Maltose metabolism of Pseudomonas fluorescens
نویسندگان
چکیده
منابع مشابه
Carbohydrate Metabolism by Pseudomonas Fluorescens
MacGee and Doudoroff (2) have gained evidence in support of the postulated scheme by recovering the product of Reaction 1 as a crystalline trisodium salt and establishing its structure as Na3-2-keto-3-deoxy-6-phosphogluconate+2Hz0. Extracts of Pseudomonas Jluorescens catalyze the cleavage of 6-PG to pyruvate and triose phosphate at a rate 10 times faster than the rate of 6-PG dehydrogenase acti...
متن کاملPseudomonas fluorescens
nas incognita have been previously described as being able to utilize citronellol, geraniol, and linalool (3, 6). Recently, a 50-megadalton (MDa) plasmid has been associated with the degradation of geraniol (9). In this report we describe the isolation of a Pseudomonas fluorescens s train capable of utilizing linalool as a sole carbon and energy source and demonstrate the presence of a transmis...
متن کاملPlasmid Involvement in Linalool Metabolism by Pseudomonas fluorescens.
A bacterial strain was isolated from a wastewater lagoon and identified as Pseudomonas fluorescens. This isolate was able to utilize linalool as a sole carbon and energy source. The ability was found to be encoded on a 60-megadalton transmissible plasmid, pSRQ60. The plasmid was also mated into a commercial waste treatment strain, which expanded its ability to utilize other isoprenoid compounds.
متن کاملGlycine metabolism and anti-oxidative defence mechanisms in Pseudomonas fluorescens.
The role of metabolism in anti-oxidative defence is only now beginning to emerge. Here, we show that the nutritionally-versatile microbe, Pseudomonas fluorescens, reconfigures its metabolism in an effort to generate NADPH, ATP and glyoxylate in order to fend off oxidative stress. Glyoxylate was produced predominantly via the enhanced activities of glycine dehydrogenase-NADP(+) (GDH), glycine tr...
متن کاملThe kynureninase of Pseudomonas fluorescens.
Kotake and Nakayama (1) observed the conversion of kynurenine to anthranilic acid and alanine by a mammalian liver extract. Subsequently the enzyme responsible for this reaction in the mammal was partly purified (2,3) and the enzyme, prepared from vitamin Be-deficient animals, was shown to require pyridoxal phosphate for its maximal activity (2). During an investigation of tryptophan metabolism...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1975
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.124.1.262-268.1975