Arogenate Dehydrogenase fromStreptomyces phaeochromogenesPurification and Properties
- 1 January 1985
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 366 (2) , 1063-1066
- https://doi.org/10.1515/bchm3.1985.366.2.1063
Abstract
Arogenate dehydrogenase, the terminal enzyme of tyrosine biosynthesis in S. phaeochromogenes, was purified to homogeneity by a five-step procedure. The enzyme is a dimer of Mr 57,600 as determined by dodecyl sulfate polyacrylamide gel electrophoresis after cross-linking of the monomers, or of 66,300 as found by gel permeation chromatography, and consists of two identical subunits of Mr 28,100. The pI of the enzyme is 4.45 and the Km values of 0.105 mM for arogenate and 0.01 mM for .**GRAPHIC**.This publication has 3 references indexed in Scilit:
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- Purification and Properties of Histidinol Dehydrogenase from Salmonella typhimuriumJournal of Biological Chemistry, 1965