Partial purification and properties of a β-<i>N</i>-acetylglucosaminidase from the fungus <i>Sclerotinia fructigena</i>

Reyes, Fuensanta; Byrde, R. J. W.

doi:10.1042/bj1310381

Cited by 72 publications

(21 citation statements)

References 25 publications

(18 reference statements)

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“…The influence of the molar ratio sucrose:vinyl laurate was Fungi were grown at 25°C in stationary culture in 1-L conical flasks with 200 mL of medium as described by Reyes and Byrde (1973); 20-days-old autolyzed cultures were taken, filtered, concentrated, dialyzed, and freeze-dried.…”

Section: Resultsmentioning

confidence: 99%

Lipase-catalyzed regioselective acylation of sucrose in two-solvent mixtures

Ferrer

Cruces

Bernabé

et al. 1999

Biotechnol. Bioeng.

145

114

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Section: Resultsmentioning

confidence: 99%

Lipase-catalyzed regioselective acylation of sucrose in two-solvent mixtures

Ferrer

Cruces

Bernabé

et al. 1999

Biotechnol. Bioeng.

145

114

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“…With the M . rouxii enzyme, as compared with other fungal p-GlcNAc'ases, the efficiency of 1 was outstanding, the Ki value being 10-50 times lower [8, 9,221. The simple lactone oxime 2 was found to be a new 8-GlcNAc'ase inhibitor (Table l), although it attained only about 0.4-0.7 times the potency of the lactone 1 itself.…”

Section: Discussionmentioning

confidence: 99%

N‐Acetylgucosaminono‐1,5‐lactone oxime and the corresponding (phenylcarbamoyl)oxime

Horsch

Hoesch

Vasella

et al. 1991

European Journal of Biochemistry

150

108

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Using N-acetylglucosaminono-I ,5-lactone (1) as the reference, the inhibitory activity of its (formal) derivatives N-acetylglucosaminono-1,5-lactone oxime (2) and N-acetylglucosaminono-1,5-lactone 0-(phenylcarbamoy1)-oxime (3) was tested against P-N-acetylglucosaminidase of different origins (animal, plant, fungus). Displaying inhibition constants of 0.45 pM and 0.62 pM, for the animal and plant enzyme, respectively, the simple oxime 2 was about equally potent as the parent lactone 1, and 50-400 times more efficient than two recently described new P-N-acetylglucosaminidase inhibitors. The (phenylcarbamoy1)oxime 3 performed even better, particularly with the fungal enzyme (Ki = 40 nM), i.e. was about 350 times more potent than the lactone. In all cases competitive inhibition was observed with 4-nitrophenyl-~-N-acetylglucosaminide as the substrate. With K J K , ratios up to 3300 for 2 and 13600 for 3, the mode of action of these novel inhibitors is probably that of transition state mimicry. Suggestions are made for their use as a tool in biological research.Aldono-l,5-lactones are well known potent competitive inhibitors of glycosidases acting on substrates of the corresponding configuration [l, 21. In particular, this relates to the inhibition of P-N-acetylglucosaminidase (P-GlcNAc'ase; EC 3.2.1.30) by N-acetylglucosaminono-1,5-lactone (1; see Fig. 1) [3], although with values ranging over 0.8-660 pM [4-91 inhibitor constants display considerable variation. Such lactones are thought to adopt a conformation similar to that of a glycopyranosyl cation and to be effective as transitionstate approximates [lo] (for current views of the theory of transition state affinity and the design of enzyme inhibitors, see 11 1, 121).As glucono-l,5-lactone oxime and its phenylcarbamoyl derivative were found to be about equal or even better inhibitors of P-glucosidase than the parent lactone [ 131, investigations into the effect of the corresponding N-acetylglucosamine derivatives 2 and 3 on p-GlcNAc'ase seemed promising. In addition, to estimate the extent to which the source of the P-GlcNAc'ase might have a bearing on its susceptibility to inhibition, experiments were performed with enzymes of widely different organisms. A preliminary account of part of this work has been published [14]. Abbreviations. 4-Np-GlcNAc, 4-nitrophenyl-~-N-acetylglucosaminide; P-GlcNAc'ase, P-N-acetylglucosaminidase. MATERIALS AND METHODS SourcesEnzyme. P-N-Acetylglucosaminidase (EC 3.2.1.30).Chemical Co.), but the enzyme preparation from Mucor rouxii was obtained in this laboratory as follows. Log-phase hyphae of the fungus were cultivated [15] and the cells washed thoroughly with 20 mM Bistris pH 6.5, drained, and disrupted with glass beads (0.5 mm) in an MSK homogenizer (Braun, Melsungen) for 60 s at 4000 rpm. After removal of the beads, followed by centrifugation at 4000 x g for 5 min, and then at 54 500 x g for 45 min, the supernatant ( z 70 ml) was subjected to anion-exchange chromatography, using a column of DEAE-Sephadex A-25 (d 50 x 150 mm) and...

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“…In the entomopathogenic fungus Beauveria bassiana, the enzyme was induced with GlcNAc, but it was repressed in the presence of glucose and NH 4 NO 3 and was partially repressed when glucose or NH 4 NO 3 was added . N-acetylglucosaminidase plays an important role in the autolysis of filamentous fungi such as Sclerotinia fructigena (Reyes and Byrde 1973), Neurospora crassa (Reyes et al 1981) and Aspergillus niger (Lahoz et al 1976). Although autolysis of C. albicans is rare and the chitin content of cell walls is low (Sullivan et al 1983), the Nacetylglucosaminidase may be involved in the chitin turnover of C. albicans cell walls during growth by degrading chitin oligomers Molloy et al 1994).…”

Section: Fig 2 A-d Growth and N-acetylglucosaminidase Activity Inmentioning

confidence: 99%

Regulation of N -acetylglucosaminidase production in Candida albicans

Niimi

Shepherd

et al. 1997

Archives of Microbiology

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The N-acetylglucosaminidase of Candida albicans is a secreted hydrolytic enzyme that contributes to the yeast's virulence. There was a significant increase in the N-acetylglucosaminidase activity of C. albicans cells released from carbon starvation in medium containing N-acetylglucosamine. The increased enzyme activity in N-acetylglucosamine-grown cells correlated with increased transcription of the HEX1 gene, which encodes C. albicans N-acetylglucosaminidase. In contrast, glucose repressed HEX1 transcription, and glucose-grown cells had on average 94-fold lower N-acetylglucosaminidase activities than did N-acetylglucosamine-grown cells. N-acetylglucosaminidase induction in cells grown on N-acetylglucosamine was also repressed by fructose, mannose or galactose, although to a lesser extent than by glucose, and sucrose repressed enzyme production by only 10%. Eighty-eight percent of the enzyme in N-acetylglucosamine-grown cells was localised in the periplasm, and after incubation for 5 h, 30 or 70% of the total enzyme activity was secreted into the medium by yeast or mycelial cells, respectively. The cellular location of the enzyme and the regulation of production by the carbon source indicate a scavenging role for C. albicans N-acetylglucosaminidase.

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Partial purification and properties of a β-N-acetylglucosaminidase from the fungus Sclerotinia fructigena

Cited by 72 publications

References 25 publications

Lipase-catalyzed regioselective acylation of sucrose in two-solvent mixtures

Lipase-catalyzed regioselective acylation of sucrose in two-solvent mixtures

N‐Acetylgucosaminono‐1,5‐lactone oxime and the corresponding (phenylcarbamoyl)oxime

Regulation of N -acetylglucosaminidase production in Candida albicans

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