Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Randy S. Fischer"'
Publikováno v:
FEMS Microbiology Letters. 115:39-44
An important metabolic capability of Neisseria gonorrhoeae is the utilization of host-derived lactate. Two isoenzymes of the membrane-associated, pyridine dinucleotide-independent type of lactate dehydrogenase (iLDH) participate in lactate assimilati
Publikováno v:
Journal of General Microbiology. 138:1309-1316
A cohesive phylogenetic cluster that is limited to enteric bacteria and a few closely related genera possesses a bifunctional protein that is known as the T-protein and is encoded by tyrA. The T-protein carries catalytic domains for chorismate mutase
Publikováno v:
Journal of Biological Chemistry. 267:2487-2493
The gene encoding cyclohexadienyl dehydratase (denoted pheC) was cloned from Pseudomonas aeruginosa by functional complementation of a pheA auxotroph of Escherichia coli. The gene was highly expressed in E. coli due to the use of the high-copy number
Publikováno v:
Journal of General Microbiology. 137:1293-1301
Summary: The pheA gene encoding the bifunctional P-protein (chorismate mutase: prephenate dehydratase) was cloned from Pseudomonas stutzeri and sequenced. This is the first gene of phenylalanine biosynthesis to be cloned and sequenced from Pseudomona
Publikováno v:
Archives of biochemistry and biophysics. 256(1)
The 5- eneol -pyruvylshikimate-3-phosphate (EPSP) synthase from Bacillus subtilis was activated by monovalent cations, catalytic activity being negligible in the absence of monovalent cations. The order of cation effectiveness (NH 4 + > K + > Rb + >