Adaptive enzymes in the estimation of gluconate D-arabinose, and D-ribose.

نویسندگان

  • S S COHEN
  • R RAFF
چکیده

The small amount of carbohydrate available in our recent studies (1) of pentose formation from 6-phosphogluconic .acid has led us to examine microbiological analytical tools. In earlier studies on uranic acid metabolism in an Escherichia coli strain (2), it had become clear that the adaptive synthesis of new enzyme systems in response to the presence of specific substrates is extraordinarily specific. Cells adapted to uranic acids were incapable of fermenting n-ribose, n-arabinose, or n-xylose. Cells adapted to any one of these pentoses were incapable of fermenting the other two. Furthermore, the adaptive method provided a true control for the microbiological analysis of a mixture of sugars, since the strains examined are capable of using glucose and certain other sugars non-adaptively (i.e. with constitutive enzymes), whereas the adapted strain can utilize these substrates plus the new substrate. Therefore, non-adapted cells could be used to exhaust the substrate of fermentable material, with the exception of the substance to be determined on addition of the adapted cells. Gluconate, n-arabinose, and ribose were susceptible of analysis by this method with E. coli. Of additional interest is the analysis of the pathway of gluconate metabolism provided by these studies. Since cells adapted to gluconate were unable to utilize 2-ketogluconate, n-arabinose, or n-arabonate, we may conclude as a function of the postulates of simultaneous adaptation (3) that these substances as such were not intermediates in the degradation of gluconate.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Production of natural and rare pentoses using microorganisms and their enzymes

Biochemical methods, usually microbial or enzymatic, are suitable for the production of unnatural or rare monosaccharides. D-Arabitol was produced from Dglucose by fermentation with Candida famata R28. Dxylulose can also be produced from D-arabitol using Acetobacter aceti IFO 3281 and D-lyxose was produced enzymatically from D-xylulose using L-ribose isomerase (L-RI). Ribitol was oxidized to L-...

متن کامل

Nucleophilic substitution reactions of pyranose polytosylates.

The 2,3,4-tri-toluenesulfonate ester derivatives of the methyl pyranosides of l-arabinose, d-ribose, d-lyxose, and d-xylose have been prepared, and their substitution reactions with various nucleophiles have been examined. For arabinose, xylose, and ribose, highly regioselective monosubstitutions were observed with benzoate, nitrite, and azide anions. These reactions have led to short and simpl...

متن کامل

Metabolism of Pentoses and Pentitols by Aerobacter Aerogenes. I. Demonstration of Pentose Isomerase, Pentulokinase, and Pentitol Dehydrogenase Enzyme Families.

Mortlock, R. P. (Michigan State University, East Lansing) and W. A. Wood. Metabolism of pentoses and pentitols by Aerobacter aerogenes. I. Demonstration of pentose isomerase, pentulokinase, and pentitol dehydrogenase enzyme families. J. Bacteriol. 88:838-844. 1964.-Aerobacter aerogenes PRL-R3 is capable of utilizing as sole substrates for energy and growth seven of the eight aldopentoses and al...

متن کامل

Preparation of Nucleosides Derived from 2-Nitroimidazole and d-Arabinose, d-Ribose, and d-Galactose by the Vorbrüggen Method and Their Conversion to Potential Precursors for Tracers To Image Hypoxia

2-Nitroimidazole was silylated using hexaethyldisilazane and then reacted with 1-O-acetyl derivatives of D-arabinose, D-ribose, and D-galactose in acetonitrile at mild temperatures (-20 °C to rt), catalyzed by triethylsilyl triflate (Vorbrüggen conditions). The α-anomer was formed in the former case and the β-anomers in the latter two cases (highly) selectively. When D-arabinose and D-ribose we...

متن کامل

Molecular cloning and analysis of the ptsHI operon in Lactobacillus sake.

The ptsH and ptsI genes of Lactobacillus sake, encoding the general enzymes of the phosphoenolpyruvate: carbohydrate phosphotransferase system (PTS), were cloned and sequenced. HPr (88 amino acids), encoded by ptsH, and enzyme I (574 amino acids), encoded by ptsI, are homologous to the corresponding known enzymes of other bacteria. Nucleotide sequence and mRNA analysis showed that the two genes...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 188 2  شماره 

صفحات  -

تاریخ انتشار 1951