Alteration of the Diastereoselectivity of 3-Methylaspartate Ammonia Lyase by Using Structure-Based Mutagenesis-Reference-Cited by-同舟云学术

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Alteration of the Diastereoselectivity of 3-Methylaspartate Ammonia Lyase by Using Structure-Based Mutagenesis

Published:2009-09-04 Issue:13 Volume:10 Page:2236-2245
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Raj Hans,Weiner Barbara,Puthan Veetil Vinod,Reis Carlos R.,Quax Wim J.,Janssen Dick B.,Feringa Ben L.,Poelarends Gerrit J.

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/cbic.200900311/fullpdf

Reference27 articles.

1. The Purification and Properties of β-Methylaspartase

2. Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding .beta.-methylaspartase and characterization of the recombinant protein

3. Substrate specificity of the 3-methylaspartate ammonia-lyase reaction: observation of differential relative reaction rates for substrate-product pairs

4. Preparation of N-substituted aspartic acids via enantiospecific conjugate addition of N-nucleophiles to fumaric acids using methylaspartase: synthetic utility and mechanistic implications 1

5. The Mechanism of the β-Methylaspartase Reaction

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3. Conformational gating in ammonia lyases;Biochimica et Biophysica Acta (BBA) - General Subjects;2020-07

4. Recent Applications of Carbon‐Nitrogen Lyases in Asymmetric Synthesis of Noncanonical Amino Acids and Heterocyclic Compounds;ChemBioChem;2020-06-08

5. Structure-function investigation of 3-methylaspartate ammonia lyase reveals substrate molecular determinants for the deamination reaction;PLOS ONE;2020-05-21

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