The cyclic phosphodiesterases (3'-nucleotidases) of the Enterobacteriaceae

Neu, Harold C.

doi:10.1021/bi00850a060

Cited by 31 publications

(17 citation statements)

References 12 publications

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“…Moreover, the E. coil enzyme is activated by heating at 55° in the presence of Cot +, whereas the B. subtilis var. amyloliquefacus enzyme is partially inactivated due to the same treatment, as was also found for the enzymes from Vibrio alginol yticus (3,4), Proteus mirabilis (5, 6) and other Enterobacteriaceae (7,8).…”

Section: Discussionsupporting

confidence: 67%

See 1 more Smart Citation

Purification and some properties of 2', 3'-cyclic phosphodiesterase from the cell-free extract of Bacillus subtilis var. amyloliquefacus.

Seki

Fukuda

1981

J. Gen. Appl. Microbiol.

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A ribonucleoside 2',3'-cyclic phosphodiesterase (cyclic phosphodiesterase) having 3'-nucleotidase activity was purified from the cell-free extract of Bacillus subtilis var. amyloliquefacus, and its enzymatic properties were examined. The molecular weight was approximately 74,000. The enzyme was highly specific for ribonucleoside 2',3'-cyclic monophosphate (2',3'-cyclic mononucleotide), and ribonucleoside 3'-monophosphate (3'-mononucleotide), and also hydrolyzed bis p-nitrophenyl phosphate (bis p-NPP) but at a rate much slower than that of 3'-mononucleotide. Both cyclic phosphodiesterase and 3'-nucleotidase activities had an optimum pH of about 6.7, and phosphodiesterase activity against bis p-NPP indicated a relatively sharp pH optimum at 5.0. Only phosphodiesterase activity against bis p-NPP was greatly activated by Co2~, but both cyclic phosphodiesterase and 3'-nucleotidase activities were inhibited. However, Co2+ had an effect of protecting the enzyme against heat inactivation. 3'-Nucleotidase activity was not affected by EDTA, while phosphodiesterase activities against both 2',3'-cyclic mononucleotide and bis p-NPP were greatly inhibited. The enzyme hydrolyzed 3'-AMP with Km 0.046 mM and Vmax 1,585 µmol per hr per mg protein, bisp-NPP with Km 0.16 mM and Vn,a. 233 ,umol per hr per mg protein.In the course of studies on the physiological changes occurring after infection of Bacillus subtilis var. amyloliquefacus with phage, we became aware that a phosphodiesterase activity hydrolyzing bis p-nitrophenyl phosphate (bis p-NPP) under the acidic pH region (an optimal pH of about 5.0) exists in the phage uninfected cell-free extract, and that this activity did not change after infection of host cell with phage.In a preliminary experiment, attempts were made to characterize the substrate specificity using the enzyme partially purified by DEAF-cellulose chromatography. 487

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Section: Discussionsupporting

confidence: 67%

“…Similar enzymes have subsequently been purified from various microorganisms (3)(4)(5)(6)(7)(8)(9). The enzymes from all those organisms are strikingly similar, but do have a few distinctly different properties.…”

mentioning

confidence: 99%

Purification and some properties of 2', 3'-cyclic phosphodiesterase from the cell-free extract of Bacillus subtilis var. amyloliquefacus.

Seki

Fukuda

1981

J. Gen. Appl. Microbiol.

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“…Our results (Tables 2-4) confirm and extend her observations. Furthermore, the substrate specificity of the V. Jischeri enzyme ( Table 5 ) clearly distinguishes it from periplasmic ribonucleoside 2' : 3'-CAMP phosphodiesterases produced by many bacteria (Anraku, 1964a, b ;Neu, 1968;Beacham et al, 1973Beacham et al, , 1977Beacham & Garrett, 1980;Uerkvitz & Beck, 198 1 ;Anderson et al, 1985). V.Jischeri could produce a cytoplasmic cAMP phosphodiesterase similar in activity to that of other bacteria; this issue was not addressed in the present study.…”

Section: Discussionmentioning

confidence: 99%

“…thereby supplementing the cellular regulatory pool of this nucleotide (Ammerman & Azam, 1982, 1987. Environmental levels of CAMP, however, are apparently too low to support bacterial growth, and the bacterial cytoplasmic membrane is in most cases highly impermeable to nucleotides (Neuhard & Nygaard, 1987).…”

Section: P V Dunlap and Othersmentioning

confidence: 99%

Growth of the marine luminous bacterium Vibrio fischeri on 3':5'-cyclic AMP: correlation with a periplasmic 3':5'-cyclic AMP phosphodiesterase

Dunlap¹,

Muêller²,

Lisa³

et al. 1992

Journal of General Microbiology

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The marine luminous bacterium Vibrio jischeri, the species-specific light-organ symbiont of monocentrid (pinecone) fish, grew on 3':5'-cyclic adenosine monophosphate (CAMP) as a sole source of carbon and energy, a capability not previously described in bacteria. In a minimal, chemically defined medium containing cAMP as the sole source of carbon and energy, V.jischeri cells grew more slowly than on glucose or ribose, but as quickly as on 5'-AMP. Expression of luminescence, which is dependent on cAMP in V.jischeri, was stimulated in cells grown on cAMP compared to cells grown on glucose or ribose. All strains of Kjischeri tested (MJ-I, B-61, ATCC 7744, MJ-A1, CG-A1) grew on CAMP, as did strains of two other marine luminous bacteria, V. fogei and Photobacterium phosphoreum, and strains of the terrestrial enteric bacterium Serratia marcescescens. Other tested species of marine luminous bacteria (P. feiognathi, Shewaneffa [ Afteromonas] hamhi, V. hmeyi, V. orientalis, V. splendidus) and terrestrial enteric bacteria (Escherichia cofi, Salmonella typhimurium), which grew on 5'-AMP or ribose, did not grow on CAMP. Assays on intact cells and periplasmic extracts revealed that V.jischeri MJ-1 produced a periplasmic 3': 5'-CAMP phosphodiesterase (CAMP phosphodiesterase) of very high specific activity 19.0 p o l phosphate released (mg protein)-' min-l ] and narrow substrate specificity (3': 5'-CAMP and 3': 5'-cGMP were attacked). The novel periplasmic location and unusually high activity of cAMP phosphodiesterase appear to account for the ability of this species to grow on CAMP. The periplasmic cAMP phosphodiesterase of Kjischeri might play a role in degrading free cAMP in seawater or in a CAMP-mediated aspect of the light organ symbiosis with monocentrid fish.

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“…Deoxyribonuclease (DNase), ribonuclease (RNase), lecithinase, lipase, protease and haemolytic activity were assayed on DNA-, RNA-, egg yolk-, casein-and blood-agar plates [ 191. 3'-and 5'-nucleotidase (uridine diphosphate-sugarhydrolase) were assayed on adenosine-5'-and 3'-monophosphate in a Tris-maleate buffer [20,21] . fig.1 B the separation of extracellular LT found in the culture fluid.…”

Section: Methodsmentioning

confidence: 99%