic barrel domain; starch-binding domain; structure-function relationships;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
168
Recensione:
Indirizzi per estratti:
Indirizzo: Janecek, S Slovak Acad Sci, Inst Mol Biol, Dubravska Cesta 21, Bratislava 84251, Slovakia Slovak Acad Sci Dubravska Cesta 21 Bratislava Slovakia 84251 a
Citazione:
V. Horvathova et al., "Amylolytic enzymes: Molecular aspects of their properties", GEN PHYSL B, 20(1), 2001, pp. 7-32

Abstract

The present review describes the structural features of alpha -amylase, beta -amylase and glucoamylase that are the best known amylolytic enzymes. Although they show similar function, i.e. catalysis of hydrolysis of alpha -glucosidic bonds in starch and related saccharides, they are quite different. alpha -amylase is the alpha --> alpha retaining glycosidase tit uses the retaining mechanism), and P-amylase together with glucoamylase are the alpha --> beta inverting glycosidases (they use the inverting mechanism). Whilebeta -amylase and glucoamylase form their own families 14 and 15, respectively, in the sequence-based classification of glycoside hydrolases, alpha -amylase belongs to a large dan of three families 13, 70 and 77 consisting of almost 30 different specificities. Structurally both alpha -amylase and beta -amylase sank among the parallel (beta/alpha)(8)-barrel enzymes, glucoamylase adopts the helical (alpha/alpha)(6)-barrel fold. The catalytic (beta/alpha)(8)-barrels of alpha -amylase and beta -amylase differ from each other. The only common sequence-structural feature is the presence of the starch-binding domain responsible for the binding and ability to digest raw starch. It is, however, present in about 10 % of amylases and behaves as an independent evolutionary module. A brief discussion on structure-function andstructure-stability relationships of cr-amylases and related enzymes is also provided.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 01:03:46