Altered large-ring cyclodextrin product profile due to a mutation at Tyr-172 in the amylomaltase of Corynebacterium glutamicum

Applied and Environmental Microbiology

Volumn 78, Issue 20, 2012, Pages 7223-7228

  Srisimarat, Wiraya ^a   Kaulpiboon, Jarunee ^b   Krusong, Kuakarun ^a   Zimmermann, Wolfgang ^c   Pongsawasdi, Piamsook ^a  

^a CHULALONGKORN UNIVERSITY   (Thailand)

^b THAMMASAT UNIVERSITY   (Thailand)

^c UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOMALTASE; CORYNEBACTERIUM GLUTAMICUM; DEGREE OF POLYMERIZATION; DISPROPORTIONATION REACTIONS; DISPROPORTIONATIONS; ENZYME CATALYSIS; ENZYME CONCENTRATIONS; HYDROLYSIS ACTIVITY; INCUBATION TIME; MUTATED ENZYMES; PRODUCT PATTERNS; SITE DIRECTED MUTAGENESIS; WILD TYPES;

AMINO ACIDS; CATALYSIS; CLONING; CYCLODEXTRINS; ESCHERICHIA COLI; POLYMERIZATION;

ENZYMES;

4 ALPHA GLUCANOTRANSFERASE; 4 ALPHA-GLUCANOTRANSFERASE; CYCLODEXTRIN; GLYCOGEN DEBRANCHING ENZYME; MUTANT PROTEIN;

BACTERIUM; CATALYSIS; ENZYME ACTIVITY; MUTATION; POLYMERIZATION;

ARTICLE; CHEMISTRY; CORYNEBACTERIUM GLUTAMICUM; ENZYMOLOGY; ESCHERICHIA COLI; GENE VECTOR; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MISSENSE MUTATION; MOLECULAR CLONING; PLASMID;

CLONING, MOLECULAR; CORYNEBACTERIUM GLUTAMICUM; CYCLODEXTRINS; ESCHERICHIA COLI; GENETIC VECTORS; GLYCOGEN DEBRANCHING ENZYME SYSTEM; KINETICS; MUTANT PROTEINS; MUTATION, MISSENSE; PLASMIDS;

CORYNEBACTERIUM GLUTAMICUM; ESCHERICHIA COLI;

EID: 84868367234     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01366-12     Document Type: Article

References (42)

1. Ausubel FM. 1995. Short protocols in molecular biology. John Wiley & Sons, Inc., New York, NY.
2. Barends TRM, et al. Structural influences on product specificity in amylomaltase from Aquifex aeolicus, in press.
3. Barends TRM, et al. 2007. Three-way stabilization of the covalent intermediate in amylomaltase, an _-amylase-like transglycosylase. J. Biol. Chem. 282:17242-17249.
4. Bozonnet S, et al. 2007. The 'pair of sugar tongs' site on the non-catalytic domain C of barley _-amylase participates in substrate binding and activity. FEBS J. 274:5055-5067.
5. Chaplin MF, Kennedy JF. 1994. Carbohydrate analysis: a practical approach, 2nd ed. Oxford University Press Inc., New York, NY.
6. Endo T, Zheng M, Zimmermann W. 2002. Enzymatic synthesis and analysis of large-ring cyclodextrins. Aust. J. Chem. 55:39-48.
7. Reference deleted
8. Fujii K, et al. 2005. Use of random and saturation mutagenesis to improve the properties of Thermus aquaticus amylomaltase for efficient production of cycloamyloses. Appl. Environ. Microbiol. 71:5823-5827.
9. Fujii K, et al. 2007. Function of second glucan binding site including tyrosines 54 and 101 in Thermus aquaticus amylomaltase. J. Biosci. Bioeng. 103:167-173.
10. Fuwa H. 1954. A new method for microdetermination of amylase activity by the use of amylose as the substrate. J. Biochem. 41:583-603.
11. Gessler K, et al. 1999. V-amylose at atomic resolution: X-ray structure of a cycloamylose with 26 glucose residues (cyclomaltohexaicosaose). Proc. Natl. Acad. Sci. U. S. A. 96:4246-4251.
12. Ikeda M, Nakagawa S. 2003. The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appl. Microbiol. Biotechnol. 62:99-109.
13. Jung JH, et al. 2011. Structural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus. Proteins 79:633-644.
14. Kalinowski J, et al. 2003. The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins. J. Biotechnol. 104:5-25.
15. Kaper T, et al. 2007. Identification of acceptor substrate binding subsites +2 and +3 in the amylomaltase from Thermus thermophilus HB8. Biochemistry 46:5261-5269.
16. Kaper T, et al. 2005. Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels. Appl. Environ. Microbiol. 71: 5098-5106.
17. Kelly RM, et al. 2008. Elimination of competing hydrolysis and coupling side reactions of a cyclodextrin glucanotransferase by directed evolution. Biochem. J. 413:517-525.
18. Kitahata S, Murakami H, Okada S. 1989. Purification and some properties of amylomaltase from Escherichia coli IFO 3806. Agric. Biol. Chem. 53:2653-2659.
19. Kitamura S, Nakatani K, Takaha T, Okada S. 1999. Complex formation of large-ring cyclodextrins with iodine in aqueous solution as revealed by isothermal titration calorimetry. Macromol. Rapid. Commun. 20:612-615.
20. Knegtel RMA, et al. 1995. Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain-251 with natural substrates and products. J. Biol. Chem. 270:29256-29264.
21. Koizumi K, Sanbe H, Kubota Y, Terada Y, Takaha T. 1999. Isolation and characterization of cyclic α-(1¡4)-glucans having degrees of polymerization 9-31 and their quantitative analysis by high-performance anionexchange chromatography with pulsed amperometric detection. J. Chromatogr. A 852:407-416.
22. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
23. Lee BH, Oh DK, Yoo SH. 2009. Characterization of 4-α-glucanotransferase from Synechocystis sp. PCC 6803 and its application to various corn starches. N. Biotechnol. 26:29-36.
24. Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M. 2003. Differential regulation of a hyperthermophilic R-amylase with a novel (Ca,Zn) two-metal center by zinc. J. Biol. Chem. 278:9875-9884.
25. Lyhne-Iversen L, Hobley TJ, Kaasgaard SG, Harris P. 2006. Structure of Bacillus halmapalus R-amylase crystallized with and without the substrate analogue acarbose and maltose. Acta Crystallogr. F 62:849-854.
26. Machida S, et al. 2000. Cycloamylose as an efficient artificial chaperone for protein refolding. FEBS Lett. 486:131-135.
27. Miwa I, Okuda J, Maeda K, Okuda G. 1972. Mutarotase effect on colorimetric determination of blood glucose with β-D-glucose oxidase. Clin. Chim. Acta 37:538-540.
28. Nielsen MM, et al. 2009. Two secondary carbohydrate binding sites on the surface of barley R-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules. Biochemistry 48:7686-7697.
29. Oudjeriouat N, et al. 2003. On the mechanism of α-amylase: acarbose and cyclodextrin inhibition of barley amylase isozymes. Eur. J. Biochem. 270:3871-3879.
30. Park JH, et al. 2007. The action mode of Thermus aquaticus YT-1 4-α-glucanotransferase and its chimeric enzymes introduced with starchbinding domain on amylose and amylopectin. Carbohydr. Polym. 67: 164-173.
31. Przylas I, et al. 2000. X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus: implications for the synthesis of large cyclic glucans. Eur. J. Biochem. 267:6903-6913.
32. Robert X, et al. 2003. The structure of barley R-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs. Structure 11:973-984.
33. Schmidt J, John M. 1979. Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glucosyltransferase (D-enzyme) and amylomaltase. Biochim. Biophys. Acta 566:100-114.
34. Sinner M, Puls J. 1978. Non-corrosive dye reagent for detection of reducing sugars in borate complex ion-exchange chromatography. J. Chromatogr. 156:197-204.
35. Srisimarat W. 2010. Characterization of a novel amylomaltase from Corynebacterium glutamicum ATCC 13032. Ph.D. thesis. Chulalongkorn University, Bangkok, Thailand.
36. Srisimarat W, et al. 2011. A novel amylomaltase from Corynebacterium glutamicum and analysis of the large-ring cyclodextrin products. J. Incl. Phenom. Macrocycl. Chem. 70:369-375.
37. Sträter N, et al. 2002. Structural basis of the synthesis of large cycloamyloses by amylomaltase. Biologia 57(Suppl 11):93-99.
38. Takaha T, Smith SM. 1999. The function of 4-α-glucanotransferase and their use for the production of cyclic glucans. Biotechnol. Genet. Eng. Rev. 16:257-280.
39. Takaha T, Yanase M, Takata H, Okada S, Smith SM. 1996. Potato D-enzyme catalyzes the cyclization of amylose to produce cycloamylose, a novel cyclic glucan. J. Biol. Chem. 271:2902-2908.
40. Terada Y, Fujii K, Takaha T, Okada S. 1999. Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose. Appl. Environ. Microbiol. 65:910-915.
41. Tomono K, et al. 2002. Interaction between cycloamylose and various drugs. J. Incl. Phenom. Macrocycl. Chem. 44:267-270.
42. Uitdehagg JCM, Enverink GJ, van der Veen BA, van der Maarel M, Dijkstra BW. Structure and mechanism of the amylomaltase from Thermus thermophilus HB8, in press.