Zobrazeno 1 - 10
of 48
pro vyhledávání: '"S. H. G. Allen"'
Publikováno v:
Journal of bacteriology. 175(22)
The Bacillus subtilis gene encoding acetate kinase was identified on the basis of sequence similarity to the Escherichia coli ackA gene and to a second E. coli gene closely related to ackA. Insertional inactivation of this region of the B. subtilis c
Publikováno v:
Journal of Biological Chemistry. 238:1637-1642
Publikováno v:
Journal of Bacteriology. 87:171-187
Allen , S. H. G. (Western Reserve University, Cleveland, Ohio), R. W. Kellermeyer, R. L. Stjernholm, and Harland G. Wood . Purification and properties of enzymes involved in the propionic acid fermentation. J. Bacteriol. 87: 171–187. 1964.—Chroma
Autor:
Dorothy M. Powelson, S. H. G. Allen
Publikováno v:
Journal of Bacteriology. 75:184-189
Publikováno v:
Journal of Biological Chemistry. 238:PC2889-PC2892
Publikováno v:
Journal of Biological Chemistry. 238:547-556
Publikováno v:
Journal of Biological Chemistry. 239:2562-2569
Publisher Summary This chapter describes the enzyme that is prepared from Propionibacterium shermanii (52W). The (S)-methyhnalonyl-CoA formed as a result of racemase action is converted to propionyl-CoA and oxaloacetate through the oxaloacetate trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7fae485a77b05b51e0376acec22ceb87
https://doi.org/10.1016/0076-6879(69)13038-4
https://doi.org/10.1016/0076-6879(69)13038-4
Publikováno v:
Archives of biochemistry and biophysics. 105
Propionyl-CoA carboxylase containing tritium-labeled biotin has been partially purified from Mycobacterium smegmatis. After preliminary purification the purity of the enzyme can be followed by specific radioactivity. The propionyl-CoA carboxylase of
Publikováno v:
Annals of the New York Academy of Sciences. 112