Evolution of an enzyme active site: The structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase-Reference-Cited by-同舟云学术

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Evolution of an enzyme active site: The structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase

Published:1998-09-01 Issue:18 Volume:95 Page:10396-10401
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Hasson M. S.,Schlichting I.,Moulai J.,Taylor K.,Barrett W.,Kenyon G. L.,Babbitt P. C.,Gerlt J. A.,Petsko G. A.,Ringe D.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference36 articles.

1. Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous

2. The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids

3. Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor

4. Octahedral coordination at the high-affinity metal site in enolase: Crystallographic analysis of the MgII-enzyme complex from yeast at 1.9 .ANG. resolution

5. A Functionally Diverse Enzyme Superfamily that Abstracts the α Protons of Carboxylic Acids

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2. The Birth of Genomic Enzymology: Discovery of the Mechanistically Diverse Enolase Superfamily;Biochemistry;2021-10-19

3. Promoting a More Integrated Approach to Structure and Function;Integrative and Comparative Biology;2021-06-28

4. Enzymes, pseudoenzymes, and moonlighting proteins: diversity of function in protein superfamilies;The FEBS Journal;2020-06-30

5. An Alternative Active Site Architecture for O2 Activation in the Ergothioneine Biosynthetic EgtB from Chloracidobacterium thermophilum;Journal of the American Chemical Society;2019-03-18

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