ライフサイエンスコーパス: beta-N-acetylglucosaminidase

1 trate specificity expected of the processing beta-N-acetylglucosaminidase.

2 iplasmic hydrolases, a chitodextrinase and a beta-N-acetylglucosaminidase.

3 or a lytic transglycosylases but rather as a beta-N-acetylglucosaminidase.

4 lucosidases but also contains a subfamily of beta-N-acetylglucosaminidases.

5 he endogenous levels of specific, processing beta-N-acetylglucosaminidase activity were significantly

6 GlcNAc)2 as chemoattractants and inducers of beta-N-acetylglucosaminidase activity.

7 We have developed an assay system for endo-beta-N-acetylglucosaminidase and glycoamidase (PNGase),

8 erminal beta-GlcNAc moiety by treatment with beta-N-acetylglucosaminidase and selective extension of

9 cterial gene lpqI, encodes an authentic NagZ beta-N-acetylglucosaminidase and that it is essential fo

10 ymes: one with (Man(9)GlcNAc(2))Asn for endo-beta-N-acetylglucosaminidase and the other with Ala-Ser-

11 m amino acid sequence comparisons, the novel beta-N-acetylglucosaminidase appears to be conserved in

12 of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O

13 Endo-beta-N-acetylglucosaminidase completely removed the radi

14 previous suggestion that the broad-spectrum beta-N-acetylglucosaminidase encoded by the SfGlcNAcase-

15 aragine 297 by the streptococcal enzyme endo-beta-N-acetylglucosaminidase (EndoS) induced a dominant

16 nes serotypes secrete two multi-modular endo-beta-N-acetylglucosaminidases, EndoS and EndoS2, that sp

17 Chemical synthesis was combined with endo-beta-N-acetylglucosaminidase (ENGase) catalysis to allow

18 GlcNAc modifications are generated when endo-beta-N-acetylglucosaminidase (ENGase) cleaves N-linked g

19 EndoBT-3987 is a key endo-beta-N-acetylglucosaminidase (ENGase) that initiates the

20 es thetaiotaomicron, encoding a surface endo-beta-N-acetylglucosaminidase (ENGase), BT3987.

21 The endo-beta-N-acetylglucosaminidases (ENGases) are an enzyme cl

22 iae clade species secrete single-domain endo-beta-N-acetylglucosaminidases (ENGases) that specificall

23 Endo-beta-N-acetylglucosaminidases (ENGases) that specificall

24 ed sugar oxazolines and mutant forms of endo beta-N-acetylglucosaminidases (ENGases).

25 e predicted protein sequence is unique among beta-N-acetylglucosaminidases excepting Cht60, recently

26 c hydrolases comprise an endoenzyme, and the beta-N-acetylglucosaminidase, ExoI, reported here.

27 Endo-beta-N-acetylglucosaminidase F(3) cleaves the beta(1-4)

28 ates for Flavobacterium meningosepticum endo-beta-N-acetylglucosaminidases F2 and F3.

29 ion using peptide : N-glycosidase F and endo-beta-N-acetylglucosaminidase F3 resulted in the formatio

30 use it can be either trimmed by a processing beta-N-acetylglucosaminidase (FDL) to produce paucimanno

31 The endo-beta-N-acetylglucosaminidase from Arthrobacter protophor

32 the transglycosylation activity of the endo-beta-N-acetylglucosaminidase from Arthrobacter protophor

33 studies on a representative member, the Nag3 beta-N-acetylglucosaminidase from Cellulomonas fimi, we

34 Endo-beta-N-acetylglucosaminidase from Streptococcus pneumoni

35 The transglycosylation activity of the endo-beta-N-acetylglucosaminidases from Arthrobacter protopho

36 The accompanying papers describe two unique beta-N-acetylglucosaminidases from Vibrio furnissii.

37 ure that allows sequential isolation of endo-beta-N-acetylglucosaminidase H (EC 3.2.1.96)-released hi

38 as of immunoprecipitates digested with endo-beta-N-acetylglucosaminidase H (Endo H), indicate that Z

39 inyl)asparagine amidase (PNGase F)- and endo-beta-N-acetylglucosaminidase H (Endo H)-released oligosa

40 uality control but can be removed using endo-beta-N-acetylglucosaminidase H (Endo H).

41 Using endo-beta-N-acetylglucosaminidase H and peptide:N-glycosidase

42 phosphorylated, but it was sensitive to endo-beta-N-acetylglucosaminidase H and to glycopeptidase A.

43 n addition to functional heterogeneity, endo-beta-N-acetylglucosaminidase H digestion and glycomic pr

44 w cytometry, brefeldin A treatment, and endo-beta-N-acetylglucosaminidase H digestion suggested that

45 e N-linked oligosaccharides released by endo-beta-N-acetylglucosaminidase H from Schizosaccharomyces

46 by the action of Streptomyces plicatus endo-beta-N-acetylglucosaminidase H on RNase B.

47 Both proteins remained endo-beta-N-acetylglucosaminidase H sensitive, indicating tha

48 of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present o

49 Ngs1 can bind GlcNAc through the N-terminal beta-N-acetylglucosaminidase homology domain.

50 d 26 were potent and selective inhibitors of beta-N-acetylglucosaminidases in the submicromolar range

51 ence or absence of this specific, processing beta-N-acetylglucosaminidase is a key factor distinguish

52 olases such as leucine aminopeptidase (LAP), beta-N-acetylglucosaminidase (NAG), their sum (N(acq)),

53 We studied transgenic mice that over express beta-N-acetylglucosaminidase (O-GlcNAcase), an enzyme th

54 transferase (OGT), which adds the sugar, and beta-N-acetylglucosaminidase (O-GlcNAcase), which hydrol

55 moval of N-acetylglucosamine is regulated by beta-N-acetylglucosaminidase (O-GlcNAcase), which was pr

56 we further characterize the recently cloned beta-N-acetylglucosaminidase, O-GlcNAcase.

57 (fdl) gene encodes the specific, processing beta-N-acetylglucosaminidase of Drosophila melanogaster.

58 The beta-N-acetylglucosaminidase of Escherichia coli was fou

59 that Sf-fdl encodes the specific, processing beta-N-acetylglucosaminidase of S. frugiperda and valida

60 cetylglucosaminyltransferase) and removal (O-beta-N-acetylglucosaminidase) of the monosaccharide.

61 Purified Jun a 1 was treated with beta-N-acetylglucosaminidase S and analysed using immuno

62 he direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc

63 We concluded that dspB encodes a soluble beta-N-acetylglucosaminidase that causes detachment and

64 sted that this gene encodes a broad-spectrum beta-N-acetylglucosaminidase that functions in glycan an

65 de hydrolase family GH85 is a family of endo-beta-N-acetylglucosaminidases that is responsible for th

66 After N-glycan release by an endo-beta-N-acetylglucosaminidase, the mannosyl arms are trim

67 An exception to this is beta-N-acetylglucosaminidase, where 15% of the activity

68 e by treatment of the soluble complexes with beta-N-acetylglucosaminidase, which catalyzes hydrolysis

69 ose type structure is produced by an unusual beta-N-acetylglucosaminidase, which removes the terminal