Evidence for a polysaccharide-binding domain in Hormoconis resinae glucoamylase P: effects of its proteolytic removal on substrate specificity and inhibition by β-cyclodextrin

References

1. Abe J., Nakajima K., Hizukuri S. 1990; Alteration of the properties of Aspergillus sp. K-27 glucoamylase on limited proteolysis with subtilisin.. Carbohydr Res 203:129–138
   [Google Scholar]
2. Aleshin A., Golubev A., Firsov L. M., Honzatko R. B. 1992; Crystal Structure of glucoamylase from Aspergillus awamori var. X100 to 2-2 A Resolution. J Biol Chem 267:19291–19298
   [Google Scholar]
3. Belshaw N.J., Williamson G. 1990; Production and purification of a granular-starch-binding domain of glucoamylase 1 from Aspergillus niger.. FEBS Lett 269:350–353
   [Google Scholar]
4. Belshaw N.J., Williamson G. 1991; Interaction of β-cyclodextrin with the granular starch binding domain of glucoamylase. Biochim Biophys Acta 1078:117–120
   [Google Scholar]
5. Belshaw N.J., Williamson G. 1993; Specificity of the binding domain of glucoamylase 1. Eur J Biochem 211:717–724
   [Google Scholar]
6. Cattlay B.J. 1979; Pullulan synthesis by Aureobasidum pullulans.. In Microbial Polysaccharides and Polysaccharases pp. 69–84 Edited by Berkeley R.C. E., Gooday G. W. , Ellwood D. C. . London: Academic Press;
   [Google Scholar]
7. Cornish-Bowden A. 1977; An automatic method for deriving steady-state rate equations. Biochem J 165:55–59
   [Google Scholar]
8. Dalmia B.K., Nikolov Z. L. 1991; Characterization of glucoamylase adsorption to raw starch. Enzyme Microb Technol 13:982–990
   [Google Scholar]
9. Fagerstrom R. 1991; Subsite mapping of Hormoconis resinae glucoamylases and their inhibition by gluconolactone. J Gen Microbiol 137:1001–1008
   [Google Scholar]
10. Fagerstrom R. 1994; Purification and specificity of recombinant Hormoconis resinae glucoamylase P and endogenous glucoamylase from Trichoderma reesei.. Enzyme Microb Technol 16:36–42
    [Google Scholar]
11. Fagerstrom R., Vainio A., Suoranta K., Pakula T., Kalkkinen N., Torkkeli H. 1990; Comparison of two glucoamylases from Hormoconis resinae. J Gen Microbiol 136:913–920
    [Google Scholar]
12. Fukuda K., Teramoto Y., Goto M., Sakamoto J., Mitsuiki S., Hayashida S. 1992; Specific inhibition by cyclodextrins of raw starch digestion by fungal glucoamylase. Biosci Biotechnol Biochem 56:556–559
    [Google Scholar]
13. Hansen S.A. 1975; Thin-layer chromatographic method for identification of oligosaccharides in starch hydrolyzates. J Chromatogr 105:338–390
    [Google Scholar]
14. Hayashida S., Nakahara K., Kanlayakrit W., Hara T., Teramoto Y. 1989; Characteristics and function of raw-starch-affinity site on Aspergillus awamori var. kawachi glucoamylase I molecule.. Aggie Biol Chem 53:143–149
    [Google Scholar]
15. Hayashida S., Teramoto Y., Inoue T., Mitsuiki S. 1990; Occurrence of an affinity site apart from the active site on the raw-starch-binding but non-raw-starch-adsorbable Bacillus subtilis 65 alpha-amylase.. Appl Environ Aiicrobiol 56:2584–2586
    [Google Scholar]
16. Joutsjoki V.V., Torkkeli T. K. 1992; Glucoamylase P gene of Hormoconis resinae. Molecular cloning, sequencing and introduction into Trichoderma reesei. FEMS Microbiol Lett 99:237–244
    [Google Scholar]
17. Joutsjoki V., Torkkeli T., Nevalainen H. 1993; Transformation of Trichoderma reesei with the Hormoconis resinae glucoamylase P (gam P) gene: production of a heterologous glucoamylase by Trichoderma reesei. Curr Genet 24:223–228
    [Google Scholar]
18. Kalkkinen N., SiTilgmann C. 1988; A gas-pulsed-phase sequencer constructed from a Beckman 890D instrument by using Applied Biosystems delivery and cartridge blocks. J Protein Chem 7:242–243
    [Google Scholar]
19. Kobayashi M., Takagi S., Matsuda K., Ichishima E. 1988; Inhibition of a-amylase and phosphorylases by cyclodextrin-dialdehyde. Agric Biol Chem 52:2703–2708
    [Google Scholar]
20. Kraulis P. J., Clore G. M., Nilges M., Jones T. A., Pettersson G., Knowles J., Gronenborn A. M. 1989; Determination of the three-dimensional structure of the C-terminal domain of cellobio-hydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry—dynamical simulated annealing.. Biochemistry 28:7241–7257
    [Google Scholar]
21. Laemmli U.K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
    [Google Scholar]
22. Marshall J.J. 1973; Inhibition of pullulanase by Shardinger dextrins. FEBS Lett 37:269–273
    [Google Scholar]
23. McCleary B.V., Anderson M. A. 1980; Hydrolysis of α-D-glucans and α-D-gluco-oligosaccharides by Cladosporium resinae glucoamylases.. Carbohydr Res 86:77–96
    [Google Scholar]
24. Meagher M. M., Nikolov Z. L., Reilly P. J. 1989; Subsite mapping of Aspergillus niger glucoamylase I and II with malto-and isomaltooligosaccharides.. Biotechnol Bioeng 34:681–688
    [Google Scholar]
25. Medda S., Saha B. C., Ueda S. 1982; Raw starch adsorption and elution behavior of glucoamylase I of black Aspergillus. J Fermentation Technol 60:261–264
    [Google Scholar]
26. Melasniemi H. 1987; Effect of carbon source on production of thermostable alpha-amylase, pullulanase and a-glucosidase by Clostridium thermohydrosulfuricum. J Gen Microbiol 133:883–890
    [Google Scholar]
27. Miranda M., Murado M. A., Sanroman A., Lema J. M. 1991; Mass transfer control of enzymatic hydrolysis of polysaccharides by glucoamvlase. Enzyme Microb Tecbnol 13:142–147
    [Google Scholar]
28. Monma M., Yamamoto Y., Kainuma K. 1989; Subsite structure of Cblara paradoxa glucoamylase and interaction of the glucoamvlase with cyclodextrins.. Agric Biol Chem 53:1503–1508
    [Google Scholar]
29. Rouvinen J., Bergfors T., Teeri T., Knowles J. K. C., Jones T. A. 1990; The three dimensional structure of cellobiohydrolase II from Yrichoderma reesei. Science 249:380–386
    [Google Scholar]
30. Scopes R.K. 1974; Measurement of protein by spectrophotometry at 205 nm. Anal Biochem 59:277–282
    [Google Scholar]
31. Savel'ev A.N., Sergeev V. R., Firsov L. M. 1989; Analysis of an additional substrate-binding site of glucoamylase I. The effect of cyclodextrin on glucoamylase-catalized reactions. Biokhimiya 54:1725–1731
    [Google Scholar]
32. Stoffer B., Frandsen T. P., Busk P. K., Schneider P., Svendsen I., Svensson B. 1993; Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger. Biochem J 292:197–202
    [Google Scholar]
33. Svensson B., Larsen K., Gunnarson A. 1986; Characterisation of a glucoamylase G2 from Aspergillus niger. Eur J Biochem 154:497–502
    [Google Scholar]
34. Svensson B., Jespersen H., Sierks M. R., MacGregor E. A. 1989; Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochem J 264:309–311
    [Google Scholar]
35. Takahashi T., Kato K., Ikegami Y., Irie M. 1985; Different behavior towards raw starch of three forms of glucoamylase from Rhizopus sp.. J Biochem 98:663–671
    [Google Scholar]
36. Thoma J.A., Koshland D. E. 1960; Competitive inhibition by substrate during enzyme action. Evidence for the induced-fit theory. J Am Chem Soc 82:3329–3333
    [Google Scholar]
37. Ueda S., Saha B. C. 1983; Behaviour of Endomjcopsis fibuligera glucoamylase towards raw starch.. Enzyme Microb Technol 5:196–198
    [Google Scholar]
38. Vainio A.E.I., Torkkeli H. T., Tuusa T., Aho S. A., Fagerstrom B. R., Korhola M. P. 1993; Cloning and expression of Hormoconis resinae glucoamylase P cDNA in Saccharomyces cerevisiae. Curr Genet 24:38–44
    [Google Scholar]
39. van Tilbeurgh H., Tomme P., Claeyssens M., Bhikhabhai R., Petterson G. 1986; Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei. Separation of functional domains.. FEBS Lett 204:223–227
    [Google Scholar]
40. Williamson G., Belshaw N. J., Williamson M. P. 1992; O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding. Biochem J 282:423–428
    [Google Scholar]