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Gene Review:

RHE_PD00043 - beta-glucosidase

Rhizobium etli CFN 42

Estruch, J.J. et al., Namchuk, M.N. et al., Wrodnigg, T.M. et al., Tull, D. et al., Kim, Y.W. et al., et al.

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Disease relevance of RHE_PD00043

The rolB gene of Agrobacterium rhizogenes, whose expression stimulates the formation of roots by transformed plant tissues and other growth alterations in transgenic plants, codes for a beta-glucosidase able to hydrolyse indole-beta-glucosides [1].
Furthermore, beta-glucosidase activity present in E. coli extracts expressing the rolC protein was inhibited by affinity-purified antibodies specific for the rolC protein [2].
The beta-glucosidase from Agrobacterium faecalis (previously Alcaligenes faecalis) has been subjected to a detailed kinetic investigation with a range of substrates to probe its specificity and mechanism [3].
The exoglycanase from Cellulomonas fimi, endoglucanase C from Clostridium thermocellum, and the beta-glucosidase from Agrobacterium faecalis were labeled using 2-deoxy-2-halo-beta-glycosides, digested with pepsin, and subjected to HPLC-ESIMS/MS analysis, scanning in the neutral loss mode [4].

High impact information on RHE_PD00043

Whereas the rolC beta-glucosidase releases cytokinins from their glucoside conjugates, the rolB encoded protein hydrolyses indole-beta-glucosides [1].
Region-directed mutagenesis of residues surrounding the active site nucleophile in beta-glucosidase from Agrobacterium faecalis [5].
The beta-glucosidase from Agrobacterium sp. catalyzes the hydrolysis of beta-glucosides via a covalent alpha-D-glucopyranosyl-enzyme intermediate involving Glu358 [6].
The role of noncovalent interactions in the catalytic mechanism of the Agrobacterium faecalis beta-glucosidase was investigated by steady-state and pre-steady state kinetic analysis of the hydrolysis of a series of monosubstituted aryl glycosides, in which the hydroxyl groups on the glycone were substituted by hydrogen or fluorine [7].
Here, we report the first application of glycosynthases to solid-phase oligosaccharide synthesis by use of the 51 kDa serine and glycine mutants of Agrobacterium sp. beta-glucosidase, Abg E358S and E358G [8].

Chemical compound and disease context of RHE_PD00043

Mechanistic consequences of replacing the active-site nucleophile Glu-358 in Agrobacterium sp. beta-glucosidase with a cysteine residue [9].
A range of new C-1 modified derivatives of the powerful glucosidase inhibitor 2,5-dideoxy-2,5-imino-D-mannitol has been synthesised and their biological activities probed with the beta-glucosidase from Agrobacterium sp. Ki values are compared with those of previously prepared close relatives [10].
The application of the hyperactive glycosynthase derived from Agrobacterium sp. beta-glucosidase (AbgE358G-2F6) to the synthesis of xylo-oligosaccharides by using alpha-D-xylopyranosyl fluoride as donor represents the first successful use of glycosynthase technology for xylosyl transfer [11].

Biological context of RHE_PD00043

The active site nucleophile of the beta-glucosidase of Agrobacterium faecalis has recently been identified by the use of inhibitors [5].
The DNA sequence was determined for the cloned Agrobacterium sp. strain ATCC 21400 beta-glucosidase gene, abg [12].

Associations of RHE_PD00043 with chemical compounds

Novel, lipophilic derivatives of 2,5-dideoxy-2,5-imino-D-mannitol (DMDP) are powerful beta-glucosidase inhibitors [13].
Furthermore, the N-methyl derivative of calystegine B2 was not catabolized by R. meliloti, and it inhibited alpha-galactosidase, but not beta-glucosidase, whereas the parent alkaloid inhibits both enzymes [14].

References

The protein encoded by the rolB plant oncogene hydrolyses indole glucosides. Estruch, J.J., Schell, J., Spena, A. EMBO J. (1991) [Pubmed]
The plant oncogene rolC is responsible for the release of cytokinins from glucoside conjugates. Estruch, J.J., Chriqui, D., Grossmann, K., Schell, J., Spena, A. EMBO J. (1991) [Pubmed]
Mechanism of Agrobacterium beta-glucosidase: kinetic studies. Kempton, J.B., Withers, S.G. Biochemistry (1992) [Pubmed]
Identification of derivatized peptides without radiolabels: tandem mass spectrometric localization of the tagged active-site nucleophiles of two cellulases and a beta-glucosidase. Tull, D., Miao, S., Withers, S.G., Aebersold, R. Anal. Biochem. (1995) [Pubmed]
Region-directed mutagenesis of residues surrounding the active site nucleophile in beta-glucosidase from Agrobacterium faecalis. Trimbur, D.E., Warren, R.A., Withers, S.G. J. Biol. Chem. (1992) [Pubmed]
Substrate-induced inactivation of a crippled beta-glucosidase mutant: identification of the labeled amino acid and mutagenic analysis of its role. Gebler, J.C., Trimbur, D.E., Warren, A.J., Aebersold, R., Namchuk, M., Withers, S.G. Biochemistry (1995) [Pubmed]
Mechanism of Agrobacterium beta-glucosidase: kinetic analysis of the role of noncovalent enzyme/substrate interactions. Namchuk, M.N., Withers, S.G. Biochemistry (1995) [Pubmed]
Solid-phase oligosaccharide and glycopeptide synthesis using glycosynthases. Tolborg, J.F., Petersen, L., Jensen, K.J., Mayer, C., Jakeman, D.L., Warren, R.A., Withers, S.G. J. Org. Chem. (2002) [Pubmed]
Mechanistic consequences of replacing the active-site nucleophile Glu-358 in Agrobacterium sp. beta-glucosidase with a cysteine residue. Lawson, S.L., Warren, R.A., Withers, S.G. Biochem. J. (1998) [Pubmed]
Probing the aglycon binding site of a beta-glucosidase: a collection of C-1-modified 2,5-dideoxy-2,5-imino-D-mannitol derivatives and their structure-activity relationships as competitive inhibitors. Wrodnigg, T.M., Diness, F., Gruber, C., Häusler, H., Lundt, I., Rupitz, K., Steiner, A.J., Stütz, A.E., Tarling, C.A., Withers, S.G., Wölfler, H. Bioorg. Med. Chem. (2004) [Pubmed]
Enzymatic transglycosylation of xylose using a glycosynthase. Kim, Y.W., Chen, H., Withers, S.G. Carbohydr. Res. (2005) [Pubmed]
Structure and transcription analysis of the gene encoding a cellobiase from Agrobacterium sp. strain ATCC 21400. Wakarchuk, W.W., Greenberg, N.M., Kilburn, D.G., Miller, R.C., Warren, R.A. J. Bacteriol. (1988) [Pubmed]
Novel, lipophilic derivatives of 2,5-dideoxy-2,5-imino-D-mannitol (DMDP) are powerful beta-glucosidase inhibitors. Wrodnigg, T.M., Withers, S.G., Stütz, A.E. Bioorg. Med. Chem. Lett. (2001) [Pubmed]
Biological activities of the nortropane alkaloid, calystegine B2, and analogs: structure-function relationships. Goldmann, A., Message, B., Tepfer, D., Molyneux, R.J., Duclos, O., Boyer, F.D., Pan, Y.T., Elbein, A.D. J. Nat. Prod. (1996) [Pubmed]

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