메뉴 건너뛰기




Volumn 20, Issue 1, 2003, Pages 69-78

Cloning and characterization of a second α-amylase gene (LKA2) from Lipomyces kononenkoae IGC4052B and its expression in Saccharomyces cerevisiae

Author keywords

Amylase; Lipomyces kononenkoae; LKA2; Saccharomyces cerevisiae

Indexed keywords

AMINO ACID; AMYLASE; BACTERIAL ENZYME; COMPLEMENTARY DNA; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; FUNGAL PROTEIN; GLUCAN 1,4 ALPHA GLUCOSIDASE; NUCLEOTIDE; PHOSPHOGLYCERATE KINASE; STARCH;

EID: 0037438660     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/yea.934     Document Type: Review
Times cited : (18)

References (40)
  • 1
    • 0025816093 scopus 로고
    • Construction of a Saccharomyces cerevisiae strain able to ferment cellobiose
    • Adam AC, Polaina J. 1991. Construction of a Saccharomyces cerevisiae strain able to ferment cellobiose. Curr Genet 20: 5-8.
    • (1991) Curr. Genet. , vol.20 , pp. 5-8
    • Adam, A.C.1    Polaina, J.2
  • 2
    • 0023661282 scopus 로고
    • Three-dimensional structure of porcine pancreatic α-amylase at 2.9 Å resolution. Role of calcium in structure and activity
    • Buisson G, Duee E, Haser R, 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.
    • (1987) EMBO J. , vol.6 , pp. 3909-3916
    • Buisson, G.1    Duee, E.2    Haser, R.3    Payan, F.4
  • 3
    • 0031201675 scopus 로고    scopus 로고
    • Molecular mechanism in α-glucosidase and glucoamylase
    • Chiba S. 1997. Molecular mechanism in α-glucosidase and glucoamylase. Biosci Biotech Biochem 61: 1233-1239.
    • (1997) Biosci. Biotech. Biochem. , vol.61 , pp. 1233-1239
    • Chiba, S.1
  • 4
    • 21844507627 scopus 로고
    • Purification and characterization of two extracellular glucoamylase isozymes from Lipomyces kononenkoae CBS5608 mutant
    • Chun SB, Bai S, Im SY, Choi WK, Lee JJ. 1995. Purification and characterization of two extracellular glucoamylase isozymes from Lipomyces kononenkoae CBS5608 mutant. J Biochem Mol Biol 48: 375-381.
    • (1995) J. Biochem. Mol. Biol. , vol.48 , pp. 375-381
    • Chun, S.B.1    Bai, S.2    Im, S.Y.3    Choi, W.K.4    Lee, J.J.5
  • 5
    • 0027202325 scopus 로고
    • Molecular structure of the SWA2 gene encoding an AMY1-related α-amylase from Schwanniomyces occidentales
    • Claros MG, Abarca D, Fernandex-Lobato M, Jimenez A. 1993. Molecular structure of the SWA2 gene encoding an AMY1-related α-amylase from Schwanniomyces occidentales. Curr Genet 24: 75-83.
    • (1993) Curr. Genet. , vol.24 , pp. 75-83
    • Claros, M.G.1    Abarca, D.2    Fernandex-Lobato, M.3    Jimenez, A.4
  • 6
    • 0028805858 scopus 로고
    • Cloning and expression of an Aspergillus kawachii endo-1,4-,β-xylanase gene in Saccharomyces cerevisiae
    • Crous JM, Pretorius IS, Van Zyl WH. 1995. Cloning and expression of an Aspergillus kawachii endo-1,4-,β-xylanase gene in Saccharomyces cerevisiae. Curr Genet 28: 467-473.
    • (1995) Curr. Genet. , vol.28 , pp. 467-473
    • Crous, J.M.1    Pretorius, I.S.2    Van Zyl, W.H.3
  • 7
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smithies O. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12: 387-394.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-394
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 8
    • 0023948010 scopus 로고
    • High efficiency transformation of Escherichia coli by high voltage electroporation
    • Dower WJ, Miller JF, Ragsdale CW. 1988. High efficiency transformation of Escherichia coli by high voltage electroporation. Nucleic Acids Res 16: 6127.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 9
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D, St Jean A, Woods RA, Schiestl RH. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20: 1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 10
    • 0033998979 scopus 로고    scopus 로고
    • Review: Cyclodextrins and their interaction with amylolytic enzymes
    • Hamilton LM, Kelly CT, Fogarty WM. 2000. Review: cyclodextrins and their interaction with amylolytic enzymes. Enzyme Microb Technol 26: 561-567.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 561-567
    • Hamilton, L.M.1    Kelly, C.T.2    Fogarty, W.M.3
  • 11
    • 0023663451 scopus 로고
    • Compilation and comparison of the sequence context around the AUG start codons in Saccharomyces cerevisiae mRNAs
    • Hamilton R, Watanabe CK, De Boer HA. 1987. Compilation and comparison of the sequence context around the AUG start codons in Saccharomyces cerevisiae mRNAs. Nucleic Acids Res 15: 3581-3593.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 3581-3593
    • Hamilton, R.1    Watanabe, C.K.2    De Boer, H.A.3
  • 12
    • 0019186616 scopus 로고
    • A small cosmid for efficient cloning of large DNA fragments
    • Hohn B, Collins J. 1980. A small cosmid for efficient cloning of large DNA fragments. Gene 11: 291-298.
    • (1980) Gene , vol.11 , pp. 291-298
    • Hohn, B.1    Collins, J.2
  • 13
    • 0025239538 scopus 로고
    • Random mutagenesis used to probe structure and function of Bacillus stearothermophilus α-amylase
    • Holm L, Koivula AK, Lehtovaara PM, Hemminki A, Knowles JK. 1990. Random mutagenesis used to probe structure and function of Bacillus stearothermophilus α-amylase. Protein Eng 3: 181-191.
    • (1990) Protein Eng. , vol.3 , pp. 181-191
    • Holm, L.1    Koivula, A.K.2    Lehtovaara, P.M.3    Hemminki, A.4    Knowles, J.K.5
  • 14
    • 0002000552 scopus 로고
    • A comparative study of the amylolytic ability of Lipomyces and Schwanniomyces yeast species
    • Horn CH, De Kock A, Du Preez JC, Lategan PM. 1988. A comparative study of the amylolytic ability of Lipomyces and Schwanniomyces yeast species. System Appl Microbiol 10: 106-110.
    • (1988) System Appl. Microbiol. , vol.10 , pp. 106-110
    • Horn, C.H.1    De Kock, A.2    Du Preez, J.C.3    Lategan, P.M.4
  • 15
    • 0023406627 scopus 로고
    • Nucleotide sequence of the glucoamylase gene GLU1 in the yeast Saccharomycopsis fibuligera
    • Itoh T, Ohtsuki I, Yamashita I, Fukui S. 1987. Nucleotide sequence of the glucoamylase gene GLU1 in the yeast Saccharomycopsis fibuligera. J Bacteriol 169: 4171-4176.
    • (1987) J. Bacteriol. , vol.169 , pp. 4171-4176
    • Itoh, T.1    Ohtsuki, I.2    Yamashita, I.3    Fukui, S.4
  • 16
    • 0027453939 scopus 로고
    • Regional sequence homologies in starch-degrading enzymes
    • Janse BJH, Steyn AJC, Pretorius IS. 1993. Regional sequence homologies in starch-degrading enzymes. Curr Genet 24: 400-407.
    • (1993) Curr. Genet. , vol.24 , pp. 400-407
    • Janse, B.J.H.1    Steyn, A.J.C.2    Pretorius, I.S.3
  • 17
    • 0035008872 scopus 로고    scopus 로고
    • New ways of initiating translation in eukaryotes?
    • Kozak M. 2001. New ways of initiating translation in eukaryotes? Mol Cell Biol 21: 1899-1907.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 1899-1907
    • Kozak, M.1
  • 18
    • 0001785242 scopus 로고
    • A new concept of the criteria for classification of various amylolytic enzymes and related enzymes, similarities in specificities and structures
    • Takehiko Y (ed.). CRC Press: Boca Raton, FL
    • Kuriki T, Okada S. 1995. A new concept of the criteria for classification of various amylolytic enzymes and related enzymes, similarities in specificities and structures. In Enzyme Chemistry and Molecular Biology of Amylases and Related Enzymes, Takehiko Y (ed.). CRC Press: Boca Raton, FL; 87-92.
    • (1995) Enzyme Chemistry and Molecular Biology of Amylases and Related Enzymes , pp. 87-92
    • Kuriki, T.1    Okada, S.2
  • 20
    • 0021548907 scopus 로고
    • DNA base sequence complementarity and the definition of fungal taxa
    • Kurtzman CP. 1984. DNA base sequence complementarity and the definition of fungal taxa. Microbiol Sci 1: 44-48.
    • (1984) Microbiol. Sci. , vol.1 , pp. 44-48
    • Kurtzman, C.P.1
  • 21
    • 0027759277 scopus 로고
    • Elements of the yeast pheromone response pathway required for filamentous growth of diploids
    • Liu H, Styles CA, Fink GR. 1993. Elements of the yeast pheromone response pathway required for filamentous growth of diploids. Science 262: 1741-1744.
    • (1993) Science , vol.262 , pp. 1741-1744
    • Liu, H.1    Styles, C.A.2    Fink, G.R.3
  • 22
    • 0026628162 scopus 로고
    • Alteration of bond-cleavage pattern in the hydrolysis catalyzed by Saccharomycopsis α-amylase altered by site-directed mutagenesis
    • Matsui I, Ishikawa K, Miyairi S, Fukui S, Honda K. 1992. Alteration of bond-cleavage pattern in the hydrolysis catalyzed by Saccharomycopsis α-amylase altered by site-directed mutagenesis. Biochemistry 31: 5232-5236.
    • (1992) Biochemistry , vol.31 , pp. 5232-5236
    • Matsui, I.1    Ishikawa, K.2    Miyairi, S.3    Fukui, S.4    Honda, K.5
  • 24
    • 0026522467 scopus 로고
    • Architectural features of pre-mRNA introns in the fission yeast Schizosaccharomyces pombe
    • Prabhala G, Rosenberg GH, Kaufer NF. 1992. Architectural features of pre-mRNA introns in the fission yeast Schizosaccharomyces pombe. Yeast 8: 171-182.
    • (1992) Yeast , vol.8 , pp. 171-182
    • Prabhala, G.1    Rosenberg, G.H.2    Kaufer, N.F.3
  • 25
    • 0029186962 scopus 로고
    • Purification and characterization of a new α-amylase of intermediate thermal stability from the yeast Lipomyces kononenkoae
    • Prieto JA, Bort BR, Martínez J, Randez-Gil F, Buesa C, Sanz P. 1995. Purification and characterization of a new α-amylase of intermediate thermal stability from the yeast Lipomyces kononenkoae. Biochem Cell Biol 73: 41-49.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 41-49
    • Prieto, J.A.1    Bort, B.R.2    Martínez, J.3    Randez-Gil, F.4    Buesa, C.5    Sanz, P.6
  • 27
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski RS, Hieter P. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 28
    • 14744286169 scopus 로고
    • Electrospray mass spectrometry characterization of posttranslational modifications of barley α-amylase 1 produced in yeast
    • Søogaard M, Andersen JS, Roepstorff P, Svensson B. 1993. Electrospray mass spectrometry characterization of posttranslational modifications of barley α-amylase 1 produced in yeast. Biotechnology 11: 1162-1165.
    • (1993) Biotechnology , vol.11 , pp. 1162-1165
    • Søogaard, M.1    Andersen, J.S.2    Roepstorff, P.3    Svensson, B.4
  • 30
    • 0018410152 scopus 로고
    • Extracellular amylolytic system of the yeast Lipomyces kononenkoae
    • Spencer-Martins I, Van Uden N. 1979. Extracellular amylolytic system of the yeast Lipomyces kononenkoae. Eur J Appl Microbiol 6: 241-250.
    • (1979) Eur. J. Appl. Microbiol. , vol.6 , pp. 241-250
    • Spencer-Martins, I.1    Van Uden, N.2
  • 31
    • 0020371909 scopus 로고
    • Extracellular isoamylase produced by the yeast Lipomyces kononenkoae
    • Spencer-Martins I. 1982. Extracellular isoamylase produced by the yeast Lipomyces kononenkoae. Appl Environ Microbiol 44: 1253-1257.
    • (1982) Appl. Environ. Microbiol. , vol.44 , pp. 1253-1257
    • Spencer-Martins, I.1
  • 32
    • 0012395778 scopus 로고
    • Production and properties of an extracellular cyclodextrin hydrolase from the yeast Lipomyces kononenkoae
    • Spencer-Martins I. 1984. Production and properties of an extracellular cyclodextrin hydrolase from the yeast Lipomyces kononenkoae. Int J Microbiol 2: 31-38.
    • (1984) Int. J. Microbiol. , vol.2 , pp. 31-38
    • Spencer-Martins, I.1
  • 33
    • 0028884418 scopus 로고
    • Cloning, sequence analysis and expression in yeast of a cDNA containing a Lipomyces kononenkoae α-amylase-encoding gene
    • Steyn AJC, Marmur J, Pretorius IS. 1995. Cloning, sequence analysis and expression in yeast of a cDNA containing a Lipomyces kononenkoae α-amylase-encoding gene. Gene 166: 65-71.
    • (1995) Gene , vol.166 , pp. 65-71
    • Steyn, A.J.C.1    Marmur, J.2    Pretorius, I.S.3
  • 34
    • 0029770112 scopus 로고    scopus 로고
    • Cloning, mapping and characterization of a genomic copy of Lipomyces kononenkoae
    • Steyn AJC, Marmur J, Pretorius IS. 1996. Cloning, mapping and characterization of a genomic copy of Lipomyces kononenkoae. Yeast 12: 925-937.
    • (1996) Yeast , vol.12 , pp. 925-937
    • Steyn, A.J.C.1    Marmur, J.2    Pretorius, I.S.3
  • 35
    • 0028860703 scopus 로고
    • Characterization of a novel α-amylase from Lipomyces kononenkoae and expression of its gene (LKA1) in Saccharomyces cerevisiae
    • Steyn AJC, Pretorius IS. 1995. Characterization of a novel α-amylase from Lipomyces kononenkoae and expression of its gene (LKA1) in Saccharomyces cerevisiae. Curr Genet 28: 526-533.
    • (1995) Curr. Genet. , vol.28 , pp. 526-533
    • Steyn, A.J.C.1    Pretorius, I.S.2
  • 36
    • 0024746996 scopus 로고
    • Analysis of the α-amylase gene of Schwanniomyces occidentalis and the secretion of its gene product in transformants of different yeast genera
    • Strasser AWM, Selk R, Dohmen RJ, et al. 1989. Analysis of the α-amylase gene of Schwanniomyces occidentalis and the secretion of its gene product in transformants of different yeast genera. Eur J Biochem 184: 699-706.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 699-706
    • Strasser, A.W.M.1    Selk, R.2    Dohmen, R.J.3
  • 37
    • 0023645671 scopus 로고
    • Crystallization of barley malt α-amylases and preliminary X-ray diffraction studies of the high pI isozyme, α-amylase 2
    • Svensson B, Gibson RM, Haser R, Astier JP. 1987. Crystallization of barley malt α-amylases and preliminary X-ray diffraction studies of the high pI isozyme, α-amylase 2. J Biochem 262: 13682-13684.
    • (1987) J. Biochem. , vol.262 , pp. 13682-13684
    • Svensson, B.1    Gibson, R.M.2    Haser, R.3    Astier, J.P.4
  • 38
    • 84985702845 scopus 로고
    • Selective isolation of derepressed mutants of an α-amylase yeast by the use of 2-deoxyglucose
    • Van Uden N, Cabeca-Silva C, Madeira-Lopes A, Spencer-Martins I. 1980. Selective isolation of derepressed mutants of an α-amylase yeast by the use of 2-deoxyglucose. Biotechnol Bioeng 22: 651-654.
    • (1980) Biotechnol. Bioeng. , vol.22 , pp. 651-654
    • Van Uden, N.1    Cabeca-Silva, C.2    Madeira-Lopes, A.3    Spencer-Martins, I.4
  • 39
    • 0020108296 scopus 로고
    • DNA sequence required for efficient transcription termination in yeast
    • Zaret KS, Sherman F. 1982. DNA sequence required for efficient transcription termination in yeast. Cell 28: 563-573.
    • (1982) Cell , vol.28 , pp. 563-573
    • Zaret, K.S.1    Sherman, F.2
  • 40
    • 0028233256 scopus 로고
    • Fission yeast gene structure and recognition
    • Zhang MQ, Marr TG. 1994. Fission yeast gene structure and recognition. Nucleic Acids Res 22: 1750-1759.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1750-1759
    • Zhang, M.Q.1    Marr, T.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.