X-ray Structure of Novamyl, the Five-Domain “Maltogenic” α-Amylase from Bacillus stearothermophilus: Maltose and Acarbose Complexes at 1.7 Å Resolution,-Reference-Cited by-同舟云学术

X-ray Structure of Novamyl, the Five-Domain “Maltogenic” α-Amylase from Bacillus stearothermophilus: Maltose and Acarbose Complexes at 1.7 Å Resolution,

Published:1999-06-01 Issue:26 Volume:38 Page:8385-8392
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dauter Zbigniew¹,Dauter Miroslawa¹,Brzozowski A. Marek¹,Christensen Søren¹,Borchert Torben V.¹,Beier Lars¹,Wilson Keith S.¹,Davies Gideon J.¹

Affiliation:

1. Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York Y010 5DD, U.K., and Novo Nordisk A/S, Novo Allé, DK-2880 Bagsværd, Denmark

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi990256l

Reference37 articles.

1. A classification of glycosyl hydrolases based on amino acid sequence similarities

2. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities

3. Updating the sequence-based classification of glycosyl hydrolases

4. Multiple attack hypothesis of α-amylase action: Action of porcine pancreatic, human salivary, and Aspergillus oryzae α-amylases

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