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1 disease caused by a deficiency of the enzyme beta-mannosidase.
2  previously purified by Kengen et al., and a beta-mannosidase.
3  a previously unobserved structural-fold for beta-mannosidases.
4                                              Beta-mannosidase, a lysosomal enzyme which acts exclusiv
5 nan requires endo-1,4-beta-mannanase and 1,4-beta-mannosidase activities.
6     Homozygous mutant mice have undetectable beta-mannosidase activity.
7 ilar gene organization with tomato endosperm beta -mannosidase and barley seed beta -glucosidase/ bet
8                             In addition, the beta-mannosidase and beta-glucosidase from P. furiosus b
9                                          The beta-mannosidase and beta-glucosidase genes were isolate
10 ity; however, this enzyme also exhibited 1,4-beta-mannosidase and cellodextrinase activities.
11    Based on these sequence similarities, the beta-mannosidase and the beta-glucosidase can both be cl
12 olecular masses of 59.0 and 54.6 kDa for the beta-mannosidase and the beta-glucosidase, respectively.
13 LysMan), core-specific alpha1,6-mannosidase, beta-mannosidase, and cleavage at the reducing terminus
14 nnosidase and barley seed beta -glucosidase/ beta -mannosidase BGQ60.
15 slG is not, as previously suggested, an endo-beta-mannosidase but instead a retaining endo-beta-gluco
16         The complete sequence of the caprine beta-mannosidase cDNA coding region has been determined,
17                                            A beta-mannosidase could be known to hydrolyze beta-mannos
18 uenced the entire coding region of the human beta-mannosidase gene using a combination of cDNA librar
19 gues showed good and selective inhibition of beta-mannosidase (Helix pomatia).
20 etic analysis demonstrates that BtMan2A is a beta-mannosidase in which substrate binding energy is pr
21 e, alpha- and beta-galactosidase, alpha- and beta-mannosidase) in an assay that measured the rate of
22 otential treatment strategies, we produced a beta-mannosidase knockout mouse.
23 alysis and identified that the expression of beta-mannosidase (MANBA) was lower in kidneys of subject
24 he beta-glucosidase, the primary role of the beta-mannosidase may not be disaccharide hydrolysis.
25 res, we determine that most glucosidases and beta-mannosidases preferentially bind their substrates i
26                                          The beta-mannosidase showed optimal activity at pH 7.4 and 1
27 k the phosphate binding residues, are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic lin
28 ing we found that it is a trimeric retaining beta-mannosidase, that is susceptible to several known m
29              The catalytic efficiency of the beta-mannosidase was significantly lower than that repor
30                   Km and Vmax values for the beta-mannosidase were determined to be 0.79 mM and 31.1