The Role of Dehydroalanine in Catalysis by Histidine Ammonia Lyase
- 31 July 1995
- journal article
- research article
- Published by Wiley in Angewandte Chemie International Edition in English
- Vol. 34 (13-14) , 1464-1465
- https://doi.org/10.1002/anie.199514641
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Histidine Ammonia-Lyase Mutant S143C Is Posttranslationally Converted into Fully Active Wild-Type Enzyme. Evidence for Serine 143 To Be the Precursor of Active Site DehydroalanineBiochemistry, 1994
- Serine‐202 is the putative precursor of the active site dehydroalanine of phenylalanine ammonia lyase Site‐directed mutagenesis studies on the enzyme from parsley (Petroselinum crispum L.)FEBS Letters, 1994
- Identification of Serine-143 as the Most Likely Precursor of Dehydroalanine in the Active Site of Histidine Ammonia-lyase. A study of the Overexpressed Enzyme by Site-Directed MutagenesisBiochemistry, 1994
- Identification of Ser143 as the Site of Modification in the Active Site of Histidine Ammonia-LyaseArchives of Biochemistry and Biophysics, 1993
- Mechanism of action of urocanaseEuropean Journal of Biochemistry, 1990
- Evidence for a carbanion intermediate in the elimination of ammonia from L-histidine catalyzed by histidine ammonia-lyaseJournal of the American Chemical Society, 1990
- Hazards of deducing enzyme structure-activity relationships on the basis of chemical applications of molecular biologyAccounts of Chemical Research, 1989
- 4-Nitro-L-histidine as a substrate for histidine ammonia-lyase: The role of β-hydrogen acidity in the rate-limiting stepBiochemical and Biophysical Research Communications, 1979
- Stereospecific irreversible inhibition of histidine ammonia-lyase by L-cysteineBiochemistry, 1974
- Steric course of the histidase reactionFEBS Letters, 1970