How Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase Deals with Both Enantiomers of 2-Amino-1-propanol as Substrates: Structure-Based Rationalization,,-Reference-Cited by-同舟云学术

How Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase Deals with Both Enantiomers of 2-Amino-1-propanol as Substrates: Structure-Based Rationalization,,

Published:2010-12-30 Issue:4 Volume:50 Page:591-598
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Shibata Naoki¹²,Higuchi Yoshiki¹²,Toraya Tetsuo³

Affiliation:

1. Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan

2. RIKEN Harima Institute, SPring-8 Center, 1-1-1 Koto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan

3. Department of Bioscience and Biotechnology, Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka, Kita-ku, Okayama 700-8530, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi101696h

Reference40 articles.

1. The Stereochemistry of the Conversion of D and L 1,2-Propanediols to Propionaldehyde

2. Zum Mechanismus der Propandioldehydrase-Reaktion

3. Zur Stereochemie der Propandioldehydrase-Reaktion

4. Comparison of reactivity between d-propanediol and l-propanediol in intramolecular oxidation-reduction catalyzed by dioldehydrase requiring cobamide coenzyme

5. Relative enantiomer binding and reaction rates with propanediol dehydrase

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