Analysis of essential histidine residues of maize branching enzymes by chemical modification and site-directed mutagenesis

Journal of Protein Chemistry

Volumn 17, Issue 7, 1998, Pages 579-590

  Funane, Kazumi ^a,b   Libessart, Nathalie ^a   Stewart, Douglas ^a,c   Michishita, Toru ^a,d   Preiss, Jack ^a  

^a Michigan State University ^*  (United States)

^b NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

^c UNIVERSITY OF ADELAIDE   (Australia)

^d Agricultural Research Institute   (Japan)

Author keywords

Branching enzyme; Chemical modification; Diethyl pyrocarbonate; Histidine residues; Site directed mutagenesis; Substrate binding

Indexed keywords

1,4 ALPHA GLUCAN BRANCHING ENZYME; AMYLOPECTIN; AMYLOSE; CARBOHYDRATE; DIETHYL PYROCARBONATE; HISTIDINE; HYDROXYLAMINE; MALTOSE; MUTANT PROTEIN;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; MAIZE; NONHUMAN; PROTEIN MODIFICATION; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI; ZEA MAYS;

EID: 0031758305     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02780959     Document Type: Article

References (54)

1. Baba, T., Kimura, K., Mizuno, K., Etoh, H., Ishida, Y., Shida, O., and Arai, Y. (1991). Sequence conservation of the catalytic region of amylolytic enzymes in maize branching enzyme-I, Biochem. Biophys. Res. Commun. 181, 87-94.
2. Boel, E., Brady, L., Brozozowski, A. M., Derewenda, Z., Dodson, G. G., Jansen, V. J., Peterson, S. B., Swift, H., Thim, L., and Woldike, H. F. (1990). Calcium binding in α-amylases: An X-ray diffraction study at 2.1-Å resolution of two enzymes from Aspergillus, Biochemistry 29, 6244-6249.
3. Boyer, C. D., and Preiss, J. (1978). Multiple forms of (1,4)-α-D-glucan, (1,4)-α-D-glucan-6-glycosyl transferase from developing Zea mays L Kernels, Carbohydr. Res. 61, 321-334.
4. Buisson, G., Duée, E., Haser, R., and Payan, F. (1987). Three dimensional structure of porcine pancreatic α-amylase at 2.9 Å resolution. Role of calcium in structure and activity, EMBO J. 6, 3909-3916.
5. Burnette, W. W. (1981). Western blotting. Electerophoretic transfer of protein from SDS-polyacrylamide gels to nitrocellulose and radiographic detection with antibody and radiolabelled protein A, Anal. Biochem. 112, 195-203.
6. Cao, H., and Preiss, J. (1996). Evidence for essential arginine residues at the active sites of maize branching enzymes, J. Protein Chem. 15, 291-304.
7. Dang, P. L., and Boyer, C. D. (1988). Maize leaf and kernel starch synthases and branching enzymes, Phytochemistry 27, 1255-1259.
8. Fisher, D. K., Boyer, C. D., and Hannah, L. C. (1993). Starch branching enzyme II from maize endosperm, Plant Physiol. 102, 1045-1046.
9. Goldner, W., and Beevers, H. (1989). Starch synthase and starch branching enzyme from germinating castor bean endosperm, Phytochemistry 28, 1809-1812.
10. Guan, H. P., and Preiss, J. (1993). Differentiation of the properties of the branching isozymes from maize (Zea mays), Plant Physiol. 102, 1269-1273.
11. Guan, H. P., Baba, T., and Preiss, J. (1994a). Expression of branching enzyme I of maize endosperm in Escherichia coli. Plant Physiol. 104, 1449-1453.
12. Guan, H. P., Baba, T., and Preiss, J. (1994b). Expression of branching enzyme II of maize endosperm in Escherichia coli, Cell. Mol. Biol. 40, 981-985.
13. Guan, H. P., Kuruki, T., Sivak, M., and Preiss, J. (1995). Maize branching enzyme catalyzes synthesis of glycogen-like polysaccharide in glgB-deficient Escherichia coli, Proc. Natl. Acad. Sci. USA 92, 964-967.
14. Hawker, J. S., Ozbun, J. L., Ozaki, H., Greenberg, E., and Preiss, J. (1974). Interaction of spinach leaf adenosine diphosphatase glucose α-1,4 glucan α-4-glucosyl transferase and α-1,4 glucan, α-1,4 glucan-6-glycosyl transferase in synthesis of branched α-glucan, Arch. Biochem. Biophys. 160, 530-551.
15. Holm, L., Koivula, A. K., Lehtovaara, P. M., Hemminki, A., and Knowles, J. K. C. (1990). Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus alpha-amylase, Protein Eng. 3, 181-191.
16. Huang, Y., and Dennis, D. T. (1995). Histidine residues 139, 163 and 500 are essential for catalytic activity of cofactor-independent phosphoglyceromutase from developing endosperm of the castor plant. Eur. J. Biochem. 229, 395-402.
17. Ishikawa, K., Matsui, I., and Honda, K. (1990). Substrate-dependent shift of optimum pH in porcine pancreatic α-amylose-catalyzed reactions. Biochemistry 29, 7119-7123.
18. Jespersen, H. M., MacGregor, E. A., Sierks, M. R., and Svensson, B. (1991). Comparison of the domain-level organization of starch hydrolases and related enzymes, Biochem. J. 280, 51-55.
19. 8-barrel domain and evolutionary relationship to other amylolytic enzymes, J. Protein Chem. 12, 791-805.
20. Klein, C., and Shulz, G. E. (1991). Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution, J. Mol. Biol. 217, 737-750.
21. Knegtel, R. M. A., Strokopytov, B., Penninga, D., Faber, O. G., Rozeboom, H. J., Kalk, K. H., Dijkhuizen, L., and Dijkstra, B. W. (1995). Crystallographic studies of the interaction of cyclodextrin glycosyltransferases from Bacillus circulans strain 251 with natural substrates and products, J. Biol. Chem. 270, 29256-29264.
22. Kubota, M., Matsuura, Y., Sakai, S., and Katsube, Y. (1991). Molecular structure of B. stearothermophilus cyclodextrin glucanotransferase and analysis of substrate binding site, Denpun Kagaku 38, 141-146.
23. Kuriki, T. (1992). Can protein engineering interconvert glucanohydrolases/gluconotransferases, and their specificities? Trends Glycosci. Glycotechnol. 4, 567-572.
24. Kuriki, T., and Okada, S. (1995). A new concept of the criteria of various amylolytic enzymes and related enzymes; similarities in specificities and structures, in Enzyme Chemistry and Molecular Biology of Amylases and Related Enzymes (Amylase Research Society of Japan, ed.), CRC Press, Boca Raton, Florida, pp. 87-92.
25. Kuriki, T., Okada, S., and Imanaka, T. (1988). New type of pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis, J. Bacteriol. 170, 1554-1559.
26. Kuriki, T., Takata, H., Okada, S., and Imanaka, T. (1991). Analysis of the active center of Bacillus stearothermophilus neopullulanase, J. Bacteriol. 173, 6147-6152.
27. Kuriki, T., Guan, H. P., Sivak, M., and Preiss, J. (1996). Analysis of the active center of branching enzyme II from maize endosperm, J. Protein Chem. 15, 305-313.
28. Kuriki, T., Stewart, D. C., and Preiss, J. (1997). Construction of chimeric enzymes out of maize endosperm branching enzymes I and II: Activity and properties, J. Biol. Chem. 272, 28999-29004.
29. Laemmli, U. K. (1970). Cleavage of structure proteins during the assembly of the head bacteriophage T4, Nature 227, 680-685.
30. Lundblad, R. L. (1991). Chemical Reagents for Protein Modification, 2nd ed., pp. 105-128.
31. MacGregor, E. A., and Svensson, B. (1989). A super-secondary structure predicted to be common to several α-1,4-D-glucan-cleaving enzymes, Biochem. J. 259, 145-152.
32. Matsuura. Y., Kusunoki, M., Harada, W., and Kakudo, M. (1984). Structure and possible catalytic residues of Taka-amylase A, J. Biochem. (Tokyo) 95, 697-702.
33. Miles, E. W. (1977). Modification of histidyl residues in proteins by diethylpyrocarbonate, Meth. Enzymol. 47, 431-442.
34. 2 subunit of tryptophan synthetase by photo-oxidation in the presence of pyridoxal 5′-phosphate and L-serine and by diethylpyrocarbonate, J. Biol. Chem. 249, 2843-2851.
35. Mizuno, K., Kimura, K., Arai, Y., Kawasaki, T., Shimada, H., and Baba, T. (1992). Starch branching enzymes from immature rice seeds, J. Biochem. 112, 643-651.
36. Mizuno, K., Kawasaki, T., Shimada, H., Satoh, H., Kobayashi, E., Okumura, S., Arai, Y., and Baba, T. (1993). Alteration of the structural properties of starch components by lack of an isoform of starch branching enzyme in rice seeds, J. Biol. Chem. 268, 19084-19091.
37. Nagashima, T., Tada, S., Kitamoto, K., Gomi, K., Kumagai, C., and Toda, H. (1992). Site-directed mutagenesis of the catalytic active-site residues of Taka-amylase A, Biosci. Biotech. Biochem. 56, 207-210.
38. Nakamura, Y., Takeichi, T., Kawaguchi, K., and Yamanouchi, H. (1992). Purification of two forms of starch branching enzyme (Q-enzyme) from developing rice endosperm, Physiol. Plant. 84, 329-335.
39. Nakamura, A., Haga, K., and Yamane, K. (1993). Three histidine residues in the active center of cyclodextrin glucanotransferase from Alkalophilic bacillus sp. 1011: Effects of the replacement on pH dependence and transition-state stabilization, Biochemistry 32, 6624-6631.
40. Poulsen, P., and Kreiberg, J. D. (1993). Starch branching enzyme cDNA from Solanum tuberosum, Plant Physiol. 102, 1053-1054.
41. Romeo, T., Kumar, A., and Preiss, J. (1988). Analysis of Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes, Gene 70, 363-376.
42. Sambrook, J., Fristsch, E. F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
43. Sanger, F., Nicklen, S., and Coulson, A. R. (1977). DNA sequencing with chain-terminating inhibitors, Proc. Natl. Acad. Sci. USA 74, 5463-5467.
44. Singh, B. K., and Preiss, J. (1985). Starch branching enzymes from maize: Immunological characterization using polyclonal and monoclonal antibodies, Plant Physiol. 78, 849-852.
45. Sivak, M., and Preiss, J. (1995). In Seed Development and Germination, Marcel Dekker, New York, pp. 139-168.
46. Smith, A. M. (1988). Major differences in isoforms of starch-branching enzyme between developing embryos of round and wrinkled-seeded peas (Pisum sativum L.), Planta 175, 270-279.
47. Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985). Measurement of protein using bicinchoninic acid, Anal. Biochem. 150, 76-85.
48. Sogaard, M., Kadziola, A., Haser, R., and Svensson, B. (1993). Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley amylase 1, J. Biol. Chem. 268, 22480-22484.
49. Steiner, K. E., and Preiss, J. (1977). Biosynthesis of bacterial glycogen: Genetic and allosteric regulation of glycogen biosynthesis in Salmonella typhimulium LT-2, J. Bacteriol. 129, 246-253.
50. Suzuki, Y., Ito, N., Yuuku, T., Yamagata, H., and Udaka, S. (1989). Amino acid stabilizing a Bacillus α-amylase against irreversible thermoinactivation, J. Biol. Chem. 264, 18933-18938.
51. Svensson, B. (1994). Protein engineering in the α-amylase family: Catalytic mechanism, substrate specificity, and stability, Plant Mol. Biol. 25, 141-157.
52. Takata, H., Kuriki, T., Okada, S., Takesada, Y., Iizuka, M., Minamiura, N., and Imanaka, T. (1992). Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at α-(1-4)- and α-(1-6)-glucosidic linkages, J. Biol. Chem. 267, 18447-18452.
53. Takeda, Y., Guan, H. P., and Preiss, J. (1993). Branching of amylose by branching isoenzymes of maize endosperm, Carbohydr. Res. 240, 253-263.
54. Vangrysperre, W., Ampe, C., Kersters-Hilderson, H., and Tempst, P. (1989). Single active-site histidine in D-xylose isomerase from Streptomyces violaceoruber, Biochem. J. 263, 195-199.