Enzymatic activities on purine and pyrimidine metabolism in nine mycoplasma species contaminating cell cultures

Hamet, M.; Bonissol, C; Cartier, P

doi:10.1016/0009-8981(80)90225-9

Cited by 39 publications

(14 citation statements)

References 9 publications

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“…In other words, all four preparations can synthesize adenosine, deoxyadenosine, inosine, deoxyinosine, guanosine, deoxyguanosine, uridine, or deoxyuridine from their respective nucleobases (adenine, hypoxanthine, guanine, and uracil) with either R-1-P or dR-1-P ( As reported by others (11,19,21), we also found uridine phosphorylase activity, i.e., the interconversion of uracil and R-1-P to uridine ( f This result was reassessed by the 10-fold enhancement assay procedure reported in Table 2. g This result was reassessed by fast-pressure liquid chromatography.…”

Section: Resultsmentioning

confidence: 58%

Synthesis of deoxyribomononucleotides in Mollicutes: dependence on deoxyribose-1-phosphate and PPi

McElwain¹,

Pollack²

1987

J Bacteriol

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Cell extracts of Acholeplasma laidlawii B-PG9, Acholeplasma morum S2, Mycoplasma capricolum 14, and Mycoplasma gallisepticum S6 were examined for 37 cytoplasmic enzyme activities involved in the salvage and biosynthesis of purines. All of these organisms had adenine phosphoribosyltransferase activity (EC 2.4.2.7) and hypoxanthine phosphoribosyltransferase activity (EC 2.4.2.8). All of these organisms had purine-nucleoside phosphorylase activity (EC 2.4.2.1) in the synthetic direction using ribose-1-phosphate (R-1-P) or deoxyribose-1-phosphate (dR-1-P); this activity generated ribonucleosides or deoxyribonucleosides, respectively. The pyrimidine nucleobase uracil could also be ribosylated by using either R-1-P or dR-i-P as a donor. The synthesis of deoxyribonucleosides from nucleobases and dR-1-P has been reported from only one other procaryote, Eschenichia coli (L. A. Mason and J. 0. Lampen, J. Biol. Chem. 193:539-547, 1951

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Section: Resultsmentioning

confidence: 58%

Synthesis of deoxyribomononucleotides in Mollicutes: dependence on deoxyribose-1-phosphate and PPi

McElwain¹,

Pollack²

1987

J Bacteriol

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“…Such nonspecific enzymes that hydrolyze dUTP and dCTP include nucleoside triphosphatase (1, 9), adenosine triphosphatase (8), and alkaline phosphatase (3). Both adenosine triphosphatase (6,16) and an alkaline phosphatase-like activity (12) have been reported in extracts of A . laidlawii.…”

Section: Methodsmentioning

confidence: 99%

Pyrimidine Deoxyribonucleotide Metabolism in Members of the Class Mollicutes

Williams

Pollack²

1985

International Journal of Systematic Bacteriology

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Cell extracts from six Acholeplasma species, six Mycoplasma species, and Spiroplasma Jlwicola 23-6T (T = type strain) were examined for enzyme activities of pyrimidine deoxyribonucleotide metabolism. A11 of these organisms had thymidine kinase and thymidine phosphorylase activities, and all lacked deoxycytidine triphosphatase activity. The 13 members of the Mollicutes were separated into three groups by the presence or absence of the following four enzyme activities: (i) the adenosine triphosphate-insensitive deoxyuridine triphosphate-specific hydrolyzing deoxyuridine triphosphatase, (ii) a deoxyuridine monophosphate phosphatase, (iii) deoxycytidine deaminase, and (iv) deoxycytidine monophosphate deaminase. Five of the six Acholeplasma species (all Acholeplasma species except Acholeplasma florum LIT) had all four enzymatic activities. The six Mycoplasma species only had the deoxycytidine and deoxycytidine monophosphate deaminase activities. The only two plant isolates studied, A . Jlorum LIT and S . Jloricola 23-6T, lacked all four enzymatic activities.The class Mollicutes contains two orders. The order Mycoplasmatales is composed of two families, the Mycoplasmataceae, which has two genera (Mycoplasma and Ureaplasma), and the Spiroplasmataceae, which has o n e genus ( S p i r o p l a s m a ) (4). The second order, A c h o l e p l a s m a t a l e s , c o n t a i n s o n e f a m i l y , t h e Achdeplasmataceae, with one genus, Acholeplasma (5). A number of biochemical, nutritional, and morphological characteristics have been used to distinguish these genera and families. They include sterol requirement for growth, genome sizes, ability to hydrolyze urea, localization of reduced nicotinamide adenine dinucleotide oxidase, and presence of helical forms during growth (4, 5). However, no one has distinguished genera or families of the Mollicutes by the presence or absence of enzymes involved in pyrimidine deoxyribonucleotide metabolism.Recently, we characterized the adenosine triphosphate (ATP)-insensitive highly specific deoxyuridine triphosphate ( d U T P ) -h y d r 01 y zi ng d e o x y uri d i n e t r i p h o s p h a t e nucleotidohydrolase (dUTPase; EC 3.6.1.23) from Acholeplasma laidlawii B-PG9 (17). In the present study, we examined five other Acholeplasma species, six Mycoplasma species, and one Spiroplasma species for dUTPase and o t h e r e n z y m e a c t i v i t i e s involved in pyrimidine deoxyribonucleotide metabolism. Our data suggest that it may be possible, with one exception, to distinguish these genera based upon the presence or absence of the ATP-insensitive dUTP-specific dUTPase (17), deoxyuridine monophosphate (dUMP) phosphatase, deoxycytidine (dC) deaminase, and deoxycytidine monophosphate (dCMP) deaminase activities in cell extracts. (56.6 Ci/mmol) were purchased from Amersham Corp., Arlington Heights, Ill. Polyethyleneimine-cellulose thinlayer chromatography plates were purchased from Analtech, Newark, Del. MATERIALS AND METHODSOrganisms. Acholeplasma florum LIT (T = type strain) and Spiroplasm...

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“…Also, there are reports of nucleotidase activity detection towards some (d)NMPs but not others, indicating different substrate specificities (Tryon and Pollack, 1985). Proudfoot et al (2004) identified three uncharacterized E. coli proteins containing nucleotidase activity, SurE, YfbR, and YjjG, which exhibit different substrate Bizarro and Schuck 195 Hamet et al, 1980. 8 Cocks et al, 1988.…”

Section: Purine and Pyrimidine Nucleotide Pathways In Mollicutesmentioning

confidence: 99%

Purine and pyrimidine nucleotide metabolism in Mollicutes

Bizarro

Schuck

2007

Genet. Mol. Biol.

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Several mollicute genome projects are underway, offering unique opportunities to study genes and metabolic pathways on a genome-wide scale. Here, we have analyzed the conservation and diversity of purine and pyrimidine metabolism in mycoplasmas. An evaluation of discrepancies between genomic analysis and enzymatic data revealed interesting aspects about these organisms. We found important examples in which enzyme activity was reported without the annotation of a corresponding gene. An interesting example concerns phosphopentomutase. In Mollicutes, we have identified CDSs orthologous to sequences recently identified as new phosphopentomutases in archaeobacteria that are structurally related to phosphomannomutases. It is suggested that these sequences could replace the function of phosphopentomutases in mollicutes lacking the canonical phosphopentomutase gene (deoB). Also, the activity of 5'-nucleotidase was reported in mollicutes that do not possess any CDS related to ushA. Hypothetical proteins exhibiting domains similar to newly characterized 5' nucleotidases in Escherichia coli are proposed as possible CDSs related to this enzymatic activity in Mollicutes. Based on our analysis, the reductive genome evolution of Mollicutes does not appear to result in a minimum set of genes nor a minimum set of metabolic functions shared by all mollicute species.

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Enzymatic activities on purine and pyrimidine metabolism in nine mycoplasma species contaminating cell cultures

Cited by 39 publications

References 9 publications

Synthesis of deoxyribomononucleotides in Mollicutes: dependence on deoxyribose-1-phosphate and PPi

Synthesis of deoxyribomononucleotides in Mollicutes: dependence on deoxyribose-1-phosphate and PPi

Pyrimidine Deoxyribonucleotide Metabolism in Members of the Class Mollicutes

Purine and pyrimidine nucleotide metabolism in Mollicutes

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