These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
210 related articles for article (PubMed ID: 8890914)
1. Structure and energetics of the glucoamylase-isomaltose transition-state complex probed by using modeling and deoxygenated substrates coupled with site-directed mutagenesis. Frandsen TP; Stoffer BB; Palcic MM; Hof S; Svensson B J Mol Biol; 1996 Oct; 263(1):79-89. PubMed ID: 8890914 [TBL] [Abstract][Full Text] [Related]
2. Catalytic mechanism of glucoamylase probed by mutagenesis in conjunction with hydrolysis of alpha-D-glucopyranosyl fluoride and maltooligosaccharides. Sierks MR; Svensson B Biochemistry; 1996 Feb; 35(6):1865-71. PubMed ID: 8639668 [TBL] [Abstract][Full Text] [Related]
3. Substrate binding mechanism of Glu180-->Gln, Asp176-->Asn, and wild-type glucoamylases from Aspergillus niger. Christensen U; Olsen K; Stoffer BB; Svensson B Biochemistry; 1996 Nov; 35(47):15009-18. PubMed ID: 8942667 [TBL] [Abstract][Full Text] [Related]
4. Energetic and mechanistic studies of glucoamylase using molecular recognition of maltose OH groups coupled with site-directed mutagenesis. Sierks MR; Svensson B Biochemistry; 2000 Jul; 39(29):8585-92. PubMed ID: 10913265 [TBL] [Abstract][Full Text] [Related]
5. Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue active site sequences and thiol/disulfide engineering. Fierobe HP; Stoffer BB; Frandsen TP; Svensson B Biochemistry; 1996 Jul; 35(26):8696-704. PubMed ID: 8679632 [TBL] [Abstract][Full Text] [Related]
6. Mutational analysis of the roles in catalysis and substrate recognition of arginines 54 and 305, aspartic acid 309, and tryptophan 317 located at subsites 1 and 2 in glucoamylase from Aspergillus niger. Frandsen TP; Christensen T; Stoffer B; Lehmbeck J; Dupont C; Honzatko RB; Svensson B Biochemistry; 1995 Aug; 34(32):10162-9. PubMed ID: 7640270 [TBL] [Abstract][Full Text] [Related]
7. Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose. Giardina T; Gunning AP; Juge N; Faulds CB; Furniss CS; Svensson B; Morris VJ; Williamson G J Mol Biol; 2001 Nov; 313(5):1149-59. PubMed ID: 11700070 [TBL] [Abstract][Full Text] [Related]
8. Recruitment of both uniform and differential binding energy in enzymatic catalysis: xylanases from families 10 and 11. Wicki J; Schloegl J; Tarling CA; Withers SG Biochemistry; 2007 Jun; 46(23):6996-7005. PubMed ID: 17503782 [TBL] [Abstract][Full Text] [Related]
9. Functional roles of the invariant aspartic acid 55, tyrosine 306, and aspartic acid 309 in glucoamylase from Aspergillus awamori studied by mutagenesis. Sierks MR; Svensson B Biochemistry; 1993 Feb; 32(4):1113-7. PubMed ID: 8424940 [TBL] [Abstract][Full Text] [Related]
10. Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism. Aleshin AE; Stoffer B; Firsov LM; Svensson B; Honzatko RB Biochemistry; 1996 Jun; 35(25):8319-28. PubMed ID: 8679589 [TBL] [Abstract][Full Text] [Related]
11. Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori. Sierks MR; Ford C; Reilly PJ; Svensson B Protein Eng; 1990 Jan; 3(3):193-8. PubMed ID: 1970434 [TBL] [Abstract][Full Text] [Related]
12. Binding of isomaltose and maltose to the glucoamylase from Aspergillus niger, as studied by fluorescence spectrophotometry and steady-state kinetics. Ohnishi M; Matsumoto T; Yamanaka T; Hiromi K Carbohydr Res; 1990 Sep; 204():187-96. PubMed ID: 2279245 [TBL] [Abstract][Full Text] [Related]
13. Overexpression and characterization of Aspergillus awamori wild-type and mutant glucoamylase secreted by the methylotrophic yeast Pichia pastoris: comparison with wild-type recombinant glucoamylase produced using Saccharomyces cerevisiae and Aspergillus niger as hosts. Fierobe HP; Mirgorodskaya E; Frandsen TP; Roepstorff P; Svensson B Protein Expr Purif; 1997 Mar; 9(2):159-70. PubMed ID: 9056481 [TBL] [Abstract][Full Text] [Related]
14. Site-directed mutagenesis of the catalytic base glutamic acid 400 in glucoamylase from Aspergillus niger and of tyrosine 48 and glutamine 401, both hydrogen-bonded to the gamma-carboxylate group of glutamic acid 400. Frandsen TP; Dupont C; Lehmbeck J; Stoffer B; Sierks MR; Honzatko RB; Svensson B Biochemistry; 1994 Nov; 33(46):13808-16. PubMed ID: 7947792 [TBL] [Abstract][Full Text] [Related]
15. Stopped-flow fluorescence and steady-state kinetic studies of ligand-binding reactions of glucoamylase from Aspergillus niger. Olsen K; Svensson B; Christensen U Eur J Biochem; 1992 Oct; 209(2):777-84. PubMed ID: 1425682 [TBL] [Abstract][Full Text] [Related]
16. Some details of the reaction mechanism of glucoamylase from Aspergillus niger--kinetic and structural studies on Trp52-->Phe and Trp317-->Phe mutants. Christensen T; Stoffer BB; Svensson B; Christensen U Eur J Biochem; 1997 Dec; 250(3):638-45. PubMed ID: 9461285 [TBL] [Abstract][Full Text] [Related]
17. Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis. Sierks MR; Ford C; Reilly PJ; Svensson B Protein Eng; 1993 Jan; 6(1):75-9. PubMed ID: 8433972 [TBL] [Abstract][Full Text] [Related]
18. Roles of the aromatic side chains in the binding of substrates, inhibitors, and cyclomalto-oligosaccharides to the glucoamylase from Aspergillus niger probed by perturbation difference spectroscopy, chemical modification, and mutagenesis. Svensson B; Sierks MR Carbohydr Res; 1992 Apr; 227():29-44. PubMed ID: 1499029 [TBL] [Abstract][Full Text] [Related]
19. Automated docking of glucosyl disaccharides in the glucoamylase active site. Coutinho PM; Dowd MK; Reilly PJ Proteins; 1997 Jun; 28(2):162-73. PubMed ID: 9188734 [TBL] [Abstract][Full Text] [Related]
20. Glucoamylase mutants in the conserved active-site segment Trp170-Tyr175 located at a distance from the site of catalysis. Stoffer BB; Dupont C; Frandsen TP; Lehmbeck J; Svensson B Protein Eng; 1997 Jan; 10(1):81-7. PubMed ID: 9051738 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]