Conversion of Aspartate Aminotransferase into anl-Aspartate β-Decarboxylase by a Triple Active-site Mutation
Open Access
- 1 October 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (44) , 31203-31208
- https://doi.org/10.1074/jbc.274.44.31203
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Redesigning the Substrate Specificity of an Enzyme by Cumulative Effects of the Mutations of Non-active Site ResiduesJournal of Biological Chemistry, 1999
- Conversion of Tyrosine Phenol-lyase to Dicarboxylic Amino Acid β-Lyase, an Enzyme Not Found in NaturePublished by Elsevier ,1999
- Directed evolution of an aspartate aminotransferase with new substrate specificitiesProceedings of the National Academy of Sciences, 1998
- Engineering nitrile hydratase activity into a cysteine protease by a single mutationBiochemistry, 1995
- Redesign of the substrate specificity ofescherichia coliaspartate aminotransferase to that ofescherichia colityrosine aminotransferase by homology modeling and site-directed mutagenesisProtein Science, 1995
- Evolutionary relationships among pyridoxal‐5′‐phosphate‐dependent enzymesEuropean Journal of Biochemistry, 1994
- Converting Trypsin to Chymotrypsin: The Role of Surface LoopsScience, 1992
- Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductaseBiochemistry, 1991
- Redesign of the coenzyme specificity of a dehydrogenase by protein engineeringNature, 1990
- A Specific, Highly Active Malate Dehydrogenase by Redesign of a Lactate Dehydrogenase FrameworkScience, 1988