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Volumn 65, Issue 12, 2001, Pages 2763-2772

Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM 9

Author keywords

Acetic acid bacteria; Cyclic alcohol oxidation; Membrane bound dehydrogenase; NAD dependent cyclic alcohol dehydrogenase; Quinoprotein cyclic alcohol dehydrogenase

Indexed keywords

BACTERIA (MICROORGANISMS); GLUCONOBACTER; GLUCONOBACTER FRATEURII;

EID: 0035751610     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.2763     Document Type: Article
Times cited : (20)

References (33)
  • 1
    • 0023794416 scopus 로고
    • Anaerobic metabolism of cyclohexanol by denitrifying bacteria
    • Dangel, W., Tschech, A., and Fuchs, G., Anaerobic metabolism of cyclohexanol by denitrifying bacteria. Arch. Microbiol., 150, 358-362 (1988).
    • (1988) Arch. Microbiol. , vol.150 , pp. 358-362
    • Dangel, W.1    Tschech, A.2    Fuchs, G.3
  • 2
    • 0016824525 scopus 로고
    • The metabolism of cyclohexanol by Acinetobacter NC1B 9871
    • Donoghue, N. A., and Trudgill, P. W., The metabolism of cyclohexanol by Acinetobacter NC1B 9871. Eur. J. Biochem., 60, 1-7 (1975).
    • (1975) Eur. J. Biochem. , vol.60 , pp. 1-7
    • Donoghue, N.A.1    Trudgill, P.W.2
  • 4
    • 0024331052 scopus 로고
    • Enzyme reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species
    • Dangel, W., Tschech, A., and Fuchs, C., Enzyme reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol., 152, 273-279 (1989).
    • (1989) Arch. Microbiol. , vol.152 , pp. 273-279
    • Dangel, W.1    Tschech, A.2    Fuchs, C.3
  • 5
    • 0021800336 scopus 로고
    • Isolation and characterization of a cyclohexane-metabolizing Xanthobacter sp.
    • Trower, M. K., Buckland, R. M., Higgins, R., and Griffin, M., Isolation and characterization of a cyclohexane-metabolizing Xanthobacter sp. Appl. Environ. Microbiol., 49, 1282-1289 (1985).
    • (1985) Appl. Environ. Microbiol. , vol.49 , pp. 1282-1289
    • Trower, M.K.1    Buckland, R.M.2    Higgins, R.3    Griffin, M.4
  • 6
    • 0033871150 scopus 로고    scopus 로고
    • Genetic analysis of a gene cluster for cyclohexanol oxidation in Acinetobacter sp. strain SE19 by in vitro transposition
    • Cheng, Q., Thomas, S. M., Kostichka, K., Valentine, J. R., and Nagarajan, V., Genetic analysis of a gene cluster for cyclohexanol oxidation in Acinetobacter sp. strain SE19 by in vitro transposition. J. Bacteriol., 182, 4744-4751 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 4744-4751
    • Cheng, Q.1    Thomas, S.M.2    Kostichka, K.3    Valentine, J.R.4    Nagarajan, V.5
  • 8
    • 85007953007 scopus 로고
    • Studies on the organism producing isopropanol from acetone. Part V. Enzymological on the oxidation-reduction of Lactobacillus brevis var. hofuensis
    • Hoshino, K., Studies on the organism producing isopropanol from acetone. Part V. Enzymological on the oxidation-reduction of Lactobacillus brevis var. hofuensis. Nihon Nogeikagaku Kaishi (in Japanese), 34, 608-615 (1960).
    • (1960) Nihon Nogeikagaku Kaishi (in Japanese) , vol.34 , pp. 608-615
    • Hoshino, K.1
  • 9
    • 85007974576 scopus 로고
    • Studies on the organism producing isopropanol from acetone. Part VI. Isopropanol dehydrogenase and alcohol dehydrogenase of Lactobacillus brevis var. hofuensis
    • Hoshino, K., Studies on the organism producing isopropanol from acetone. Part VI. Isopropanol dehydrogenase and alcohol dehydrogenase of Lactobacillus brevis var. hofuensis. Nihon Nogeikagaku Kaishi (in Japanese), 34, 616-619 (1960).
    • (1960) Nihon Nogeikagaku Kaishi (in Japanese) , vol.34 , pp. 616-619
    • Hoshino, K.1
  • 10
    • 0019495032 scopus 로고
    • Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase
    • Wermuth, B., Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem., 256, 1206-1213 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 1206-1213
    • Wermuth, B.1
  • 11
    • 84954880610 scopus 로고
    • Novel enzymatic production of D-(-)-pantoyl lactone through the stereospecific reductation of ketopantoic acid
    • Kataoka, M., Shimizu, S., and Yamada, H., Novel enzymatic production of D-(-)-pantoyl lactone through the stereospecific reductation of ketopantoic acid. Agric. Biol. Chem., 54, 177-182 (1990).
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 177-182
    • Kataoka, M.1    Shimizu, S.2    Yamada, H.3
  • 12
    • 0025294272 scopus 로고
    • A novel NADPH-dependent aldehyde reductase, catalyzing asymetric reduction of β-keto acid esters, from Sporobolomyces salmonicolor. Purification and characterization
    • Yamada, H., Shimizu, S., Kataoka, M., Sakai, H., and Miyoshi, T., A novel NADPH-dependent aldehyde reductase, catalyzing asymetric reduction of β-keto acid esters, from Sporobolomyces salmonicolor. Purification and characterization. FEMS Microbiol. Lett., 70, 45-48 (1990).
    • (1990) FEMS Microbiol. Lett. , vol.70 , pp. 45-48
    • Yamada, H.1    Shimizu, S.2    Kataoka, M.3    Sakai, H.4    Miyoshi, T.5
  • 13
    • 0033545524 scopus 로고    scopus 로고
    • Purification and characterization of new aldehyde reductases from Sporobolomyces salmonicolor AKU4429
    • Kita, K., Nakase, K., Yanase, H., Kataoka, M., and Shimizu, S., Purification and characterization of new aldehyde reductases from Sporobolomyces salmonicolor AKU4429. J. Mol. Catalysis B: Enzymatic, 6, 305-313 (1999).
    • (1999) J. Mol. Catalysis B: Enzymatic , vol.6 , pp. 305-313
    • Kita, K.1    Nakase, K.2    Yanase, H.3    Kataoka, M.4    Shimizu, S.5
  • 15
    • 0032951737 scopus 로고    scopus 로고
    • Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes
    • Kataoka, M., Yamamoto, K., Kawabata, H., Wada, M., Yanase, H., and Shimizu, S., Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes. Appl. Microbiol. Biotechnol., 51, 486-490 (1999).
    • (1999) Appl. Microbiol. Biotechnol. , vol.51 , pp. 486-490
    • Kataoka, M.1    Yamamoto, K.2    Kawabata, H.3    Wada, M.4    Yanase, H.5    Shimizu, S.6
  • 16
    • 0015394709 scopus 로고
    • The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872
    • Griffin, M., and Trudgill, P. W., The metabolism of cyclopentanol by Pseudomonas N.C.I.B. 9872. Biochem. J., 129, 595-603 (1972).
    • (1972) Biochem. J. , vol.129 , pp. 595-603
    • Griffin, M.1    Trudgill, P.W.2
  • 17
    • 0017163060 scopus 로고
    • Purification and some properties of polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3
    • Suzuki, T., Purification and some properties of polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3. Agric. Biol. Chem., 40, 497-504 (1976).
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 497-504
    • Suzuki, T.1
  • 18
    • 0017871629 scopus 로고
    • Oxidation of secondary alcohols by polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3
    • Suzuki, T., Oxidation of secondary alcohols by polyvinyl alcohol-degrading enzyme produced by Pseudomonas O-3. Agric. Biol. Chem., 42, 1187-1194 (1978).
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 1187-1194
    • Suzuki, T.1
  • 19
    • 0000218094 scopus 로고
    • Purification and properties of secondary alcohol oxidase from a strain of Pseudomonas
    • Morita, M., Hamada, N., Sakai, K., and Watanabe, Y., Purification and properties of secondary alcohol oxidase from a strain of Pseudomonas. Agric. Biol. Chem., 43, 1225-1235 (1979).
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 1225-1235
    • Morita, M.1    Hamada, N.2    Sakai, K.3    Watanabe, Y.4
  • 20
    • 0041605164 scopus 로고
    • The stereochemical specificity of the oxidation of cyclitols by Acetobacter suboxydans
    • Magasanik, B., Franzl, R. E., and Chargaff, E., The stereochemical specificity of the oxidation of cyclitols by Acetobacter suboxydans. J. Am. Chem. Soc., 74, 2618-2621 (1952).
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 2618-2621
    • Magasanik, B.1    Franzl, R.E.2    Chargaff, E.3
  • 21
    • 0041605167 scopus 로고
    • The cyclitol-oxidizing enzyme system of Acetobacter suboxydans
    • Anderson, L., Tomita, K., Kussi, P., and Kirkwood, S., The cyclitol-oxidizing enzyme system of Acetobacter suboxydans. J. Biol. Chem., 204, 769-780 (1953).
    • (1953) J. Biol. Chem. , vol.204 , pp. 769-780
    • Anderson, L.1    Tomita, K.2    Kussi, P.3    Kirkwood, S.4
  • 23
    • 0042723713 scopus 로고
    • Cyclitol oxidation by Acetobacter suboxydans. II. Additional cyclitols and the third specificity rule
    • Anderson, L., Takeda, R., Angyal, S. J., and McHugh, D. J., Cyclitol oxidation by Acetobacter suboxydans. II. Additional cyclitols and the third specificity rule. Arch. Biochem. Biophys., 78, 518-531 (1958).
    • (1958) Arch. Biochem. Biophys. , vol.78 , pp. 518-531
    • Anderson, L.1    Takeda, R.2    Angyal, S.J.3    McHugh, D.J.4
  • 24
    • 0014027060 scopus 로고
    • The pathway of myo-inositol degradation in Aerobacter aerogenes. Dehydrogenation and dehydration
    • Berman, T., and Magasanik, B., The pathway of myo-inositol degradation in Aerobacter aerogenes. Dehydrogenation and dehydration. J. Biol. Chem., 241, 800-806 (1966).
    • (1966) J. Biol. Chem. , vol.241 , pp. 800-806
    • Berman, T.1    Magasanik, B.2
  • 25
    • 0014027127 scopus 로고
    • The pathway of myo-inositol degradation in Aerobacter aerogenes. Ring scission
    • Berman, T., and Magasanik, B., The pathway of myo-inositol degradation in Aerobacter aerogenes. Ring scission. J. Biol. Chem., 241, 807-813 (1966).
    • (1966) J. Biol. Chem. , vol.241 , pp. 807-813
    • Berman, T.1    Magasanik, B.2
  • 26
    • 0015923924 scopus 로고
    • Inositol dehydrogenase from the yeast Cryptococcus melibiosum
    • Vidal-leiria, M., and van Uden, N., Inositol dehydrogenase from the yeast Cryptococcus melibiosum. Biochem Biophys. Acta, 293, 295-303 (1973).
    • (1973) Biochem Biophys. Acta , vol.293 , pp. 295-303
    • Vidal-Leiria, M.1    Van Uden, N.2
  • 27
    • 0015970614 scopus 로고
    • Rapid purification of lactate dehydrogenase from rat liver and hepatoma: A new approach
    • Ryan, L. D. and Vestling, C. S., Rapid purification of lactate dehydrogenase from rat liver and hepatoma: a new approach. Arch. Biochem. Biophys., 160, 279-284 (1974).
    • (1974) Arch. Biochem. Biophys. , vol.160 , pp. 279-284
    • Ryan, L.D.1    Vestling, C.S.2
  • 29
    • 77957025803 scopus 로고
    • Alcohol dehydrogenase from acetic acid bacteria, membrane-bound
    • ed. Wood, W. A., Academic Press, Ltd., New York
    • Ameyama, M. and Adachi, O., Alcohol dehydrogenase from acetic acid bacteria, membrane-bound. in "Methods in Enzymology", Vol. 89, ed. Wood, W. A., Academic Press, Ltd., New York, pp. 450-457 (1982).
    • (1982) Methods in Enzymology , vol.89 , pp. 450-457
    • Ameyama, M.1    Adachi, O.2
  • 30
    • 0016642871 scopus 로고
    • A simple technique for eliminating interference by detergents in the Lowry method of protein determination
    • Dully, J. R., and Grieve, P. A., A simple technique for eliminating interference by detergents in the Lowry method of protein determination. Anal. Biochem., 64, 136-141 (1975).
    • (1975) Anal. Biochem. , vol.64 , pp. 136-141
    • Dully, J.R.1    Grieve, P.A.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 (1970).
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0008710258 scopus 로고
    • Determination of sedimentation rates
    • ed. Chervenka, C. H., Spinco Division of Beckman Instruments Inc., Palo Alto, California
    • Chervenka, C. H., Determination of sedimentation rates. in "A Manual of Methods for the Analytical Ultracentrifuge", ed. Chervenka, C. H., Spinco Division of Beckman Instruments Inc., Palo Alto, California, pp. 23-27 (1970).
    • (1970) A Manual of Methods for the Analytical Ultracentrifuge , pp. 23-27
    • Chervenka, C.H.1
  • 33
    • 0028202832 scopus 로고
    • Respiratory chains and bioenergetics of acetic acid bacteria
    • ed. Rose, A.H. and Tempest, D. W., Academic Press, Ltd., London
    • Matsushita, K., Toyama, H., and Adachi, O., Respiratory chains and bioenergetics of acetic acid bacteria. in "Advances in Microbial Physiology", Vol. 36, ed. Rose, A.H. and Tempest, D. W., Academic Press, Ltd., London, pp. 247-301 (1994).
    • (1994) Advances in Microbial Physiology , vol.36 , pp. 247-301
    • Matsushita, K.1    Toyama, H.2    Adachi, O.3


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