Growth of Aerobacter aerogenes on D-arabinose and L-xylose.
نویسندگان
چکیده
Aerobacter aerogenes is noted for its versatility in being capable of growth by utilizing many of the rare and unnatural carbohydrates as substrates. The mechanism of growth on several of these unnatural carbohydrates has been previously reported. A. aerogenes PRL-R3 possesses the ability to synthesize, in response to the common substrate ribitol, a ribitol dehydrogenase which will also catalyze the oxidation of the rare pentitols xylitol and L-arabitol, but high enzyme concentrations are required before a significant rate of metabolism of these latter two pentitols can occur. Xylitol and L-arabitol are not inducers of the enzyme, and growth with these pentitols as substrates is due to the selection of mutants derepressed for ribitol dehydrogenase (Mortlock, Fossitt, and Wood., Bacteriol. Proc., p. 95, 1964). A mutation for the synthesis of a new or specific pentitol dehydrogenase is not required to permit growth on these unnatural pentitols, even though it is unlikely that the organism has previously encountered these substrates in nature. It has been postulated that growth on the rare aldopentose L-xylose occurs by a similar mechanism with the utilization of D-arabinose isomerase for the isomerization of L-xylOse to L-xylulose (Mortlock et al., Bacteriol. Proc., p. 95, 1964).
منابع مشابه
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 کاملRegulation of pentitol metabolism by Aerobacter aerogenes. I. Coordinate control of ribitol dehydrogenase and D-ribulokinase activities.
Induction studies on Aerobacter aerogenes strain PRL-R3, using ribitol as the inducer-substrate, indicated that two enzymes of ribitol catabolism, ribitol dehydrogenase and d-ribulokinase, are coordinately induced. The utilization of d-arabinose as a substrate resulted in the induction of ribitol dehydrogenase as well as d-ribulokinase. Mutants which were constitutive for ribitol dehydrogenase ...
متن کاملPathway of L-xylose and L-lyxose degradation in Aerobacter aerogenes.
Pen&e utilization in Aerobacter aerogenes has been shown from fermentation studies with Cl%beled pentoses (1, 2) and with cell extracts (3) to involve the conversion of the pentose to n-xylulose 5-phosphate, which is further metabolized via n-sedoheptulose 7-phosphate, n-fructose 6-phosphate, and intermediates of the Embden-Meyerhof pathway. Although Aerobacter aerogenes can grow on all eight o...
متن کاملMetabolism of D-arabinose by Aerobacter aerogenes: purification of the isomerase.
In Aerobacter aerogenes, the mutational event permitting the utilization of d-arabinose as a source of carbon and energy is a regulatory mutation resulting in the constitutive synthesis of certain enzymes of the l-fucose catabolic pathway. l-Fucose isomerase catalyzes the isomerization of d-arabinose to d-ribulose. This enzyme was purified to homogeneity as indicated by a single band in disc-ge...
متن کاملPurification and properties of L-xylulokinase.
Previously evidence was presented for the existence of a new enzyme, L-xylulokinase, which is instrumental in the degradation of L-xylulose by Aerobacter aerogenes (1). This enzyme is of interest because it initiates a pathway for the metabolism of L-xylulose which is different from that known to occur in mammals (2). This paper describes the purification and properties of Lxylulokinase from L-...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 90 4 شماره
صفحات -
تاریخ انتشار 1965