Identification of essential histidine residues in a recombinant α-amylase of thermophilic and alkaliphilic Bacillus sp. strain TS-23

Extremophiles

Volumn 7, Issue 6, 2003, Pages 505-509

  Chang, Chen Tien ^b   Lo, Huei Fen ^b,c   Chi, Meng Chun ^a   Yao, Chia Yu ^c   Hsu, Wen Hwei ^d   Lin, Long Liu ^a  

^a NATIONAL CHIAYI UNIVERSITY   (Taiwan)

^b PROVIDENCE UNIVERSITY   (Taiwan)

^c HUNGKUANG UNIVERSITY   (Taiwan)

^d NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

Author keywords

Amylase; Bacillus sp. TS 23; Histidine; Site directed mutagenesis

Indexed keywords

BACILLUS SP. TS-23;

AMYLASE; HISTIDINE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; CELL CULTURE; CLASSIFICATION; COMPARATIVE STUDY; CULTURE MEDIUM; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

ALPHA-AMYLASE; AMINO ACID SEQUENCE; BACILLUS; CELLS, CULTURED; CULTURE MEDIA; ENZYME STABILITY; ESCHERICHIA COLI; HISTIDINE; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 4544288389     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-003-0341-8     Document Type: Article

References (35)

1. Amemura A, Chakraborty R, Fujita M, Noumi T, Futai M (1988) Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15. J Biol Chem 263:9271-9275
2. Buisson G, Duée E, Haser R, Payan F (1987) Three-dimensional structure of porcine pancreatine α-amylase at 2.9 Å resolution: role of calcium in structure and activity. EMBO J 6:3909-3916
3. Declerck N, Joyet P, Gaillardin C, Masson JM (1990) Use of amber suppressors to investigate the thermostability of Bacillus licheniformis α-amylase: amino acid replacements at 6 histidine residues reveal a critical position at His-133. J Biol Chem 265:15481-15488
4. Declerck N, Machius M, Wiegand G, Huber R, Gaillardin C (2000) Probing structural determinants specifying high thermostability in Bacillus licheniformis α-amylase. J Mol Biol 301:1041-1057
5. Demirjian DC, Morís-Varas F, Cassidy CS (2001) Enzymes for extremophiles. Curr Opin Chem Biol 5:144-151
6. Hagihara H, Hayashi Y, Endo K, Igarashi K, Ozawa T, Kawai S, Ozaki K, Ito S (2001) Deduced amino-acid sequence of a calcium-free α-amylase from a strain of Bacillus. Eur J Biochem 268:3974-3982
7. Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequences similarities. Biochem J 280: 309-316
8. Igarashi K, Hatada Y, Hagihara H, Saeki K, Takaiwa M, Uemura T, Ara K, Ozaki K, Kawai S, Kobayashi T, Ito S (1998) Enzymatic properties of a novel liquefying α-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences. Appl Environ Microbiol 64:3282-3289
9. Ihara H, Sasaki T, Tsubi A, Yamagata H, Tsukago N, Udata S (1985) Complete nucleotide sequence of a thermophilic α-amylase: homology between prokaryotic and eukaryotic α-amylases at the active sites. J Biochem (Tokyo) 98:95-103
10. Ishikawa K, Matsui I, Honda K, Nakatani H (1992) Multi-functional roles of a histidine residue in human pancreatic α-amylase. Biochem Biophys Res Commun 183:286-291
11. Ishikawa K, Matsui I, Kobayashi S, Nakatani H, Honda K (1993) Substrate recognition at the binding site in mammalian pancreatic α-amylase. Biochemistry 32:6259-6265
12. Ito S, Kobayashi T, Ara K, Ozaki K, Kawai S, Hatada Y (1998) Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures. Extremophiles 2: 185-190
13. Katsuragi N, Takizawa N, Murooka Y (1987) Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70. J Bacteriol 169:2301-2306
14. Kimura K, Kataoka S, Ishii Y, Takano T, Yamane K (1987) Nucleotide sequence of the β-cyclodextrin glucanotransferase gene of alkalophilic Bacillus sp. strain 1011 and similarity of its amino acid sequence to those of α-amylases. J Bacteriol 169:4399-4402
15. Kunkel TA, Roberts JD, Zakour RA (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154:367-382
16. Kuriki T, Imanaka T (1989) Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus. J Gen Microbiol 135:1521-1528
17. Kuriki T, Imanaka T (1999) The concept of the α-amylase family: structural similarity and common catalytic mechanism. J Biosci Bioeng 87: 557-565
18. Lawson CL, van Montfort R, Strokopytov B, Rozeboom HJ, Kalk KH, de Vries G, Penninga D, Dijkhuizen L, Dijkstra BW (1994) Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form. J Mol Biol 236: 590-600
19. Lin LL, Tasu MR, Chu WS (1994) General characteristics of thermostable amylopullulanases and amylases from the alkalophilic Bacillus sp. TS-23. Appl Microbiol Biotechnol 42:51-56
20. Lin LL, Hsu WH, Chu WS (1997) A gene encoding for an α-amylase from thermophilic Bacillus sp. strain TS-23 and its expression in Escherichia coli. J Appl Microbiol 82: 325-334
21. Lo HF, Lin LL, Li CC, Hsu WH, Chang CT (2001) The N-terminal signal sequence and the last 98 amino acids are not essential for the secretion of Bacillus sp. TS-23 α-amylase in Escherichia coli. Curr Microbiol 43: 170-175
22. Machius M, Wiegand G, Huber R (1995) Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J Mol Biol 246: 545-559
23. Matsuura Y, Kusunok M, Harada W, Kakudo M (1984) Structure and possible catalytic residues of Taka-amylase A. J Biochem (Tokyo) 95:697-702
24. Nakamura A, Haga K, Yamane K (1993) Three histidine residues in the active center of cyclodextrin gluconotransferase from alkalophilic Bacillus sp. 1011: effects replacement on pH dependence and transition-state stabilization. Biochemistry 32:6624-6631
25. Nishide T, Emi M, Nakamura Y, Matsubara K (1984) Corrected sequences of cDNAs for human salivary and pancreatic α-amylases. Gene 28:263-270
26. Rogers JC, Millman C (1983) Isolation and sequence analysis of a barley α-amylase cDNA clone. J Biol Chem 258:8169-8174
27. Sahlström S, Bräthen E (1997) Effects of enzyme preparations for baking, mixing time and resting time on bread quality and bread staling. Food Chem 58: 75-80
28. Strokopytov B, Knegtel RMA, Penninga D, Roozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW (1996) Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution: implications for product specificity. Biochemistry 35: 4241-4249
29. Takase K (1994) Site-directed mutagenesis reveals critical importance of the catalytic site in the binding of α-amylase by wheat proteinaceous inhibitor. Biochemistry 33:7925-7930
30. Tseng CC, Miyamoto M, Ramalingam KC, Hemavathy KC, Levine MJ, Ramasubbu N (1999) The roles of histidine residues at the starch-binding site in streptococcal-binding activities of human salivary amylase. Arch Oral Biol 44:119-127
31. Uitdehaag JCM, Mosi R, Kalk KH, van der Veen BA, Dijkhuizen L, Withers SG, Dijkstra BW (1999) X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the α-amylase family. Nat Struct Biol 6: 432-436
32. Vieille C, Zeikus JG. (1996) Thermozymes: identifying molecular determinatants of protein structural and functional stability. Trends Biotechnol 14:183-190
33. Vihinen M, Mäntsälä P (1989) Microbial amylolytic enzymes. Crit Rev Biochem Mol Biol 24: 329-418
34. Watanabe K, Kitamura K, Iha H, Suzuki Y (1990) Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene. Eur J Biochem 192:609-620
35. Watanabe K, Miyake K, Suzuki Y (2001) Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6- glucosidase. Biosci Biotechnol Biochem 65:2058-2064