ライフサイエンスコーパス: glucoamylase

1 he STA genes of yeast, which encode secreted glucoamylase.

2 ue is also critical for strong inhibition of glucoamylase.

3 cking the peripheral subdomain of eukaryotic glucoamylases.

4 ch-binding domain (SBD) of Aspergillus niger glucoamylase 1 (GA-I) with substrate has been investigat

5 the granular starch binding domain (SBD) of glucoamylase 1 from Aspergillus niger has been determine

6 matic degradation of crystalline starches by glucoamylase 1.

7 iptional downregulation of the gene encoding glucoamylase, a major secreted protein, but not two non-

8 hibition of maltase, sucrase, isomaltase and glucoamylase activity by acarbose, epigallocatechin gall

9 ere very effective in inhibiting maltase and glucoamylase activity, but only white tea extract inhibi

10 r and Arg125-->Lys had only minor effects on glucoamylase activity.

11 ole of a loop region, highly conserved among glucoamylase and other starch hydrolases which also incl

12 g N- and C-terminal subunits of both maltase-glucoamylase and sucrase-isomaltase.

13 h escapes digestion by host small intestinal glucoamylases and transits the colon where it is degrade

14 Isofagomine inhibits beta-glucosidase, glucoamylase, and isomaltase more strongly than 1-deoxyn

15 Based on the results, the purified glucoamylase appeared to be a newly isolated enzyme.

16 e starch binding domain serves to target the glucoamylase at sites where the starch granular matrix i

17 charide showed very strong inhibition toward glucoamylase, being nearly as potent an inhibitor as aca

18 mutation decreases the thermal stability of glucoamylase by 19 degrees C with little effect on activ

19 coamylases may have evolved from prokaryotic glucoamylases by the substitution of the N-terminal doma

20 ile the structures of other fungal and yeast glucoamylase catalytic and starch binding domains have b

21 e have cloned human small intestinal maltase-glucoamylase cDNA to permit study of the individual cata

22 Maltase-glucoamylase cDNA was amplified from human intestinal RN

23 gal proteases, a lipase, and an amylase with glucoamylase demonstrated improved dietary protein, lipi

24 It has been hypothesized that human mucosal glucoamylase (EC 3.2.1.20 and 3.2.1.3) activity serves a

25 Crystal structures at pH 4 of complexes of glucoamylase from Aspergillus awamori var. X100 with the

26 single-residue mutants at the active site of glucoamylase from Aspergillus niger.

27 Herein, we investigate a glucoamylase from newly isolated Aspergillus niger.

28 The catalytic mechanism of glucoamylase (GA) is investigated by comparing kinetic r

29 e catalytic mechanism of Aspergillus awamori glucoamylase (GA) were identified by studying pre-steady

30 been applied to various hydrolases including glucoamylase (GA).

31 Glucoamylases (GAs) from a wild and a deoxy-d-glucose-re

32 sor of the glucose- and Snf1-regulated STA1 (glucoamylase) gene.

33 ggest the presence of potentially functional glucoamylase (GH15)-like domains near their amino termin

34 encoding aglA gene under the control of the glucoamylase (glaA) promoter.

35 al structure of a complete Hypocrea jecorina glucoamylase has been determined at 1.8 A resolution.

36 operating temperature of Aspergillus awamori glucoamylase has been increased by several thermostable

37 Maltase-glucoamylase has two catalytic sites identical to those

38 and the previously constructed Trp120-->Phe glucoamylases have significantly reduced activity toward

39 salt activated lipase (hBAL); human maltase-glucoamylase (hMGA); human pancreatic alpha-amylase (hPA

40 Domains similar to those of prokaryotic glucoamylases in maltose phosphorylases (Family GH65) an

41 ch a domain in PhK by demonstrating that the glucoamylase inhibitor acarbose binds PhK, perturbs its

42 orted to date and also a strong inhibitor of glucoamylase, isomaltase, and alpha-glucosidase.

43 Eukaryotic glucoamylases may have evolved from prokaryotic glucoamy

44 Brush-border maltase-glucoamylase (MGA) activity serves as the final step of

45 e by the mucosal alpha-glucosidases, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI).

46 , pancreatic amylase (AMY2A, AMY2B), maltase-glucoamylase (MGAM), and sucrase-isomaltase (SI) genes o

47 The glucoamylase nature of the enzyme was also confirmed usi

48 ee energy values for enzymes DPP-IV, maltase-glucoamylase, pancreatic alpha-amylase and sucrase-isoma

49 immaturity or malnutrition and that maltase-glucoamylase plays a unique role in the digestion of mal

50 t are homologous to the sporulation-specific glucoamylase SGA and to two other sequences, S2 and S1.

51 e model, which suggests that the H. jecorina glucoamylase structure we report is independent of cryst

52 al distortion observed in the active site of glucoamylase suggests that favorable electrostatic inter

53 Human maltase-glucoamylase was purified by immunoisolation and partial

54 stal structures of a two-domain, prokaryotic glucoamylase were determined to high resolution from the

55 Residues 121-125 of A. awamori glucoamylase were singly substituted, and their individu

56 cosidase, isomaltase, alpha-mannosidase, and glucoamylase, were obtained.

57 ctural homologue to human intestinal maltase-glucoamylase with a highly conserved catalytic domain an

58 ally fused downstream of the carrier protein glucoamylase with a Lys-Arg KEX2-like cleavage site at t