Functional characteristics of C-terminal regions of starch-branching enzymes from developing seeds of kidney bean (Phaseolus vulgaris L.)

Plant Science

Volumn 166, Issue 5, 2004, Pages 1149-1158

  Ito, Hiroyuki ^a   Hamada, Shigeki ^a   Isono, Naoto ^a   Yoshizaki, Takayuki ^a   Ueno, Hiroshi ^a   Yoshimoto, Yasushi ^b   Takeda, Yasuhito ^b   Matsui, Hirokazu ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b KAGOSHIMA UNIVERSITY   (Japan)

Author keywords

BE; Branching enzyme; Degree of polymerization; Dp; High performance anion exchange chromatography pulsed amperometric detector; HPAEC PAD; Kidney bean (Phaseolus vulgaris L.) starch branching enzyme; PvSBE; Recombinant PvSBE; rPvSBE; SBE

Indexed keywords

BIOCHEMISTRY; ENZYMES; REACTION KINETICS; STARCH;

KIDNEY BEANS; PLANT STARCH BRANCHING ENZYMES;

PLANTS (BOTANY);

PHASEOLUS VULGARIS;

EID: 1842788556     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2003.12.019     Document Type: Article

References (36)

1. Borovsky D., Smith E.E., Whelan W.J. On the mechanism of amylose branching by potato Q-enzyme. Eur. J. Biochem. 62:1976;307-312.
2. Boyer C.D., Preiss J. Evidence for independent genetic control of the multiple forms of maize endosperm starch branching enzymes and starch synthases. Plant Physiol. 67:1981;1141-1145.
3. Kim K.N., Fisher D.K., Gao M., Guiltinan M.J. Molecular cloning and characterization of the Amylose-Extender gene encoding starch branching enzyme IIB in maize. Plant Mol. Biol. 38:1998;945-956.
4. Mizuno K., Kawasaki T., Shimada H., Satoh H., Kobayashi E., Okumura S., Arai Y., Baba T. Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds. J. Biol. Chem. 268:1993;19084-19091.
5. Bhattacharyya M.K., Smith A.M., Ellis T.H.N., Hedley C., Martin C. The wrinkled-seed character of pea described by Mendel is caused by a transposon-like insertion in a gene encoding starch-branching enzyme. Cell. 60:1990;115-122.
6. Burton R.A., Bewley J.D., Smith A.M., Bhattacharyya M.K., Tatge H., Ring S., Bull V., Hamilton W.D.O., Martin C. Starch branching enzymes belonging to distinct enzyme families are deferentially expressed during pea embryo development. Plant J. 7:1995;3-15.
7. Hamada S., Nozaki K., Ito H., Yoshimoto Y., Yoshida H., Hiraga S., Onodera S., Honma M., Takeda Y., Matsui H. Two starch-branching-enzyme isoforms occur in different fractions of developing seeds of kidney bean. Biochem. J. 359:2001;23-34.
8. Janecek S., Svensson B., MacGregor E.A. Relation between domain evolution, specificity, and taxonomy of the α-amylase family members containing a C-terminal starch-binding domain. Eur. J. Biochem. 270:2003;635-645.
9. Takata H., Kuriki T., Okada S., Takesada Y., Iizuka M., Minamiura N., Imanaka T. Action of neopullulanase: neopullulanase catalyzes both hydrolysis and transglycosylation at α-(1 → 4)- and α-(1 → 6)-glucosidic linkages. J. Biol. Chem. 267:1992;18447-18452.
10. 8-barrel domain and evolutionary relationship to other amylolytic enzymes. J. Prot. Chem. 12:1993;791-805.
11. Abad M.C., Binderup K., Rkos-Steiner J., Arni R.K., Preiss J., Geiger J.H. The X-ray crystallographic structure of Escherichia coli branching enzyme. J. Biol. Chem. 277:2002;42164-42170.
12. Hondoh H., Kuriki T., Matsuura Y. Three-dimensional structure and substrate binding of Bacillus stearothermophilus Neopullulanase. J. Mol. Biol. 326:2003;177-188.
13. Katsuya Y., Mezaki Y., Kubota M., Matsuura Y. Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolution. J. Mol. Biol. 281:1998;885-897.
14. Kamitori S., Abe A., Ohtaki A., Kaji A., Tonozuka T., Sakano Y. Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 α-amylase 1 (TVAI) at 1.6 Å resolution and α-amylase 2 (TVAII) at 2.3 Å resolution. J. Mol. Biol. 318:2002;443-453.
15. Yokota T., Tonozuka T., Kamitori S., Sakano Y. The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 α-amylases: effect of domain N on activity, specificity, stability and dimerization. Biosci. Biotechnol. Biochem. 65:2001;401-408.
16. Binderup K., Mikkelsen R., Preiss J. Truncation of the amino terminus of branching enzyme changes its chain transfer pattern. Arch. Biochem. Biophys. 397:2002;279-285.
17. Devillers C.H., Piper M.E., Ballicora M.A., Preiss J. Characterization of the branching patters of glycogen branching enzyme truncated on the N-terminus. Arch. Biochem. Biophys. 418:2003;34-38.
18. Svensson B., Jespersen H., Sierks M.R., MacGregor E.A. Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochem. J. 264:1989;309-311.
19. Janecek S., Sevcik J. The evolution of starch-binding domain. FEBS Lett. 456:1999;119-125.
20. Kuriki T., Stewart D.C., Preiss J. Construction of chimeric enzymes out of maize endosperm branching enzyme I and II: activity and properties. J. Biol. Chem. 272:1997;28999-29004.
21. Hong S., Preiss J. Localization of C-terminal domains required for the maximal activity or for determination of substrate preference of maize branching enzymes. Arch. Biochem. Biophys. 378:2000;349-355.
22. Nozaki K., Hamada S., Nakamori T., Ito H., Sagisaka S., Yoshida H., Takeda Y., Honma M., Matsui H. Major isoforms of starch branching enzymes in premature seeds of kidney bean (Phaseolus vulgaris L.). Biosci. Biotech. Biochem. 65:2001;1141-1148.
23. Boyer C.D., Preiss J. Multiple forms of (1 → 4)-α-D-glucan, (1 → 4)-α-D-glucan-6-glycosyl transferase from developing Zea mays L. kernels. Carbohydr. Res. 61:1978;321-334.
24. Takeda Y., Guan H.P., Preiss J. Branching of amylose by branching isoenzymes of maize endosperm. Carbohydr. Res. 240:1993;253-263.
25. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
26. Hanashiro I., Abe J., Hizukuri S. A periodic distribution of the chain length of amylopectin as revealed by high-performance anion-exchange chromatography. Carbohydr. Res. 283:1996;151-159.
27. Tomlinson K.L., Lloyd J.R., Smith A.M. Importance of isoforms of starch-branching enzyme in determining the structure of starch in pea leaves. Plant J. 11:1997;31-43.
28. Matsuura Y., Kusunoki M., Harada W., Kakudo M. Structure and possible catalytic residues of Taka-amylase A. J. Biochem. (Tokyo). 95:1984;697-702.
29. Klein C., Schulz G.E. Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution. J. Mol. Biol. 217:1991;737-750.
30. Edwards A., Borthakur A., Bornemann S., Venail J., Denyer K., Waite D., Fulton D., Smith A., Martin C. Specificity of starch synthase isoforms from potato. Eur. J. Biochem. 266:1999;724-736.
31. Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins. 19:1994;55-72.
32. Garnier J., Gibrat J.-F. GOR secondary structure prediction method version IV. Methods Enzymol. 266:1996;540-553.
33. Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:1999;195-202.
34. Cuff J.A., Barton G.J. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins. 40:2000;502-511.
35. Guan H., Li P., Imparl-Radosevich J., Preiss J., Keeling P. Comparing the properties of Escherichia coli branching enzyme and maize branching enzyme. Arch. Biochem. Biophys. 342:1997;92-98.
36. Ji Q., Vincken J.-P., Suurs L.C.J.M., Visser G.F. Microbial starch-binding domains as a tool for targeting proteins to granules during starch biosynthesis. Plant Mol. Biol. 51:2003;789-801.