In vivo Regulation of NADP-specific Glutamate Dehydrogenase by L-Amides in Stemphylium botryosum
نویسندگان
چکیده
منابع مشابه
Characterization of L-asparagine transport systems in Stemphylium botryosum.
L-Asparagine uptake by Stemphylium botryosum is mediated by two distinct energy- and temperature-dependent transport systems. One permease is relatively specific for L-asparagine and L-glutamine and is present in nutrient-sufficient mycelium. The specific permease shows an optimum pH at 5.2, saturation kinetics (Km = 4.4 x 10(-4) M, Vmax = 1.1 mumol/g per min), competitive gradient of L-asparag...
متن کاملRe-investigation of the effects of L-glutamine and L-asparagine on the Neurospora crassa NADP-specific glutamate dehydrogenase.
L-Glutamine, when purified free of traces of NH4+ present in solution, does not act as an alternative substrate to NH4+ for the NADP-specific glutamate dehydrogenase of Neurospora. L-Glutamine interferes with detection of small quantities of NH4+ by Nessler's reagent. L-Asparagine is not an alternative substrate to NH4+ for this enzyme.
متن کاملsuppression of coke formation in thermal cracking by coke inhibitors
the main purpose of this research was to:1.develop a coking model for thermal cracking of naphtha.2.study coke inhibition methods using different coke inhibitors.developing a coking model in naphtha cracking reactors requires a suitable model of the thermal cracking reactor based on a reliable kinetic model.to obtain reliable results all these models shall be solved simultaneously.for this pu...
15 صفحه اولAmino-acid sequence of NADP-specific glutamate dehydrogenase of neurospora crassa.
A tentative primary structure of the NADP-specific glutamate dehydrogenase [L-glutamate: NADP oxidoreductase (deaminating), EC 1.4.1.4] from Neurospora crassa has been determined. The proposed sequence contains 452 amino-acid residues in each of the identical subunits of the hexameric enzyme. Comparison of the sequence with that of the bovine liver enzyme reveals considerable homology in the am...
متن کاملRegulation of glutamate dehydrogenase in Bacillus subtilis.
The activity of the nicotinamide adenine dinucleotide-dependent glutamate dehydrogenase in Bacillus subtilis was influenced by the carbon source, but not the nitrogen source, in the growth medium. The highest specific activity for this enzyme was found when B. subtilis was grown in a minimal or rich medium that contained glutamate as the carbon source. It is proposed that glutamate dehydrogenas...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1978
ISSN: 0022-1287
DOI: 10.1099/00221287-106-2-343