메뉴 건너뛰기




Volumn 179, Issue 2, 2003, Pages 101-107

A zinc-containing mannitol-2-dehydrogenase from Leuconostoc pseudomesenteroides ATCC 12291: Purification of the enzyme and cloning of the gene

Author keywords

Leuconostoc pseudomesenteroides; Mannitol 2 dehydrogenase; mdh gene; MDR; Medium chain alcohol polyol dehydrogenase reductase protein family; NAD+ dependent dehydrogenase; Zinc containing

Indexed keywords

EDETIC ACID; MAGNESIUM ION; MANGANESE; MANNITOL DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; ZINC ION;

EID: 0037281550     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-002-0507-2     Document Type: Article
Times cited : (43)

References (32)
  • 1
    • 0013769988 scopus 로고
    • Estimation of the molecular weights of proteins by Sephadex gel-filtration
    • Andrews P (1964) Estimation of the molecuar weights of proteins by Sephadex gel-filtration. Biochem J 91:222-233
    • (1964) Biochem J , vol.91 , pp. 222-233
    • Andrews, P.1
  • 2
    • 0001780077 scopus 로고    scopus 로고
    • Lactic acid bacteria: Classification and physiology
    • Salminen S, von Wright A (eds). Marcel Dekker, New York
    • Axelsson L (1998) Lactic acid bacteria: classification and physiology. In: Salminen S, von Wright A (eds) Lactic acid bacteria-Microbiology and functional aspects, 2nd edn. Marcel Dekker, New York, pp 1-72
    • (1998) Lactic Acid Bacteria - Microbiology and Functional Aspects, 2nd Edn. , pp. 1-72
    • Axelsson, L.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micrgram quantities of protein utilizing the principles of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of micrgram quantities of protein utilizing the principles of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0031579663 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence and expression of a mannitol dehydrogenase gene from Pseudomonas fluorescens DSM 50106 in Escherichia coli
    • Brünker P, Altenbuchler J, Kulbe KD, Mattes R (1997) Cloning, nucleotide sequence and expression of a mannitol dehydrogenase gene from Pseudomonas fluorescens DSM 50106 in Escherichia coli. Biochim Biophys Acta 1351:157-167
    • (1997) Biochim Biophys Acta , vol.1351 , pp. 157-167
    • Brünker, P.1    Altenbuchler, J.2    Kulbe, K.D.3    Mattes, R.4
  • 5
    • 0014690895 scopus 로고
    • Observations on molecular weight determinations on polyacrylamide gel
    • Dunker AK, Rueckert RR (1969) Observations on molecular weight determinations on polyacrylamide gel. J Biol Chem 244:5074-5080
    • (1969) J Biol Chem , vol.244 , pp. 5074-5080
    • Dunker, A.K.1    Rueckert, R.R.2
  • 6
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman P, Begg G (1967) A protein sequenator. Eur J Biochem 1:80-91
    • (1967) Eur J Biochem , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 9
    • 0039699818 scopus 로고    scopus 로고
    • SDR and MDR: Completed genome sequences show these protein families to be large, of old origin, and of complex nature
    • Jörnvall H, Hoog JO, Persson B (1999) SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature. FEBS Lett 445:262-264
    • (1999) FEBS Lett , vol.445 , pp. 262-264
    • Jörnvall, H.1    Hoog, J.O.2    Persson, B.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-695
    • (1970) Nature , vol.227 , pp. 680-695
    • Laemmli, U.K.1
  • 11
    • 0020676045 scopus 로고
    • Kinetic analysis of rat liver sorbitol dehydrogenase
    • Leising NC, McGuiness ET (1983) Kinetic analysis of rat liver sorbitol dehydrogenase. Int J Biochem 15:651-656
    • (1983) Int J Biochem , vol.15 , pp. 651-656
    • Leising, N.C.1    McGuiness, E.T.2
  • 12
    • 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
  • 14
    • 0023856594 scopus 로고
    • Purification and characterization of human liver sorbitol dehydrogenase
    • Maret W, Auld DS (1988) Purification and characterization of human liver sorbitol dehydrogenase. Biochemistry 27:1622-1628
    • (1988) Biochemistry , vol.27 , pp. 1622-1628
    • Maret, W.1    Auld, D.S.2
  • 15
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, pp 352-355
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 16
    • 0022345326 scopus 로고
    • Mannitol metabolism in Agaricus bisporus: Purification and properties of mannitol dehydrogenase
    • Morton N, Dickerson AG, Hammond JBW (1985) Mannitol metabolism in Agaricus bisporus: purification and properties of mannitol dehydrogenase. J Gen Microbiol 131:2885-2890
    • (1985) J Gen Microbiol , vol.131 , pp. 2885-2890
    • Morton, N.1    Dickerson, A.G.2    Hammond, J.B.W.3
  • 17
    • 0026491205 scopus 로고
    • Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning
    • Ng K, Ye R, Wu XC, Wong SL (1992) Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning. J Biol Chem 267:24989-24994
    • (1992) J Biol Chem , vol.267 , pp. 24989-24994
    • Ng, K.1    Ye, R.2    Wu, X.C.3    Wong, S.L.4
  • 18
    • 0028151542 scopus 로고
    • A super-family of medium-chain dehydrogenases/reductases (MDR)
    • Persson B, Zigler JS, Jörnvall H (1994) A super-family of medium-chain dehydrogenases/reductases (MDR). Eur J Biochem 226:15-22
    • (1994) Eur J Biochem , vol.226 , pp. 15-22
    • Persson, B.1    Zigler, J.S.2    Jörnvall, H.3
  • 20
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal Biochem, 166:368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 21
    • 0002290724 scopus 로고
    • Nucleic acid hybridization studies on Leuconostoc and heterofermentative Lactobacilli and description of Leuconostoc amelibiosum sp. nov.
    • Schillinger U, Holzapfel W, Kandler O (1989) Nucleic acid hybridization studies on Leuconostoc and heterofermentative Lactobacilli and description of Leuconostoc amelibiosum sp. nov. Syst Appl Microbiol 12:48-55
    • (1989) Syst Appl Microbiol , vol.12 , pp. 48-55
    • Schillinger, U.1    Holzapfel, W.2    Kandler, O.3
  • 22
    • 0024726244 scopus 로고
    • Purification and properties of a polyol dehydrogenase from the phototrophic bacterium Rhodobacter sphaeroides
    • Schneider KH, Giffhorn F (1989) Purification and properties of a polyol dehydrogenase from the phototrophic bacterium Rhodobacter sphaeroides. Eur J Biochem 184:15-19
    • (1989) Eur J Biochem , vol.184 , pp. 15-19
    • Schneider, K.H.1    Giffhorn, F.2
  • 23
    • 0027382311 scopus 로고
    • Cloning, nucleotide sequence and characterization of a mannitol dehydrogenase gene from Rhodobacter sphaeroides
    • Schneider KH, Giffhorn F, Kaplan S (1993) Cloning, nucleotide sequence and characterization of a mannitol dehydrogenase gene from Rhodobacter sphaeroides. J Gen Microbiol 139:2475-2484
    • (1993) J Gen Microbiol , vol.139 , pp. 2475-2484
    • Schneider, K.H.1    Giffhorn, F.2    Kaplan, S.3
  • 25
    • 0033543212 scopus 로고    scopus 로고
    • Kinetic studies of catalytic mechanism of mannitol dehydrogenase from Pseudomonas fluorescens
    • Slatner M, Nidetzky B, Kulbe KD (1999) Kinetic studies of catalytic mechanism of mannitol dehydrogenase from Pseudomonas fluorescens. Biochemistry 38:10489-10498
    • (1999) Biochemistry , vol.38 , pp. 10489-10498
    • Slatner, M.1    Nidetzky, B.2    Kulbe, K.D.3
  • 27
    • 0002244584 scopus 로고
    • Production of D-mannitol and D-lactic acid by fermentation with Leuconostoc mesenteroides
    • Soetaert W, Buchholz K, Vandamme EJ (1995) Production of D-mannitol and D-lactic acid by fermentation with Leuconostoc mesenteroides. Agro-Food-Industry Hi-Tech 6:41-44
    • (1995) Agro-Food-Industry Hi-Tech , vol.6 , pp. 41-44
    • Soetaert, W.1    Buchholz, K.2    Vandamme, E.J.3
  • 28
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern EM (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol 8:503-517
    • (1975) J Mol Biol , vol.8 , pp. 503-517
    • Southern, E.M.1
  • 29
    • 0031766095 scopus 로고    scopus 로고
    • +-mannitol dehydrogenase cDNA from the button mushroom Agaricus bisporus, and its expression in response to NaCl stress
    • +-mannitol dehydrogenase cDNA from the button mushroom Agaricus bisporus, and its expression in response to NaCl stress. Appl Environ Micobiol 64:4689-4696
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4689-4696
    • Stoop, J.M.1    Mooibroeck, H.2
  • 30
    • 0015231962 scopus 로고
    • Effect of charge on the determination of molecular weight of proteins by gel electrophoresis in SDS
    • Tung J-S, Knight CA (1971) Effect of charge on the determination of molecular weight of proteins by gel electrophoresis in SDS. Biochem Biophys Res Commun 42:1117-1121
    • (1971) Biochem Biophys Res Commun , vol.42 , pp. 1117-1121
    • Tung, J.-S.1    Knight, C.A.2
  • 31
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira J, Messing J (1982) The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 32
    • 0035911798 scopus 로고    scopus 로고
    • Functional modeling of alcoholdehydrogenase with pyrazolylborate-zinc complexes
    • Walz R, Vahrenkamp H (2001) Functional modeling of alcoholdehydrogenase with pyrazolylborate-zinc complexes. Inorganica Chimica Acta 314:58-62
    • (2001) Inorganica Chimica Acta , vol.314 , pp. 58-62
    • Walz, R.1    Vahrenkamp, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.