Pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a. Covalent modifications of aspartic acid 191, lysine 155, and the pyruvoyl group.
Open Access
- 1 April 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (10) , 4389-4394
- https://doi.org/10.1016/s0021-9258(17)38513-7
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Structure determination of histidine decarboxylase from Lactobacillus 30a at 3.0 Å resolutionJournal of Molecular Biology, 1985
- PYRUVOYL ENZYMESAnnual Review of Biochemistry, 1984
- The molecular symmetry of histidine decarboxylase and prohistidine decarboxylase by rotation-function analysisActa crystallographica Section B, Structural science, crystal engineering and materials, 1983
- Histidine decarboxylase of lactobacillus 30a: inactivation and active-site labeling by L-histidine methyl esterBiochemistry, 1976
- Histidine decarboxylase of Lactobacillus 30a: function and reactivity of sulfhydryl groupsBiochemistry, 1976
- 7 Amino Acid DecarboxylasesPublished by Elsevier ,1972
- Histidine decarboxylase of Lactobacillus 30a. VI. Mechanism of action and kinetic propertiesBiochemistry, 1970
- Histidine decarboxylase of Lactobacillus 30a. IV. The presence of covalently bound pyruvate as the prosthetic groupBiochemistry, 1968
- Histidine decarboxylase of Lactobacillus 30a. II. Purification, substrate specificity, and stereospecificityBiochemistry, 1968
- Thiolysis of some dinitrophenyl derivatives of amino acidsBiochemical and Biophysical Research Communications, 1967