New chemical synthesis of 5′-phosphoribosyl-<i>N</i>-formylglycineamide

Chu, Samuel Y.; Henderson, J. Frank

doi:10.1139/v70-385

Cited by 10 publications

(7 citation statements)

References 2 publications

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“…Synthesis and NMR Characterization of FGAR. Several chemical syntheses of FGAR have been previously reported (Carrington, 1965;Chu & Henderson, 1970). We have used a modification of the procedure of Chu and Henderson to prepare FGAR and a variety of FGAR analogues.…”

Section: Resultsmentioning

confidence: 99%

Substrate specificity of formylglycinamidine synthetase

Schendel¹,

Stubbe²

1986

Biochemistry

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Formylglycinamidine ribonucleotide (FGAM) synthetase, which catalyzes the conversion of formylglycinamide ribonucleotide (FGAR), glutamine, and ATP to FGAM, ADP, glutamate, and Pi, has been purified to homogeneity (sp act. 0.20 mumol min-1 mg-1) from chicken liver by an alternative procedure to that of Buchanan et al. [Buchanan, J. M., Ohnoki, S., & Hong, B. S. (1978) Methods Enzymol. 51, 193-201] (sp act. 0.12 mumol min-1 mg-1). A variety of new analogues of formylglycinamide ribonucleotide have been prepared in which the formylglycinamide arm (R = CH2NHCHO) has been replaced by R = CH3, CH2OH, CH2Cl, CH2NH3, CH2NHCOCH3, CH2NHCOCH2Cl, CH2NHCO2CH2Ph, and L-CHC-H3NHCHO. These compounds have been characterized by 1H and 13C NMR spectroscopy. With compounds R = CH3, CH2OH, and CH2NHCOCH3 and ATP, in the presence or absence of glutamine, FGAM synthetase catalyzes the production of Pi at 4.5, 48, and 20%, respectively, the rate of production of Pi from formylglycinamide ribonucleotide. Only R = CH2NHCOCH3 causes glutaminase activity as well as ATPase activity and has been shown to be converted to the amidine analogue. Both FGAR (R = CH2NHCHO) and the FGAR analogue (R = CH2NHCHOCH3) in the presence of ATP and FGAM synthetase and in the absence of glutamine form a complex isolable by Sephadex G-50 chromatography. FGAM synthetase is thus highly specific for its formylglycine side chain. [18O]-beta-FGAR was prepared biosynthetically, and FGAM synthetase was shown by 31P NMR spectroscopy to catalyze the transfer of amide 18O to inorganic phosphate.

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Section: Resultsmentioning

confidence: 99%

Substrate specificity of formylglycinamidine synthetase

Schendel¹,

Stubbe²

1986

Biochemistry

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“…Malheureusement, la photodkgradation sous irradiation UV constitue un handicap majeur pour une large utilisation. Tout recemment, une famille de composks parents, les spirooxazines, connue depuis une vingtaine d'annees [I] [2] a subi un regain d'intkrst et a fait l'objet de nombreux brevets [3] et de quelques publications [4][5][6][7]. Ce type de composts prtsente une plus grande resistance a la photodkgradation [8] et laisse entrevoir des possibilitts d'utilisation concrete, dans le domaine des mattriaux 8 transmission variable notamment.…”

Section: Hv (Uv) Photomirocyanineunclassified

“…Dans les deux cas les cinetiques de dkcoloration thermique sont du type S ( t ) = A , .e--kl'' + A,.e-kz'r. SPO = spirooxazine; PM = photomkrocyanine(4) …”

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Effets de substituant, d'hétéroatome et de solvant sur les cinétiques de décoloration thermique et les spectres d'absorption de photomérocyanines en série spiro[indoline‐oxazine]

Pottier

Dubest

Guglielmetti

et al. 1990

Helvetica Chimica Acta

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Quantitative information useful for the development of new photochromic systems is obtained from the study of heteroatom and substituent effects on the thermal-bleaching kinetics and the absorption spectra of the photomerocyanines issued from spiro[indoline-oxazines]. The effect on photochromic properties of the presence of N-atoms either in the dimethine bridge or in the aromatic rings has been investigated through the comparison of spiro[indoline-naphthopyrans] C with spiro[indoline-naphthoxazines] A and with spiro[indoline-quinolinoxazines] B. Besides the occurrence of biexponential thermal-bleaching kinetics in non-polar solvents is observed: a tentative explanation for this observation is given which involves the formation, in either sequential or parallel steps, of energetically distinct stereoisomers of the opened form.

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“…Synthesis of fi-FGAM. FGAR (a mixture of anomers) was synthesized by a modification of the procedure of Chu and Henderson (1970) . FGAR was converted to FGAM by using FGAM synthetase purified from E. coli pJS80 according to the procedure of F. J. Schendel and J. Stubbe (unpublished results).…”

mentioning

confidence: 99%

Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli

Schrimsher¹,

Schendel²,

Stubbe³

et al. 1986

Biochemistry

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Aminoimidazole ribonucleotide (AIR) synthetase has been purified 15-fold to apparent homogeneity from Escherichia coli which contains a multicopy plasmid containing the purM, AIR synthetase, gene. The protein is a dimer composed of two identical subunits of Mr 38,500. The N-terminal sequence, amino acid composition, and steady-state kinetics of the protein have been determined. AIR synthetase has been shown to catalyze the transfer of the formyl oxygen of [18O]formylglycinamide ribonucleotide to Pi.

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New chemical synthesis of 5′-phosphoribosyl-N-formylglycineamide

Cited by 10 publications

References 2 publications

Substrate specificity of formylglycinamidine synthetase

Substrate specificity of formylglycinamidine synthetase

Effets de substituant, d'hétéroatome et de solvant sur les cinétiques de décoloration thermique et les spectres d'absorption de photomérocyanines en série spiro[indoline‐oxazine]

Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli

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