Studies on amino acid decarboxylases in Escherichia coli
- 1 November 1967
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 105 (2), 483-490
- https://doi.org/10.1042/bj1050483
Abstract
The isolation of highly active preparations of glutamate decarboxylase, arginine decarboxylase and histidine decarboxylase from Escherichia coli is described. These preparations showed strict specificity, and were in each case resolved into apo- and co-enzyme as shown by the significant restoration of activity that took place on addition of pyridoxal 5-phosphate.This publication has 23 references indexed in Scilit:
- Suppression of histamine synthesis in guinea pigs by α-methyl-3,4-dihydroxyphenylalanineBiochimica et Biophysica Acta (BBA) - General Subjects, 1965
- CRYSTALLINE HISTIDINEDECARBOXILASE OBTAINED FROM MICROCOCCUS SP N1964
- On the presence of different histidine decarboxylating enzymes in mammalian tissuesCellular and Molecular Life Sciences, 1961
- The interaction between pyridoxal-5-phosphate and arginine apodecarboxylaseCellular and Molecular Life Sciences, 1958
- Effects of cations on amino acid decarboxylasesBiochemical Journal, 1958
- STUDIES ON l-GLUTAMIC ACID DECARBOXYLASE FROM ESCHERICHIA COLIJournal of Biological Chemistry, 1954
- BETA-HYDROXYGLUTAMIC ACID DECARBOXYLASE1953
- Studies on bacterial amino-acid decarboxylasesBiochemical Journal, 1945
- Studies on bacterial amino-acid decarboxylasesBiochemical Journal, 1945
- The production of amines by bacteriaBiochemical Journal, 1940