Conversion of Aspartate Aminotransferase into anl-Aspartate β-Decarboxylase by a Triple Active-site Mutation-Reference-Cited by-同舟云学术

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Conversion of Aspartate Aminotransferase into anl-Aspartate β-Decarboxylase by a Triple Active-site Mutation

Published:1999-10 Issue:44 Volume:274 Page:31203-31208
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Graber Rachel,Kasper Patrik,Malashkevich Vladimir N.,Strop Pavel,Gehring Heinz,Jansonius Johan N.,Christen Philipp

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference41 articles.

1. A Specific, Highly Active Malate Dehydrogenase by Redesign of a Lactate Dehydrogenase Framework

2. Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase

3. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering

4. Converting Trypsin to Chymotrypsin: The Role of Surface Loops

5. Redesign of the substrate specificity ofescherichia coliaspartate aminotransferase to that ofescherichia colityrosine aminotransferase by homology modeling and site-directed mutagenesis

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1. Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase;Cell Reports Physical Science;2024-02

2. Redesigning transamination and decarboxylation characteristics of L-aspartate aminotransferase by site directed mutation of non-active site;Molecular Catalysis;2024-01

3. Structure-guided engineering ofPseudomonas dacunhael-aspartate β-decarboxylase forl-homophenylalanine synthesis;Chemical Communications;2020

4. Crystal structure of the aromatic-amino-acid aminotransferase fromStreptococcus mutans;Acta Crystallographica Section F Structural Biology Communications;2019-01-24

5. Bioinformatic analysis of the fold type I PLP ‐dependent enzymes reveals determinants of reaction specificity in l ‐threonine aldolase from Aeromonas jandaei;FEBS Open Bio;2018-05-21

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