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

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

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

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

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

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

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

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

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

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

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

19 Maltase-glucoamylase cDNA was amplified from human intestinal RN

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

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

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

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

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

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

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

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

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

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

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

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

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

33 Maltase-glucoamylase has two catalytic sites identical to those

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

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

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

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

38 Eukaryotic glucoamylases may have evolved from prokaryotic glucoamy

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

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

41 The glucoamylase nature of the enzyme was also confirmed usi

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

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

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

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

46 Human maltase-glucoamylase was purified by immunoisolation and partial

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

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

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

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

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