Residues at the Active Site of the Esterase 2 fromAlicyclobacillus acidocaldarius Involved in Substrate Specificity and Catalytic Activity at High Temperature
Open Access
- 1 October 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (40) , 37482-37490
- https://doi.org/10.1074/jbc.m103017200
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase 1 1Edited by D. ReesJournal of Molecular Biology, 2000
- Cold Adaptation of a Mesophilic Subtilisin-like Protease by Laboratory EvolutionJournal of Biological Chemistry, 2000
- Directed evolution study of temperature adaptation in a psychrophilic enzyme 1 1Edited by J. A. WellsJournal of Molecular Biology, 2000
- Improving the Catalytic Activity of a Thermophilic Enzyme at Low TemperaturesBiochemistry, 2000
- Thermostable Lipase ofBacillus stearothermophilus: High-level Production, Purification, and Calcium-dependent ThermostabilityBioscience, Biotechnology, and Biochemistry, 2000
- Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostabilityJournal of Molecular Biology, 1999
- Hormone-sensitive lipase is closely related to several bacterial proteins, and distantly related to acetylcholinesterase and lipoprotein lipase: Identification of a superfamily of esterases and lipasesBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1994
- A new cloning vector and expression strategy for genes encoding proteins toxic to Escherichia coliGene, 1993
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970