메뉴 건너뛰기




Volumn 63, Issue 12, 1999, Pages 2102-2109

Enzymes Responsible for Acetate Oxidation by Acetic Acid Bacteria

Author keywords

Acetate oxidation; Acetic acid bacteria; Acetyl CoA synthetase, phosphoenolpyruvate carboxylase; Vinegar fermentation

Indexed keywords


EID: 0001591994     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.2102     Document Type: Article
Times cited : (28)

References (45)
  • 1
    • 0000539854 scopus 로고
    • Family VI Acetobacter-aceae
    • In, ed. by N. R. Krieg and J. G. Holt, Williams & Wilkins, Baltimore
    • De Ley, J., Gillis, M., and Swings, J., Family VI Acetobacter-aceae. In “Bergey’s Manual of Systematic Bacteriology”, ed. by N. R. Krieg and J. G. Holt, Vol. 1, Williams & Wilkins, Baltimore, pp. 267-275 (1984).
    • (1984) Bergeys Manual of Systematic Bacteriology” , vol.1 , pp. 267-275
    • De Ley, J.1    Gillis, M.2    Swings, J.3
  • 2
    • 85007903363 scopus 로고
    • Per oxidized flavor and acidic fraction of rice vinegar
    • Yamaguchi, G. and Masai, H., Per oxidized flavor and acidic fraction of rice vinegar. Agric. Biol. Chem., 39, 1907-1911 (1975).
    • (1975) Agric. Biol. Chem. , vol.39 , pp. 1907-1911
    • Yamaguchi, G.1    Masai, H.2
  • 3
    • 0030934840 scopus 로고    scopus 로고
    • Development of thermotolerant acetic acid bacteria useful for vinegar fermentation at higher temperatures
    • Saeki, A., Theeragool, G., Matsushita, K., Toyama, H., Lotong, N., and Adachi, O., Development of thermotolerant acetic acid bacteria useful for vinegar fermentation at higher temperatures. Biosci. Biotechnol. Biochem., 61, 138-145 (1997).
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 138-145
    • Saeki, A.1    Theeragool, G.2    Matsushita, K.3    Toyama, H.4    Lotong, N.5    Adachi, O.6
  • 5
    • 0019485302 scopus 로고
    • D-Fructose dehydrogenase of Gluconobacter industrius: Purification, characterization, and application to enzymatic microdetermination of D-fructose
    • Ameyama, M., Shinagawa, E., Matsushita, K., and Adachi, O., D-Fructose dehydrogenase of Gluconobacter industrius: Purification, characterization, and application to enzymatic microdetermination of D-fructose. J. Bacteriol., 145, 814-823 (1981).
    • (1981) J. Bacteriol. , vol.145 , pp. 814-823
    • Ameyama, M.1    Shinagawa, E.2    Matsushita, K.3    Adachi, O.4
  • 6
    • 0027534829 scopus 로고
    • Application of Gluconobacter oxydans subsp. Sphaericus IFO 12467 to vinegar production
    • Saeki, A., Application of Gluconobacter oxydans subsp. sphaericus IFO 12467 to vinegar production. J. Ferment. Bioeng., 75, 232-234 (1993).
    • (1993) J. Ferment. Bioeng. , vol.75 , pp. 232-234
    • Saeki, A.1
  • 7
    • 0041437701 scopus 로고
    • Enzymic microdetermination of D-glucose, d-fructose, D-gluconate, 2-keto-D-gluconate, aldehyde, and alcohol with membrane-bound dehydrogenases
    • by W. A. Wood, Academic Press, New York
    • Ameyama, M., Enzymic microdetermination of D-glucose, d-fructose, D-gluconate, 2-keto-D-gluconate, aldehyde, and alcohol with membrane-bound dehydrogenases. In “Methods in En-zymology,” Vol. 89, ed. by W. A. Wood, Academic Press, New York, pp. 20-29 (1982).
    • (1982) Methods in En-Zymology , vol.89 , pp. 20-29
    • Ameyama, M.1
  • 9
    • 0001198106 scopus 로고
    • Acetate kinase from Veil-lonella alcalesclens
    • by J. M. Lowenstein, Academic Press, New York
    • Nishimura, J. S. and Griffith, M. J., Acetate kinase from Veil-lonella alcalesclens. In “Methods in Enzymology“Vol. 71, ed. by J. M. Lowenstein, Academic Press, New York, pp. 311-316 (1981).
    • (1981) Methods in Enzymology , vol.71 , pp. 311-316
    • Nishimura, J.S.1    Griffith, M.J.2
  • 10
    • 0019343030 scopus 로고
    • Acetyl-CoA synthetase from baker’s yeast (Saccharomyces cerevisiae)
    • by J. M. Lowenstein, Academic Press, New York
    • Frenkel, E. P. and Kitchens, R. L., Acetyl-CoA synthetase from baker’s yeast (Saccharomyces cerevisiae). In “Methods in Enzymology,” Vol. 71, ed. by J. M. Lowenstein, Academic Press, New York, pp. 317-324 (1981).
    • (1981) Methods in Enzymology , vol.71 , pp. 317-324
    • Frenkel, E.P.1    Kitchens, R.L.2
  • 11
    • 0000859908 scopus 로고
    • Phosphotransacetylase from Clostridium kluyeri
    • by J. M. Lowenstein, Academic Press, New York
    • Klotzsch, H. R., Phosphotransacetylase from Clostridium kluyeri. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 381-386 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 381-386
    • Klotzsch, H.R.1
  • 12
    • 0028985856 scopus 로고
    • Evidence for the existence of isocitrate lyase activity in methylotrophic Hyphomicrobium strains
    • Yoshida, T., Tanaka, Y., Hagishita, T., Mitsunaga, T. and Izumi, Y., Evidence for the existence of isocitrate lyase activity in methylotrophic Hyphomicrobium strains. FEMS Microbiol. Lett., 126, 221-226 (1995).
    • (1995) FEMS Microbiol. Lett. , vol.126 , pp. 221-226
    • Yoshida, T.1    Tanaka, Y.2    Hagishita, T.3    Mitsunaga, T.4    Izumi, Y.5
  • 13
    • 0042665403 scopus 로고
    • Polarographie assay for malate synthase and citrate synthase
    • by J. M. Lowenstein, Academic Press, New York
    • Weitzman, P. D. J., Polarographie assay for malate synthase and citrate synthase. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 365-368 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 365-368
    • Weitzman, P.D.J.1
  • 14
    • 0038617409 scopus 로고
    • Phosphoenolpyruvate carboxylase from Escherichia coli
    • by J. M. Lowenstein, Academic Press, New York
    • Canovas, J. L. and Kornberg, H. L., Phosphoenolpyruvate carboxylase from Escherichia coli. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 288-292 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 288-292
    • Canovas, J.L.1    Kornberg, H.L.2
  • 15
    • 77956902867 scopus 로고
    • Pyruvate kinase
    • by P. D. Boyer, Academic Press, New York
    • Kayne, F. J., Pyruvate kinase. In “The Enzymes (3rd ed.),” Vol. 8, ed. by P. D. Boyer, Academic Press, New York, pp. 353-382 (1973).
    • (1973) The Enzymes (3Rd Ed.) , vol.8 , pp. 353-382
    • Kayne, F.J.1
  • 16
    • 0004792017 scopus 로고
    • Phosphoenolpyruvate carboxykinase from pig liver mitochondria
    • by J. M. Lowenstein, Academic Press, New York
    • Lane, M. D., Chang, H. C. and Miller, R. S., Phosphoenolpyruvate carboxykinase from pig liver mitochondria. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 270-277 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 270-277
    • Lane, M.D.1    Chang, H.C.2    Miller, R.S.3
  • 17
    • 77957010084 scopus 로고
    • Pyruvate carboxylase from chicken liver
    • by J. M. Lowenstein, Academic Press, New York
    • Scrutton, M. C., Olmsted, M. R. and Utter, M. F., Pyruvate carboxylase from chicken liver. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 235-249 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 235-249
    • Scrutton, M.C.1    Olmsted, M.R.2    Utter, M.F.3
  • 18
    • 0013141879 scopus 로고
    • Pyruvate carboxylase from Saccharomyces cerevisiae
    • by J. M. Lowenstein, Academic Press, New York
    • Young, M. R., Tolbert, B. and Utter, M. F., Pyruvate carboxylase from Saccharomyces cerevisiae. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 250-258 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 250-258
    • Young, M.R.1    Tolbert, B.2    Utter, M.F.3
  • 19
    • 77957010654 scopus 로고
    • Pyruvate carboxylase from Pseudomonas
    • by J. M. Lowenstein, Academic Press, New York
    • Seubert, W. and Weicker, H., Pyruvate carboxylase from Pseudomonas. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 258-262 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 258-262
    • Seubert, W.1    Weicker, H.2
  • 20
    • 0000264190 scopus 로고
    • Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods. Malate. Determination with malate dehydrogenase
    • by J. M. Lowenstein, Academic Press, New York
    • Williamson, J. R. and Corkey, B. E., Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods. Malate. Determination with malate dehydrogenase. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 466-468 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 466-468
    • Williamson, J.R.1    Corkey, B.E.2
  • 21
    • 0000264190 scopus 로고
    • Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods. Fumarate. Determination with fumarase and malate dehydrogenase
    • by J. M. Lowenstein, Academic Press, New York
    • Williamson, J. R. and Corkey, B. E., Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods. Fumarate. Determination with fumarase and malate dehydrogenase. In “Methods in Enzymology,” Vol. 13, ed. by J. M. Lowenstein, Academic Press, New York, pp. 463-466 (1969).
    • (1969) Methods in Enzymology , vol.13 , pp. 463-466
    • Williamson, J.R.1    Corkey, B.E.2
  • 22
    • 77956994155 scopus 로고
    • Liver alcohol dehydrogenase
    • by S. P. Colowick and N. O. Kaplan, Academic Press, New York
    • Bonnichsen, R. K. and Brink, N. G., Liver alcohol dehydrogenase. In “Methods in Enzymology,” Vol. 1, ed. by S. P. Colowick and N. O. Kaplan, Academic Press, New York, pp. 495-500 (1955).
    • (1955) Methods in Enzymology , vol.1 , pp. 495-500
    • Bonnichsen, R.K.1    Brink, N.G.2
  • 23
    • 0000717689 scopus 로고
    • Enzymes as biochemical reagents. Hexokinase
    • by H. U. Bergmeyer, Verlag Chemie Weinheim GmbH
    • Bergmeyer, H. U., Gawehn, K. and Grassl, M., Enzymes as biochemical reagents. Hexokinase. In “Methods of Enzymatic Analysis,” Vol. 1, ed. by H. U. Bergmeyer, Verlag Chemie Weinheim GmbH, pp. 425-522 (1974).
    • (1974) Methods of Enzymatic Analysis , vol.1 , pp. 425-522
    • Bergmeyer, H.U.1    Gawehn, K.2    Grassl, M.3
  • 24
    • 0001118775 scopus 로고
    • Glycerol. UV-Method
    • by H. U. Bergmeyer, Verlag Chemie Wein-heim GmbH
    • Wieland, O., Glycerol. UV-Method. In “Methods of Enzymatic Analysis,” Vol. 3, ed. by H. U. Bergmeyer, Verlag Chemie Wein-heim GmbH, pp. 1404-1409 (1974).
    • (1974) Methods of Enzymatic Analysis , vol.3 , pp. 1404-1409
    • Wieland, O.1
  • 25
    • 0016642871 scopus 로고
    • A simple technique for eliminating interference by detergents in the Lowry method of protein determination
    • Dulley, 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
    • Dulley, J.R.1    Grieve, P.A.2
  • 26
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Methods of application to human serum proteins
    • Davis, B. J., Disc electrophoresis. II. Methods of application to human serum proteins. Ann. N. Y. Acad. Sci, 121, 404-427 (1964).
    • (1964) Ann. N. Y. Acad. Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 27
    • 0017091311 scopus 로고
    • Escherichia coli acetate kinase mechanism studied by net initial rate, equilibrium, and independent isotopic exchange kinetics
    • Skarstedt, M. T. and Silverstein, E., Escherichia coli acetate kinase mechanism studied by net initial rate, equilibrium, and independent isotopic exchange kinetics. J. Biol. Chem., 251, 6775-6783 (1976).
    • (1976) J. Biol. Chem. , vol.251 , pp. 6775-6783
    • Skarstedt, M.T.1    Silverstein, E.2
  • 29
    • 0017889735 scopus 로고
    • Purification and properties of acetate kinase from
    • Nakajima, H., Suzuki, K. and Imahori, K., Purification and properties of acetate kinase from Bacillus stearothermophilus. J. Biochem., 84, 193-203 (1978).
    • (1978) J. Biochem. , vol.84 , pp. 193-203
    • Nakajima, H.1    Suzuki, K.2    Imahori, K.3
  • 30
    • 0017881570 scopus 로고
    • Purification and characterization of acetate kinase from Veillonella alcalescens ATCC 17748
    • Yoshimura, F., Purification and characterization of acetate kinase from Veillonella alcalescens ATCC 17748. Arch. Biochem. Biophys., 189, 424-432 (1978).
    • (1978) Arch. Biochem. Biophys. , vol.189 , pp. 424-432
    • Yoshimura, F.1
  • 31
    • 0028202832 scopus 로고
    • Respiratory chains and bioenergetics of acetic acid bacteria
    • Rose, A. H. and Tempest, D. W., Academic Press, 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, London, pp. 247-301 (1994).
    • (1994) Advances in Microbial Physiology , vol.36 , pp. 247-301
    • Matsushita, K.1    Toyama, H.2    Adachi, O.3
  • 32
    • 0005955755 scopus 로고
    • Biochemical activities of acetic acid bacteria
    • In, ed. Asai, T., Univ. of Tokyo Press, Tokyo
    • Asai, T., Biochemical activities of acetic acid bacteria. In “Acetic Acid Bacteria,” ed. Asai, T., Univ. of Tokyo Press, Tokyo, pp. 105-314 (1968).
    • (1968) Acetic Acid Bacteria , pp. 105-314
    • Asai, T.1
  • 33
    • 0002334347 scopus 로고
    • Anaplerotic sequences and their role in metabolism
    • Kornberg, H. L., Anaplerotic sequences and their role in metabolism. Essays Biochem., 2, 1-31 (1966).
    • (1966) Essays Biochem. , vol.2 , pp. 1-31
    • Kornberg, H.L.1
  • 34
    • 85007843862 scopus 로고
    • Effects of oxygen tension in the gaseous phase on production and physical properties of bacterial cellulose formed under static culture conditions
    • Watanabe, K. and Yamanaka, S., Effects of oxygen tension in the gaseous phase on production and physical properties of bacterial cellulose formed under static culture conditions. Biosci. Biotechnol. Biochem., 59, 65-68 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 65-68
    • Watanabe, K.1    Yamanaka, S.2
  • 35
    • 0042164462 scopus 로고
    • Chemoautotrophic carbon dioxide fixation by extracts of Thiobacillus thiooxidans. I. Formation of oxaloacetic acid
    • Suzuki, I. and Werkman, C. H., Chemoautotrophic carbon dioxide fixation by extracts of Thiobacillus thiooxidans. I. Formation of oxaloacetic acid. Arch. Biochem. Biophys., 76, 103-111 (1958).
    • (1958) Arch. Biochem. Biophys. , vol.76 , pp. 103-111
    • Suzuki, I.1    Werkman, C.H.2
  • 36
    • 0042164463 scopus 로고
    • Fine control of phos-phopyruvic carboxylase activity in Escherichia coli
    • Canovas, J. L., and Kornberg, H. L., Fine control of phos-phopyruvic carboxylase activity in Escherichia coli. Biochim. Biophys. Acta, 96, 169-172 (1965).
    • (1965) Biochim. Biophys. Acta , vol.96 , pp. 169-172
    • Canovas, J.L.1    Kornberg, H.L.2
  • 37
    • 0014011440 scopus 로고
    • Phosphoenolpyruvate carboxylase: Activation by nucleotides as a possible compensatory feedback effect
    • Sanwal, B. D. and Maeba, P., Phosphoenolpyruvate carboxylase: Activation by nucleotides as a possible compensatory feedback effect. J. Biol. Chem., 241, 4557-4562 (1966).
    • (1966) J. Biol. Chem. , vol.241 , pp. 4557-4562
    • Sanwal, B.D.1    Maeba, P.2
  • 38
    • 0014028086 scopus 로고
    • Interaction of macroions and di-oxane with the allosteric phosphoenolpyruvate carboxylase
    • Sanwal, B. D., Maeba, P. and Cook, R. A., Interaction of macroions and di-oxane with the allosteric phosphoenolpyruvate carboxylase. J. Biol. Chem., 241, 5177-5182 (1966).
    • (1966) J. Biol. Chem. , vol.241 , pp. 5177-5182
    • Sanwal, B.D.1    Maeba, P.2    Cook, R.A.3
  • 39
    • 0013844919 scopus 로고
    • Feedback inhibition of phosphoenolpyruvate carboxylase of
    • Maeba, P. and Sanwal, B. D., Feedback inhibition of phosphoenolpyruvate carboxylase of Salmonella. Biochem. Biophys. Res. Commun., 21, 503-508 (1965).
    • (1965) Biochem. Biophys. Res. Commun. , vol.21 , pp. 503-508
    • Maeba, P.1    Sanwal, B.D.2
  • 40
    • 0014026183 scopus 로고
    • Regulation of the activity of phosphoenolpyruvate carboxylase by fructose diphosphate
    • Sanwal, B. D. and Maeba, P., Regulation of the activity of phosphoenolpyruvate carboxylase by fructose diphosphate. Biochem. Biophys. Res. Commun., 22, 194-199 (1966).
    • (1966) Biochem. Biophys. Res. Commun. , vol.22 , pp. 194-199
    • Sanwal, B.D.1    Maeba, P.2
  • 41
    • 0017350841 scopus 로고
    • Purification and properties of acetyl coenzyme A synthetase from baker’s yeast
    • Frenkel, E. P. and Kitchens, R. L., Purification and properties of acetyl coenzyme A synthetase from baker’s yeast. J. Biol. Chem., 252, 504-507 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 504-507
    • Frenkel, E.P.1    Kitchens, R.L.2
  • 42
    • 0015618419 scopus 로고
    • The molecular weight and thiol residues of acetyl-coenzyme A synthetase from ox heart mitochondria
    • Londesborough, J. C., Yuan, S. L. and Webster, L. T., Jr., The molecular weight and thiol residues of acetyl-coenzyme A synthetase from ox heart mitochondria. Biochem. J., 133, 23-36 (1973).
    • (1973) Biochem. J. , vol.133 , pp. 23-36
    • Londesborough, J.C.1    Yuan, S.L.2    Webster, L.T.3
  • 43
    • 0043166387 scopus 로고
    • Multiple forms of yeast acetyl-CoA synthetase
    • DeVincenzi, D. L. and Klein, H. P., Multiple forms of yeast acetyl-CoA synthetase. Fed. Proc., 29, 872 (1970).
    • (1970) Fed. Proc. , vol.29 , pp. 872
    • Devincenzi, D.L.1    Klein, H.P.2
  • 44
    • 0013814145 scopus 로고
    • Studies of the acetyl coenzyme A synthetase reaction. II. Crystalline acetyl coenzyme A synthetase
    • Webster, L. T. Jr., Studies of the acetyl coenzyme A synthetase reaction. II. Crystalline acetyl coenzyme A synthetase. J. Biol. Chem., 240, 4158-4163 (1965).
    • (1965) J. Biol. Chem. , vol.240 , pp. 4158-4163
    • Webster, L.T.1
  • 45
    • 0013815509 scopus 로고
    • Studies of the acetyl coenzyme A synthetase reaction. III. Evidence of a double requirement for divalent cations
    • Webster, L. T., Jr., Studies of the acetyl coenzyme A synthetase reaction. III. Evidence of a double requirement for divalent cations. J. Biol. Chem., 240, 4164-4169 (1965).
    • (1965) J. Biol. Chem. , vol.240 , pp. 4164-4169
    • Webster, L.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.