Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme

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Published inApplied and Environmental Microbiology Vol. 58; no. 12; pp. 4016 - 4025
Main Authors Fujiwara, S, Kakihara, H, Woo, K B, Lejeune, A, Kanemoto, M, Sakaguchi, K, Imanaka, T
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.12.1992
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Abstract Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue AEM About AEM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy AEM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0099-2240 Online ISSN: 1098-5336 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to AEM .asm.org, visit: AEM       
AbstractList Cyclodextrin glucanotransferase (CGTase; EC 2.4.1.19) is produced mainly by Bacillus strains. CGTase from Bacillus macerans IFO3490 produces alpha-cyclodextrin as the major hydrolysis product from starch, whereas thermostable CGTase from Bacillus stearothermophilus NO2 produces alpha- and beta-cyclodextrins. To analyze the cyclization characteristics of CGTase, we cloned different types of CGTase genes and constructed chimeric genes. CGTase genes from these two strains were cloned in Bacillus subtilis NA-1 by using pTB523 as a vector plasmid, and their nucleotide sequences were determined. Three CGTase genes (cgt-1, cgt-5, and cgt-232) were isolated from B. stearothermophilus NO2. Nucleotide sequence analysis revealed that the three CGTase genes have different nucleotide sequences encoding the same amino acid sequence. Base substitutions were found at the third letter of five codons among the three genes. Each open reading frame was composed of 2,133 bases, encoding 711 amino acids containing 31 amino acids as a signal sequence. The molecular weight of the mature enzyme was estimated to be 75,374. The CGTase gene (cgtM) of B. macerans IFO3490 was composed of 2,142 bases, encoding 714 amino acids containing 27 residues as a signal sequence. The molecular weight of the mature enzyme was estimated to be 74,008. The sequence determined in this work was quite different from that reported previously by other workers. From data on the three-dimensional structure of a CGTase, seven kinds of chimeric CGTase genes were constructed by using cgt-1 from B. stearothermophilus NO2 and cgtM from B. macerans IFO3490. We examined the characteristics of these chimeric enzymes on cyclodextrin production and thermostability. It was found that the cyclization reaction was conferred by the NH2-terminal region of CGTase and that the thermostability of some chimeric enzymes was lower than that of the parental CGTases.
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Author T Imanaka
K B Woo
A Lejeune
M Kanemoto
H Kakihara
S Fujiwara
K Sakaguchi
AuthorAffiliation Department of Biotechnology, Faculty of Engineering, Osaka University, Japan
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References 2137908 - Nucleic Acids Res. 1990 Jan 11;18(1):199
2972812 - J Gen Microbiol. 1988 Jan;134(1):97-105
3843705 - Anal Biochem. 1985 Oct;150(1):76-85
6678612 - Cell. 1983 May;33(1):53-63
6310323 - Methods Enzymol. 1983;101:20-78
6181373 - Mol Gen Genet. 1982;186(3):339-46
6343825 - Microbiol Rev. 1983 Mar;47(1):1-45
5916452 - Sci Am. 1966 Oct;215(4):55-60 passim
6277855 - J Bacteriol. 1982 Mar;149(3):824-30
6268607 - J Bacteriol. 1981 Sep;147(3):776-86
3530497 - Cell. 1986 Sep 12;46(6):921-8
5420325 - J Mol Biol. 1970 Mar;48(3):443-53
2671995 - Proc Natl Acad Sci U S A. 1989 Sep;86(17):6562-6
3323803 - Methods Enzymol. 1987;153:3-11
6099249 - Cold Spring Harb Symp Quant Biol. 1984;49:401-9
271968 - Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7
6609921 - J Biochem. 1984 Mar;95(3):697-702
3127377 - J Bacteriol. 1988 Apr;170(4):1554-9
518863 - Biochemistry. 1979 Dec 11;18(25):5698-703
2524186 - Biochem J. 1989 Apr 1;259(1):145-52
2748349 - Nucleic Acids Res. 1989 Jun 26;17(12):4895
3011735 - J Bacteriol. 1986 Jun;166(3):1118-22
1368519 - Agric Biol Chem. 1990 Jan;54(1):197-201
7338898 - J Mol Biol. 1981 Sep 15;151(2):261-87
13738459 - Biochem Biophys Res Commun. 1961 May 15;5:11-5
344137 - Gene. 1977;2(2):95-113
2482332 - J Gen Microbiol. 1989 Jun;135(6):1521-8
3930658 - J Gen Microbiol. 1985 Jul;131(7):1753-63
5432063 - Nature. 1970 Aug 15;227(5259):680-5
2525902 - Biochem Biophys Res Commun. 1989 Jun 30;161(3):1273-9
7462208 - J Biochem. 1980 Dec;88(6):1895-8
1368573 - Appl Microbiol Biotechnol. 1990 Aug;33(5):542-6
2530917 - Anal Biochem. 1989 Aug 15;181(1):6-11
6387910 - Science. 1984 Nov 2;226(4674):555-7
2993245 - J Bacteriol. 1985 Sep;163(3):824-31
2957361 - J Bacteriol. 1987 Sep;169(9):4399-402
2481445 - Biochem J. 1989 Nov 15;264(1):309-11
1826034 - J Mol Biol. 1991 Feb 20;217(4):737-50
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Cyclodextrin glucanotransferase (CGTase; EC 2.4.1.19) is produced mainly by Bacillus strains. CGTase from Bacillus macerans IFO3490 produces alpha-cyclodextrin...
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SubjectTerms Amino Acid Sequence
Bacillus - enzymology
Bacillus - genetics
Base Sequence
Cloning, Molecular
DNA, Bacterial - genetics
Genes, Bacterial
Geobacillus stearothermophilus - enzymology
Geobacillus stearothermophilus - genetics
Glucosyltransferases - chemistry
Glucosyltransferases - genetics
Glucosyltransferases - ultrastructure
Molecular Sequence Data
Molecular Structure
Protein Conformation
Title Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme
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