메뉴 건너뛰기




Volumn 259, Issue 2, 2006, Pages 240-248

Cloning, expression and characterization of an extracellular enolase from Leuconostoc mesenteroides

Author keywords

2 phospho D glucose; Cloning; Enolase; Expression; Leuconostoc mesenteroides; Phosphoenolpyruvate

Indexed keywords

BACTERIAL ENZYME; DEXTRANSUCRASE; ENOLASE; FLUORIDE; PHOSPHATE; PHOSPHOENOLPYRUVATE; PLASMINOGEN;

EID: 33744820300     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2006.00274.x     Document Type: Article
Times cited : (18)

References (46)
  • 2
    • 0022553595 scopus 로고    scopus 로고
    • Some aspects of the pneumococcal carrier state
    • Austrian R 1996 Some aspects of the pneumococcal carrier state. J Antimicrob Chemother 18: 35 45.
    • (1996) J Antimicrob Chemother , vol.18 , pp. 35-45
    • Austrian, R.1
  • 3
    • 0034931519 scopus 로고    scopus 로고
    • α-enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann S, Rohde M, Chhatwal GS Hammerschmidt S 2001 α-enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40: 1273 1287.
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 4
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plamin(ogen)-binding motif in surface displayed α-enolase of Streptococcus pneumoniae
    • Bergmann S, Wild D, Diekmann O, Frank R, Bracht D, Chhatwal GS Hammerschmidt S 2003 Identification of a novel plamin(ogen)-binding motif in surface displayed α-enolase of Streptococcus pneumoniae. Mol Microbiol 49: 411 423.
    • (2003) Mol Microbiol , vol.49 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3    Frank, R.4    Bracht, D.5    Chhatwal, G.S.6    Hammerschmidt, S.7
  • 6
    • 0021960451 scopus 로고
    • Specificity and mechanism of action of metal ions in yeast enolase
    • Brewer JM 1985 Specificity and mechanism of action of metal ions in yeast enolase. FEBS Lett 182: 8 14.
    • (1985) FEBS Lett , vol.182 , pp. 8-14
    • Brewer, J.M.1
  • 7
    • 0032422012 scopus 로고    scopus 로고
    • A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis
    • Brown CK, Kuhlman PL, Mattingly S, Sates K, Calie PJ Farrar WW 1998a A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis. J Protein Chem 17: 855 866.
    • (1998) J Protein Chem , vol.17 , pp. 855-866
    • Brown, C.K.1    Kuhlman, P.L.2    Mattingly, S.3    Sates, K.4    Calie, P.J.5    Farrar, W.W.6
  • 8
    • 0032422012 scopus 로고    scopus 로고
    • A model of the quaternary structure of enolases based on structural and evolutionary analysis of the octameric enolase Bacillus subtilis
    • Brown CK, Kuhlman PL, Mattingly S, Slates K, Calie PJ Farrar WW 1998b A model of the quaternary structure of enolases based on structural and evolutionary analysis of the octameric enolase Bacillus subtilis. J Prot Chem 17: 855 866.
    • (1998) J Prot Chem , vol.17 , pp. 855-866
    • Brown, C.K.1    Kuhlman, P.L.2    Mattingly, S.3    Slates, K.4    Calie, P.J.5    Farrar, W.W.6
  • 9
    • 0015385368 scopus 로고
    • Non-chromosomal antibiotic resistance in bacteria
    • genetic transformation of Escherichia coli by R-factor DNA.
    • Cohen SN, Chang ACY Hsu L 1973 Non-chromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci USA 69: 2110 2114.
    • (1973) Proc Natl Acad Sci USA , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.Y.2    Hsu, L.3
  • 10
    • 0029165459 scopus 로고
    • Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor
    • Cundell DR, Gerard NP, Gerard C, Idanpaan-Heikkila I Tuomanen EI 1995 Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor. Nature 377: 435 438.
    • (1995) Nature , vol.377 , pp. 435-438
    • Cundell, D.R.1    Gerard, N.P.2    Gerard, C.3    Idanpaan-Heikkila, I.4    Tuomanen, E.I.5
  • 13
    • 0025766291 scopus 로고
    • Miniaturization of three dextran synthesis by using a microsample plate reader
    • Fox JD Robyt JF 1991 Miniaturization of three dextran synthesis by using a microsample plate reader. Anal Biochem 195: 93 96.
    • (1991) Anal Biochem , vol.195 , pp. 93-96
    • Fox, J.D.1    Robyt, J.F.2
  • 14
    • 73049131538 scopus 로고
    • The isolation and characterization of rabbit muscle enolase
    • Holt A Wold F 1961 The isolation and characterization of rabbit muscle enolase. J Biol Chem 236: 3227 3231.
    • (1961) J Biol Chem , vol.236 , pp. 3227-3231
    • Holt, A.1    Wold, F.2
  • 15
    • 0025217794 scopus 로고
    • Isolation, characterization and inhibition kinetics of enolase from Streptococcus rattus FA-1
    • Hüther FJ, Psarros N Duschner H 1990 Isolation, characterization and inhibition kinetics of enolase from Streptococcus rattus FA-1. Infect Immun 58: 1043 1047.
    • (1990) Infect Immun , vol.58 , pp. 1043-1047
    • Hüther, F.J.1    Psarros, N.2    Duschner, H.3
  • 16
    • 0026586872 scopus 로고
    • Purification, characterization and inhibition by fluoride of enolase from Streptococcus mutans DSM 320523
    • Kaufmann M Bartholmes P 1992 Purification, characterization and inhibition by fluoride of enolase from Streptococcus mutans DSM 320523. Caries Res 26: 110 116.
    • (1992) Caries Res , vol.26 , pp. 110-116
    • Kaufmann, M.1    Bartholmes, P.2
  • 17
    • 0032907581 scopus 로고    scopus 로고
    • Facile purification and characterization of dextransucrase from Leuconostoc mesenteroides B-512FMCM
    • Kim D Kim DW 1999 Facile purification and characterization of dextransucrase from Leuconostoc mesenteroides B-512FMCM. J Microbiol Biotechnol 9: 219 223.
    • (1999) J Microbiol Biotechnol , vol.9 , pp. 219-223
    • Kim, D.1    Kim, D.W.2
  • 18
    • 0030917509 scopus 로고    scopus 로고
    • Development of constitutive dextransucrase hyper-producing mutants of Leuconostoc mesenteroides using the synchrotron radiation in the 70-1,000 eV region
    • Kim D, Kim DW, Lee JH, Park KH, Day LM Day DF 1997 Development of constitutive dextransucrase hyper-producing mutants of Leuconostoc mesenteroides using the synchrotron radiation in the 70-1,000 eV region. Biotechnol Tech 11: 319 321.
    • (1997) Biotechnol Tech , vol.11 , pp. 319-321
    • Kim, D.1    Kim, D.W.2    Lee, J.H.3    Park, K.H.4    Day, L.M.5    Day, D.F.6
  • 19
    • 0033834162 scopus 로고    scopus 로고
    • Cloning and sequencing of the α1→6 dextransucrase gene from Leuconostoc mesenteroides
    • Kim HS, Kim D, Ryu HJ Robyt. JF 2000 Cloning and sequencing of the α1→6 dextransucrase gene from Leuconostoc mesenteroides. J Microbiol Biotechnol 10: 559 563.
    • (2000) J Microbiol Biotechnol , vol.10 , pp. 559-563
    • Kim, H.S.1    Kim, D.2    Ryu, H.J.3    Robyt., J.F.4
  • 20
    • 0038582681 scopus 로고    scopus 로고
    • Dextran molecular size and degree of branching as a function of sucrose concentration, pH, and temperature of reaction of Leuconostoc mesenteroides B-512FMCM dextransucrase
    • Kim D, Robyt JF, Lee SY, Lee JH Kim YM 2003 Dextran molecular size and degree of branching as a function of sucrose concentration, pH, and temperature of reaction of Leuconostoc mesenteroides B-512FMCM dextransucrase. Carbohydr Res 338: 1183 1189.
    • (2003) Carbohydr Res , vol.338 , pp. 1183-1189
    • Kim, D.1    Robyt, J.F.2    Lee, S.Y.3    Lee, J.H.4    Kim, Y.M.5
  • 21
    • 0032213423 scopus 로고    scopus 로고
    • Large-scale preparation of highly purified dextransucrase from a high producing constitutive mutant of Leuconsotoc mesenterodies B-512FMC
    • Kitaoka M Robyt JF 1998 Large-scale preparation of highly purified dextransucrase from a high producing constitutive mutant of Leuconsotoc mesenterodies B-512FMC. Enzyme Microb Technol 23: 386 391.
    • (1998) Enzyme Microb Technol , vol.23 , pp. 386-391
    • Kitaoka, M.1    Robyt, J.F.2
  • 22
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst F, Ogasawara N, Moszer I, et al 1997 The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390: 249 256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Al, E.4
  • 23
    • 0035925904 scopus 로고    scopus 로고
    • Whole genome sequencing of meticillin-resistant Staphylococcus aureus
    • Kuroda M, Ohta T, Uchiyama I, et al 2001 Whole genome sequencing of meticillin-resistant Staphylococcus aureus. Lancet 357: 1225 1240.
    • (2001) Lancet , vol.357 , pp. 1225-1240
    • Kuroda, M.1    Ohta, T.2    Uchiyama, I.3    Al, E.4
  • 24
    • 0034103254 scopus 로고    scopus 로고
    • Enolase from Candida albicans-purification and characterization
    • Kustrzeba-Wójcicka I Golczak M 2002 Enolase from Candida albicans-purification and characterization. Comp Biochem Physiol B 126: 109 120.
    • (2002) Comp Biochem Physiol B , vol.126 , pp. 109-120
    • Kustrzeba-Wójcicka, I.1    Golczak, M.2
  • 25
    • 0022519081 scopus 로고
    • Studies on immunological properties of enolase from carp muscles after chemical modification of some amino-acid residues
    • Kustrzeba-Wójcicka I, Pietkiewicz J Wolna E 1986 Studies on immunological properties of enolase from carp muscles after chemical modification of some amino-acid residues. Arch Immunol Ther Exp 34: 93 99.
    • (1986) Arch Immunol Ther Exp , vol.34 , pp. 93-99
    • Kustrzeba-Wójcicka, I.1    Pietkiewicz, J.2    Wolna, E.3
  • 26
    • 0014949207 scopus 로고    scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK 1997 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680 685.
    • (1997) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0027126548 scopus 로고
    • Influence of pH on the Mn2+ activation of the binding to yeast enolase
    • a function study.
    • Lee BH Nowak T 1992a Influence of pH on the Mn2+ activation of the binding to yeast enolase: a function study. Biochemistry 31: 2165 2175.
    • (1992) Biochemistry , vol.31 , pp. 2165-2175
    • Lee, B.H.1    Nowak, T.2
  • 28
    • 0026681245 scopus 로고
    • Metals ion specificity at the catalytic site of yeast enolase
    • Lee ME Nowak T 1922b Metals ion specificity at the catalytic site of yeast enolase. Biochemistry 31: 2172 2180.
    • (1922) Biochemistry , vol.31 , pp. 2172-2180
    • Lee, M.E.1    Nowak, T.2
  • 29
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H Burk D 1934 The determination of enzyme dissociation constants. J Am Chem Soc 56: 658 666.
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 30
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR
    • automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking.
    • Liu YG Whittier RF 1995 Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25: 674 681.
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.G.1    Whittier, R.F.2
  • 32
    • 0019887631 scopus 로고
    • Fluoride inhibition of yeast enolase 1. Formation of the ligand complexes
    • Maurer PJ Nowak T 1981 Fluoride inhibition of yeast enolase 1. Formation of the ligand complexes. Biochemistry 20: 6894 6900.
    • (1981) Biochemistry , vol.20 , pp. 6894-6900
    • Maurer, P.J.1    Nowak, T.2
  • 34
    • 0019887606 scopus 로고
    • Fluoride inhibition of yeast enolase 2. Structural and kinetic properties of the ligand complexes determined by nuclear relaxation rate studies
    • Nowak T Maurer PJ 1981 Fluoride inhibition of yeast enolase 2. Structural and kinetic properties of the ligand complexes determined by nuclear relaxation rate studies. Biochemistry 20: 6901 6911.
    • (1981) Biochemistry , vol.20 , pp. 6901-6911
    • Nowak, T.1    Maurer, P.J.2
  • 35
    • 0023198755 scopus 로고
    • A two-step procedure for efficient electrotransfer of both high-molecular weight (>400,000) and low-molecular weight (<20,000) proteins
    • Otter TS, King M Whiteman GB 1987 A two-step procedure for efficient electrotransfer of both high-molecular weight (>400,000) and low-molecular weight (<20,000) proteins. Anal Biolchem 162: 370 377.
    • (1987) Anal Biolchem , vol.162 , pp. 370-377
    • Otter, T.S.1    King, M.2    Whiteman, G.B.3
  • 36
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional-enolase
    • its role in diseases.
    • Pancholi V 2001 Multifunctional-enolase: its role in diseases. Cell Mol Life Sci 58: 902 920.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 37
    • 0032486286 scopus 로고    scopus 로고
    • α -enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi V Fischetti VA 1998 α -enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 273: 14503 14515.
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 38
    • 0028048307 scopus 로고
    • The hyperthermophilic glycolytic enzyme enolase in the archaeon, Pyrococcus furiousus
    • comparison with mesophilic enolase.
    • Peak MJ, Peak JG, Stevens FJ, Blamey J, Mai X, Zhou H Adams MWW 1994 The hyperthermophilic glycolytic enzyme enolase in the archaeon, Pyrococcus furiousus: comparison with mesophilic enolase. Arch Biochem Biophys 313: 280 286.
    • (1994) Arch Biochem Biophys , vol.313 , pp. 280-286
    • Peak, M.J.1    Peak, J.G.2    Stevens, F.J.3    Blamey, J.4    Mai, X.5    Zhou, H.6    Adams, M.W.W.7
  • 39
    • 0020674416 scopus 로고
    • Purification and properties of enolase from carp. Comparison with enolase from mammals muscles and yeast
    • Pietkiewicz J Kustrzeba-Wójcicka I 1983 Purification and properties of enolase from carp. Comparison with enolase from mammals muscles and yeast. Comp Biochem Physiol C 75B: 693 698.
    • (1983) Comp Biochem Physiol C , vol.75 , pp. 693-698
    • Pietkiewicz, J.1    Kustrzeba-Wójcicka, I.2
  • 40
    • 0028912631 scopus 로고
    • Ocatameric enolase from the hyperthermophilic bacterium Thermotoga maritima
    • purification, characterization, and image processing.
    • Schurig H, Rutkat K, Rachel R Jaenicke R 1995 Ocatameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing. Protein Sci 4: 228 236.
    • (1995) Protein Sci , vol.4 , pp. 228-236
    • Schurig, H.1    Rutkat, K.2    Rachel, R.3    Jaenicke, R.4
  • 41
    • 0027968068 scopus 로고
    • CLUSTALW
    • improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice.
    • Thompson JD, Higgins DG Gibson TJ 1994 CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673 4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 0016258510 scopus 로고
    • Kinetics of the rabbit muscle enolase-catalyzed dehydration of 2-phosphoglycerate
    • Wang T Himoe A 1974 Kinetics of the rabbit muscle enolase-catalyzed dehydration of 2-phosphoglycerate. J Biol Chem 249: 3895 3902.
    • (1974) J Biol Chem , vol.249 , pp. 3895-3902
    • Wang, T.1    Himoe, A.2
  • 43
    • 0000404001 scopus 로고
    • Purification of brewer's and bakers' yeast enolase yielding a single active component
    • Westhead EW McLain G 1964 Purification of brewer's and bakers' yeast enolase yielding a single active component. J Biol Chem 239: 2464 2468.
    • (1964) J Biol Chem , vol.239 , pp. 2464-2468
    • Westhead, E.W.1    McLain, G.2
  • 44
    • 0031661935 scopus 로고    scopus 로고
    • Site-directed mutagenesis of streptococcal plasmin receptor protein (Plr) identifies the C-terminal Lys334 as essential for plasmin binding, but mutation of plr gene does not reduce plasmin binding to group a streptococci
    • Winram SB Lottenberg R 1998 Site-directed mutagenesis of streptococcal plasmin receptor protein (Plr) identifies the C-terminal Lys334 as essential for plasmin binding, but mutation of plr gene does not reduce plasmin binding to group A streptococci. Microbiology 144: 2025 2035.
    • (1998) Microbiology , vol.144 , pp. 2025-2035
    • Winram, S.B.1    Lottenberg, R.2
  • 45
    • 77956903746 scopus 로고
    • Boyer P.D., ed), pp. Academic Press, New York.
    • Wold F 1971 Enolase, Enzymes, Vol. 5, 3rd edn Boyer P.D., ed), pp. 499 538. Academic Press, New York.
    • (1971) Enolase, Enzymes , vol.53 , pp. 499-538
    • Wold, F.1
  • 46
    • 0000825586 scopus 로고
    • Studies on the enolase
    • Wold F Ballou CE 1957 Studies on the enolase. J Biol Chem 227: 301 312.
    • (1957) J Biol Chem , vol.227 , pp. 301-312
    • Wold, F.1    Ballou, C.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.