Structural Basis for Substrate Specificity in Phosphate Binding (β/α)8-Barrels: d-Allulose 6-Phosphate 3-Epimerase from Escherichia coli K-12-Reference-Cited by-同舟云学术

Structural Basis for Substrate Specificity in Phosphate Binding (β/α)8-Barrels: d-Allulose 6-Phosphate 3-Epimerase from Escherichia coli K-12

Published:2008-08-14 Issue:36 Volume:47 Page:9608-9617
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chan Kui K.¹,Fedorov Alexander A.¹,Fedorov Elena V.¹,Almo Steven C.¹,Gerlt John A.¹

Affiliation:

1. Departments of Biochemistry and Chemistry, University of Illinois at Urbana−Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, and Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800821v

Reference27 articles.

1. One Fold with Many Functions: The Evolutionary Relationships between TIM Barrel Families Based on their Sequences, Structures and Functions

2. Catalytic Versatility, Stability, and Evolution of the (βα)8-Barrel Enzyme Fold

3. Structural Evidence for Evolution of the β/α Barrel Scaffold by Gene Duplication and Fusion

4. Divergent evolution of a β/α-barrel subclass: Detection of numerous phosphate-binding sites by motif search

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