A cysteine-histidine-aspartate catalytic triad is involved in glutamine amide transfer function in purF-type glutamine amidotransferases
Open Access
- 1 October 1989
- journal article
- Published by Elsevier
- Vol. 264 (28) , 16613-16619
- https://doi.org/10.1016/s0021-9258(19)84750-6
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterizationBiochemistry, 1989
- Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operonsJournal of Molecular Biology, 1988
- The Catalytic Role of the Active Site Aspartic Acid in Serine ProteasesScience, 1987
- The Three-Dimensional Structure of Asn 102 Mutant of Trypsin: Role of Asp 102 in Serine Protease CatalysisScience, 1987
- Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacementsBiochemistry, 1985
- Evolution of glutamine amidotransferase genesJournal of Molecular Biology, 1985
- Nucleotide sequence of Escherichia coli pabA and its evolutionary relationship to trp (G) DJournal of Molecular Biology, 1983
- Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescensJournal of Molecular Biology, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970