Action of hydrogen fluoride on nucleotides and other esters of phosphorus(V) acids

Lipkin, David; Phillips, Bruce E.; Abrell, John W.

doi:10.1021/jo01258a003

Cited by 57 publications

(24 citation statements)

References 5 publications

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“…Purified trypsinized cell walls were prepared from S. simulans 22 and M. luteus as previously described (25). Teichoic acids were extracted by hydrolysis with 70% HF for 3 h at 0°C (13). HF was neutralized by addition of 6 N KOH, and the cell walls were extensively washed with distilled water.…”

Section: Methodsmentioning

confidence: 99%

Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase

1987

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Pep 5 and nisin are cationic peptide antibiotics which in addition to their membrane-disruptive action induce autolysis in staphylococci. To investigate the mechanism of lysis induction, the influence of the peptides on the activity of the N-acetylmuramoyl-L-alanine amidase of Staphylococcus simulans 22 was studied. In experiments with isolated cell walls at low ionic strength, the amidase activity was stimulated by the addition of Pep 5 and nisin, as well as by polylysine, streptomycin, and mono-and divalent cations. The concentrations necessary for activation depended on the nature of the cation and rahged from 5 ,uM for poly-L-lysine (n = 17) to 150 mM for Na+ at a cell wail concentration of 100 ,ug of cell wails per ml. No effect was observed if the cell walls were devoid of polyanionic constituents. Kinetic data suggested that the amidase bound to the teichoic and teichuronic acids of the cell wall and was thereby inhibited. Cationic molecules reversed this inhibition, most likely by displacing the enzyme from the polyanions. If the concentrations of the larger peptides were high in relation to cell wall concentration, the activation turned into inhibition, presumably by interfering with the access of the enzyme to its substrate. These experiments demonstrate that the activity of the amidase is modulated by basic peptides in vitro and help to explain how Pep 5 and nisin may cause lysis of treated cells.

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Section: Methodsmentioning

confidence: 99%

Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase

1987

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“…These mineral acids are employed at higher temperatures and simultaneously remove N-acetyl groups thus stabilizing any remaining unhydrolysed glycosidic bonds (1 1). By contrast aqueous HF is a very mild hydrolytic reagent and does not break N-acyl bonds (1). A further structural feature associated with an increase in the rate of hydrolysis of Zacetamidohexapyranosides was elucidated by experiments on methyl 2-acetamido-2-deoxy-a-and P-D-mannopyranosides ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Aqueous hydrofluoric acid is an extremely specific reagent for the low-temperature cleavage of different types of phosphate esters (1). The specificity is such that it has been used to remove phosphate esters from complex oligosaccharides without cleaving its 0-glycosidic linkages (2).…”

Section: Introductionmentioning

confidence: 99%

Facile cleavage of some 2-acetamido-2-deoxy-β-D-gluco- and galactopyranosides using aqueous HF

Jennings¹,

Ługowski²

1980

Can. J. Chem.

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This paper is dedicated to Prof. Raymond U . Lemieux on the occasion of his 60th birrhday HAROLD J. JENNINGS and CZESLAW LUGOWSKI. Can. J. Chem. 58;2610 (1980. Treatment of pneumococcal C-substance (PnC) with 48% aqueous H F resulted in not only the intended removal of all the phosphate esters but also in the highly specific hydrolysis of the glycosidic bond between the 2-acetamido-2-deoxy-P-D-galactopyranose and ribitol residues. Some of the structural features associated with this facile hydrolysis were elucidated from studies on the treatment of model methyl glycosides and oligosaccharides with the same reagent. These studies indicate that an increase in the rate of hydrolysis is associated with glycosides of 2-acetamidohexapyranoses having a trans diequatorial disposition of the aglycon and 2-acetamido groups. These studies also indicate that the nature of the aglycon is also a contributing factor, because although simple alkoxy and terminal open-chainglycitols are readily cleaved fromglycosides satisfying the above criteria, hydrolysis does not occur where the aglycon is another cyclized sugar moiety. Thus chitotriose can only be degraded to chitobiose using this reagent following the reduction of its terminal reducing moiety. HAROLD J. JENNINGS et CZESLAW LUGOWSKI. Can. J. Chem. 58,2610Chem. 58, (1980. L'action d'une solution aqueuse a 48% de H F sur la substance pneumocoque C (PnC) n'enlke pas seulement tous les groupements esters phosphoriques mais hydrolyse egalement de f a~o n fortement specifique la liaison glycosidique entre les unitCs acetamido-2 deoxy-2 P-D-galactopyrannose et le ribitol. On a Cclairci quelques aspects structuraux associes a cette hydrolyse facile, en se basant sur les etudes rCalisCes en traitant des modeles de glycosides de mkthyle et d'oligosaccharides avec le mime reactif. Ces Ctudes indiquent qu'une augmentation de la vitesse d'hydrolyse se produit avec les glycosides d'acetamido-2 hexapyrannoses ayant les groupements aglycone et acetamido-2 en position trans diequatoriale. Ces etudes indiquent egalement que par sa nature I'unite aglycone est un facteur contributif, parce que les groupes alkoxy simples et glycitols terminaux a chaine ouverte sont facilement enleves selon les criteres ci-dessus mentionnes. L'hydrolyse ne se produit pas quand I'unite aglycone est un noyau de sucre cyclique. Ainsi I'emploi de ce reactif sur le chitotriose suivi de la reduction de son unite terminale permet seulement deladegrader en chitobiose.[Traduit par le journal]

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“…Purified trypsinized cell walls were prepared from M. luteus and S. aureus NMSCC 133 as previously described (21). Teichoic acids were extracted by hydrolysis with 70% HF for 3 h at 0°C (16). HF was neutralized by addition of 6 N KOH, and the cell walls were washed 10 times with distilled water.…”

Section: Methodsmentioning

confidence: 99%

Purification and Partial Characterization of a Murein Hydrolase, Millericin B, Produced by Streptococcus milleri NMSCC 061

Beukes

Bierbaum

Sahl

et al. 2000

Appl Environ Microbiol

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Streptococcus milleri NMSCC 061 was screened for antimicrobial substances and shown to produce a bacteriolytic cell wall hydrolase, termed millericin B. The enzyme was purified to homogeneity by a four-step purification procedure that consisted of ammonium sulfate precipitation followed by gel filtration, ultrafiltration, and ion-exchange chromatography. The yield following ion-exchange chromatography was 6.4%, with a greater-than-2,000-fold increase in specific activity. The molecular weight of the enzyme was 28,924 as determined by electrospray mass spectrometry. The amino acid sequences of both the N terminus of the enzyme (NH 2 SENDFSLAMVSN) and an internal fragment which was generated by cyanogen bromide cleavage (NH 2 SIQTNAPWGL) were determined by automated Edman degradation. Millericin B displayed a broad spectrum of activity against gram-positive bacteria but was not active against Bacillus subtilis W23 or Escherichia coli ATCC 486 or against the producer strain itself. N-Dinitrophenyl derivatization and hydrazine hydrolysis of free amino and free carboxyl groups liberated from peptidoglycan digested with millericin B followed by thin-layer chromatography showed millericin B to be an endopeptidase with multiple activities. It cleaves the stem peptide at the N terminus of glutamic acid as well as the N terminus of the last residue in the interpeptide cross-link of susceptible strains.Most eubacteria are mechanically stabilized by the shapedetermining peptidoglycan, which consists of polysaccharide chains that are connected by short peptides. Expansion of the bacterial cell wall during growth and splitting of the septum prior to cell separation require enzymes that cleave some of the existing covalent bonds within the peptidoglycan sacculus. These enzymes are collectively known as peptidoglycan hydrolases (24). Some have been characterized as N-acetylmuramidases, N-acetylglucosaminidases, N-acetylmuramyl-L-alanine amidases, endopeptidases, and transglycosidases (10). Most peptidoglycan hydrolases have been characterized as bacteriolytic enzymes by in vitro studies (29). Lysostaphin, which is active against Staphylococcus aureus, is one such enzyme. It has been suggested that lysostaphin may function catabolically to release nutrients from other staphylococci in the environment, with the producer cell being protected by a specific immunity protein (12,18). The lytic effect of lysostaphin results from a direct attack on the integrity of the staphylococcal cell wall, specifically bringing about cleavage of the pentaglycine crosslink between the stem peptides of individual peptidoglycan subunits (4).Zoocin A, a bacteriolytic cell wall hydrolase produced by Streptococcus zooepidemicus 4881, like lysostaphin, cleaves bonds within the peptide moiety of peptidoglycan (26). Zoocin A has been shown to inhibit the growth of all Streptococcus pyogenes strains and all S. zooepidemicus strains other than 4881 itself (14). Both enzymes, lysostaphin and zoocin A, possess a catalytic domain in the N-terminal portion and a...

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Action of hydrogen fluoride on nucleotides and other esters of phosphorus(V) acids

Cited by 57 publications

References 5 publications

Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase

Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase

Facile cleavage of some 2-acetamido-2-deoxy-β-D-gluco- and galactopyranosides using aqueous HF

Purification and Partial Characterization of a Murein Hydrolase, Millericin B, Produced by Streptococcus milleri NMSCC 061

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