Genetic and Biochemical Studies on 5′-Nucleotide Fermentation

Momose, Haruo; Shiio, Isamu

doi:10.2323/jgam.15.399

Cited by 14 publications

(5 citation statements)

References 7 publications

(7 reference statements)

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“…A substantial number of gram-positive bacteria also have truly surface-bound enzymes (3,4,20,25,28,37). The nuclease of Bacillus subtilis is partially exocellular (28) and the cell-bound enzyme is released during protoplasting of the cells (1, 25).…”

Section: Discussionmentioning

confidence: 99%

Localization of Cell-bound Penicillinase in Bacillus licheniformis

1968

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When protoplasts are prepared from Bacillus licheniformis (strain 749/C, constitutive for penicillinase), approximately 60% of the cell-bound penicillinase is released. The remainder is retained by the protoplast and cannot be removed by washing. This release is specific, in that less than 7% of the cellular reduced nicotinamide adenine dinucleotide (NADH) dehydrogenase and a-glucosidase is liberated by the treatment. The freed penicillinase is excluded from G-200 Sephadex, and it is partially sedimented with a force of 65,000 X g for 20 hr. It is probably attached to characteristic tubular and vesicular structures with single-layered membranes that are comparable to structures previously described in intact penicillinaseforming cells. The specific activity of the organelle is more than six times that of twice washed peripheral membrane; furthermore, about 8% of the protein of the structure is penicillinase. At substrate concentrations (benzylpenicillin) of about onefifth the Km value, whole cells show a slight permeability restriction, although this does not occur in isolated particles and protoplasts.

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Section: Discussionmentioning

confidence: 99%

Localization of Cell-bound Penicillinase in Bacillus licheniformis

1968

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“…However, we have been unable to find nucleotidases excreted into the growth medium of B. subtilis, S. aureus, or M. lysodeikticus species. There is a 5'-nucleotidase in B. subtilis (5,15), but it is not released by any osmotic transition or by KCI elution techniques (unpublished data), which do elute the acid phosphatases of S. aureus (14). If these nucleotidases are concerned with the turnover of nucleotides in the cell wall as an alternative to feedback inhibition, this may explain the differences between the gram-negative and gram-positive organisms.…”

Section: Discussionmentioning

confidence: 99%

The 5′-Nucleotidases and Cyclic Phosphodiesterases (3′-Nucleotidases) of the Enterobacteriaceae

Neu

1968

J Bacteriol

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All members of the Enterobacteriaceae possess distinct 5'-nucleotidases and cyclic phosphodiesterases (3'-nucleotidases) that can be differentiated from the acid and alkaline phosphatases and the acid sugar hydrolases. The nucleotidases and cyclic phosphodiestei ases of the various Enterobacteriaceae are remarkably similar in properties. All of the 5'-nucleotidases hydrolyze 5'-nucleotides, adenosine triphosphate, and uridine diphosphoglucose. Their pH optimum is from 5.7 to 6.1. The cyclic phosphodiesterases hydrolyze 3'-nucleotides, cyclic phosphonucleotides, bis-(p-nitrophenyl)phosphate, and p-nitrophenylphosphate. Their pH optimum is from 7.2 to 7.8. For both enzymes, cobalt showed optimal metal stimulation. An intracellular protein inhibitor for the 5'-nucleotidase is present in all of the Enterobacteriaceae. No inhibitor of cyclic phosphodiesterase activity exists, although hydrolysis of both cyclic phosphonucleotides and 3'-nucleotides is inhibited by ribonucleic acid. Neither of the enzymes is subject to control by phosphate level or by catabolite repression. Of the other bacteria studied, only Haemophilus and Bacillus subtilis contained significant 3'or 5'-nucleotidase activity.

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“…[1][2][3][4][5] We have also already reported that we derived methionine sulfoxide resistant mutants from an inosineproducing strain of Bacillus subtilis, and obtained a mutant AG 169 that did not excrete inosine but produced considerable amounts of xanthosine and guanosine. 6 ) But this mutant could not accumulate a sufficient amount of guanosine to be contented.…”

Section: Production Of Guanosine By Psicofuranine and Decoyinine Resimentioning

confidence: 93%