Role of Lysine 39 of Alanine Racemase from Bacillus stearothermophilus That Binds Pyridoxal 5′-Phosphate
Open Access
- 1 February 1999
- journal article
- Published by Elsevier
- Vol. 274 (7) , 4189-4194
- https://doi.org/10.1074/jbc.274.7.4189
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Transamination as a Side-Reaction Catalyzed by Alanine Racemase of Bacillus stearothermophilusThe Journal of Biochemistry, 1998
- Reaction of Alanine Racemase with 1-Aminoethylphosphonic Acid Forms a Stable External Aldimine,Biochemistry, 1998
- Determination of the Structure of Alanine Racemase from Bacillus stearothermophilus at 1.9-Å Resolution,Biochemistry, 1997
- Kinetics of Thermostable Alanine Racemase ofBacillus stearothermophilusBioscience, Biotechnology, and Biochemistry, 1994
- Direct Brønsted Analysis of the Restoration of Activity to a Mutant Enzyme by Exogenous AminesScience, 1989
- Thermostable D-amino acid aminotransferase from a thermophilic Bacillus speciesJournal of Biological Chemistry, 1989
- Thermostable alanine racemase from Bacillus stearothermophilus: DNA and protein sequence determination and secondary structure predictionBiochemistry, 1988
- Thermostable alanine racemase from Bacillus stearothermophilus: molecular cloning of the gene, enzyme purification, and characterizationBiochemistry, 1986
- Proton nmr studies of substrate hydrogen exchange reactions catalyzed by L-methionine .gamma.-lyaseBiochemistry, 1985
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976