Summary
Methods for establishing the kinetic mechanisms of dehydrogenase reactions are dealt with in general terms. Examples ranging from relatively simple to obviously complex enzymes, and showing various mechanistic features of interest and importance are discussed.
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References
Abdallah, M.A., Biellmann, J.-F. & Lagrange, P. (1979) Biochemistry 18, 836–838.
Adams, J.A., Jacobson, H.I., Levy, H.R. & Talalay, P. (1965) Steroids, Suppl. 1, 75–84.
Ainslie, G.R. & Cleland, W.W. (1972) J. Biol. Chem. 247, 946–951.
Ainsworth, S. (1975) J. theor. Biol. 50, 129–151.
Ainsworth, S. (1977a) J. theor. Biol. 64, 381–389.
Ainsworth, S. (1977b) In “Steady-state enzyme kinetics”, pp. 182–201, Macmillan, London.
Alberty, R.A. (1953) J. Am. Chem. Soc. 75, 1928–1932.
Alberty, R.A. (1958) J. Am. Chem. Soc. 80, 1777–1782.
Askelöf, P., Korsfeldt, M. & Mannervik, B. (1976) Eur. J. Biochem. 69, 61–67.
Atkins, G.L. & Nimmo, I.A. (1975) Biochem. J. 149, 775–777.
Bardsley, W.G. & Childs, R.E. (1975) Biochem. J. 149, 313–328.
Barnes, L.D., McGuire, A.J. & Atkinson, D.E. (1972) Biochemistry, 11, 4322–4328.
Bell, J.E. & Dalziel, K. (1975a) Biochim. Biophys. Acta, 391, 249–258.
Bell, J.E. & Dalziel, K. (1975b) Biochim. Biophys. Acta, 410. 243–251.
Bernhard, S.A., Dunn, M.F., Luisi, P.L. & Schack, P. (1970) Biochemistry, 9, 185–192.
Betz, G. (1971) J. Biol. Chem. 246, 2063–2068.
Biellmann, J.-F., Lapinte, C., Haid, E. & Weimann, G. (1979) Biochemistry, 18, 1212–1217.
Biesecker, G., Harris, J.I., Thierry, J.C., Walker, J.E. & Wonacott, R.J. (1977) Nature (London) 266, 328–333.
Birken, S. & Pisano, M.A. (1976) J. Bacteriol. 125, 225–232.
Blaner, W.S. & Churchich, J. (1979) J. Biol. Chem. 254, 1794–1798.
Boers, W. & Verhoeven, J.W. (1973) Biochim. Biophys. Acta, 328, 1–9.
Bosron, W.F., Li, T.-K., Dafeldecker, W.P. & Vallee, B.L. (1979) Biochemistry, 18, 1101–1105.
Boyer, P.D. (1959) Arch. Biochem. Biophys. 82, 387–410.
Boyer, P.D. & Silverstein, E. (1963) Acta Chem. Scand., 17, 5195 - S202.
Britton, H.G. (1966) Arch. Biochem. Biophys. 117, 167–183.
Britton, H.G. (1973) Biochem. J. 133, 255–261.
Britton, H.G. (1977) Biochem. J. 161, 517–526.
Britton, H.G. & Clarke, J.B. (1968) Biochem. J. 110, 161–179.
Britton, H.G. & Dann, L.G. (1978) Biochem. J. 169, 29–37.
Brodelius, P.E. & Kaplan, N.O. (1979) Arch. Biochem. Biophys., 194, 449–456.
Brooks, R.L. & Shore, J.D. (1971) Biochemistry, 10, 3855–3858.
Buc, H. (1967) Biochem. Biophys. Res. Comm., 28, 59–64.
Buehner, M., Ford, G.C., Moras, D., Olsen, K.W. & Rossmann, M.G. (1974) J. Mol. Biol., 90, 25–49.
Burns, D.J.W., Engel, L.L. & Bethune, J.L. (1972) Biochemistry, 11, 2699–2703.
Byers, L.D., She, H.S. & Alayoff, A. (1979) Biochemistry, 18, 2471–2480.
Callewaert, D.M., Rosemblatt, M.S. & Tchen, T.T. (1974) J. Biol. Chem., 249, 1737–1741.
Cannistraro, V.J., Borack, L.I. & Chase, T. (1979) Biochim. Biophys. Acta, 569, 1–5.
Cantwell, A.M. & Dennis, D. (1970) Biochem. Biophys. Res. Commun., 41, 1166–1170.
Chang, H.-L., Holten, D. & Karin, R. (1979) Can. J. Biochem., 57, 396–401.
Christensen, U., Tüchsen, E. & Andersen, B. (1975) Acta Chem. Scand., B29, 81–87.
Cleland, W.W. (1963a) Biochim. Biophys. Acta, 67, 104–137.
Cleland, W.W. (1963b) Biochim. Biophys. Acta, 67, 173–187.
Cleland, W.W. (1963c) Biochim. Biophys. Acta, 67, 188–196.
Cleland, W.W. (1963d) Nature (London), 198, 463–465.
Cleland, W.W. (1967a) Ann. Rev. Biochem., 36, 77–112.
Cleland, W.W. (1967b) Adv. Enzymol., 29, 1–32.
Cleland, W.W. (1970) In “The enzymes”, (Boyer, P.D. ed.), 3rd edn. Vol. 1, pp. 1–65 Academic Press, New York.
Cleland, W.W. (1975) Biochemistry, 14, 3220–3224.
Cleland, W.W. (1977) Adv. Enzymol., 45, 273–387.
Colquhounm D. (1971) Lectures on biostatistics, pp. 257–272, Clarendon Press, Oxford.
Conway, A. & Kosland, D.E. Jr. (1968) Biochemistry 7, 4011–4022.
Cornish-Bowden, A. (1976) Biochem. J. 159, 167.
Cornish-Bowden, A. & Koshalnd, D.E. Jr. (1975) J. M. D.G. & Fisher, H.Fol. Biol. 95, 201–212.
Cross. D.G. & Fisher, H.F. (1970) J. Biol.Chem. 245, 2612–2621.
Dalziel, K. (1957) Acta Chem. Scand. 11, 1706–1723.
Dalziel, K. (1958) Trans. Faraday Soc. 54, 1247–1253.
Dalziel, K. (1961a) Biochem. J. 80, 440–445.
Dalziel, K. (1961b) Nature (London), 191, 1098–1099.
Dalziel, K. (1962a) Biochem. J. 84, 240–244.
Dalziel, K. (1962b) Biochem. J. 84, 244–254.
Dalziel, K. (1962c) Nature (London) 195, 384–385.
Dalziel, K. (1963a) J. Biol. Chem. 238, 1538–1543.
Dalziel, K. (1963b) J. Biol. Chem. 238, 2850–2858.
Dalziel, K. (1963c) Nature (London), 197, 462–464.
Dalziel, K. (1969) Biochem. J. 114, 547–556.
Dalziel, K. (1975) In “The enzymes”, 3rd edn. (Boyer, P.D. ed.),Vol. 11, pp. 1–60, Academic Press, New York.
Dalziel, K. & Dickinson, F.M. (1966a) Biochem. J. 100, 34–46.
Dalziel, K. & Dickinson, F.M. (1966b) Biochem. J. 100, 491–500.
Dann, L.G. & Britton, H.G. (1978) Biochem. J. 169, 39–54.
Davidson, W.S. & Flynn, G.T. (1979) Biochem. J. 171, 595–601.
Davidson, B.E., Sajgo, M., Noller, H.F. & Harris, J.I. (1967) Nature (London) 216, 1181–1185.
DeVjilder, J.J.M. & Stater, E.C. (1968) Biochim. Biophys. Acta 167, 23–34.
Dickinson, F.M. & Dalziel, K. (1967) Biochem. J. 104, 165–172.
Doublet, M.-O. & Olomucki, A. (1975) Eur. J. Biochem. 59, 175–183.
Doublet, M.-O., Olomucki, A., Baici, A. & Luisi, P.L. (1975) Eur. J. Biochem. 59, 185–191
Dowd, J.E. & Riggs, D.S. (1965) J. Biol. Chem., 240, 863–869.
Dubrow, R. & Pizer, L.I. (1977) J. Biol. Chem., 252, 1539–1551.
Dunn, M.F. (1974) Biochemistry, 13, 1146–1151.
Dunn, M.F., Bernhard, S.A., Anderson, D., Copeland, A., Morris, R.G. & Rogue, J.-P. (1979) Biochemistry 18, 2346–2354.
Dworschack, R.T. & Plapp, B.U. (1977) Biochemistry, 16, 2716–2725.
Eigen, M. & de Maeyer, L. (1963) In “Techniques of Organic Chemistry”, ( Friess, S.L., Lewis, E.S. & Weissberger, A. eds.), Vol. 8 pp. 895–1054 New York, Interscience.
Eigen, M. & Hammes, G.G. (1963) Adv. Enzymol. 25, 1–38.
Eisenbern, H., Josephs, R. & Reisler, E. (1976) Adv. Protein. Chem., 30, 101–181.
Eisenthal, R. & Cornsih-Bowden, A. (1974) Biochem. J. 139, 715–720.
Endrenyi, L., Chan, M.-S. & Wong, J.T.-F. (1971) Can. J. Biochem. 49, 581–598.
Fahien, L.A. (1966) J. Biol. Chem., 241, 4115–4123.
Fawcett, C.P., Ciotti, M.M. & Kaplan, N.O. (1961) Biochim. Acta 54, 210–212.
Fine, I.H., Kaplan, N.O. & Kuftinec, P. (1963) Biochemistry 2, 116–121.
Fisher, H.F. (1973) Adv. Enzymol., 39, 369–417.
Flores, R. (1979) TIBS, 4, N32 - N33.
Flynn, T.G., Shires, J. & Walton, D.J. (1975) J. Biol. Chem., 250, 2933–2940.
Ford, W.T., Graham, E.W. & Cram, D.J. (1967) J. Am.Chem. Soc., 89, 4661–4669.
Fromm, H.J. (1963) J. Biol. Chem., 238, 2938–2944.
Fromm, H.J. (1975) Initial rate enzyme kinetics Springer-Verlag, Berlin.
Furfine, C.A. & Velick, S.F. (1965) J. Biol. Chem., 240, 844–855.
Gezici, S. & Dinagk, G.F. (1979) Int. Biochem., 10, 427–432.
Gibson, Q.H. & Milnes, L. (1964) Biochem. J., 91, 161–171.
Glick, N., Landman, A.D. & Roufogalis, B.D. (1979) TIBS, 4, N82 - N83.
Goldin, B.R. & Frieden, C. (1972) Curr. Top. Cell. Regul., 4, 77–117.
Groman, E.U., Schultz, R.M. & Engel, L.L. (1975) J. Biol. Chem., 250, 5450–5454.
Gutfreund, H. (1971) Ann. Rev. Biochem., 40, 315–341.
Hadorn, M. (1975) Doctoral Diss. ETH 5558, ZĂĽrich.
Hadorn, M., John, U.A., Meier F.K. & Dutler, H. (1975) Eur. J. Biochem., 54, 65–73.
Hakala, M.T., Glaid, A.J. & Schwert, G.W. (1956) J. Biol. Chem. 221, 191–209.
Halvorson, H.R. (1979) Biochemistry, 18, 2480–2487.
Hanes, C.S., Bronskill, P.M., Gurr, P.A. & Wong, J.T.-F. (1972) Can. J. Biochem., 50, 1385–1413.
Hardman, M.J. & Blackwell, L.F. (1974) Biochim. Biophys. Acta, 350, 247–252.
Harris, J.I. & Perham, R.N. (1968) Nature (London) 219, 1025–1028.
Harris, J.I. & Waters, M. (1976) In “The enzymes”, (Boyer, P.D. ed.), 3rd edn., Vol. 13, pp. 1–49, Academic Press, New York.
Harris, J.I., Meriwether, B.P. & Park, J.H. (1963) Nature (London), 198, 154–157.
Hathaway, J.A. & Atkinson, D.E. (1963) J. Biol. Chem., 238, 2875–2881.
Heffron, J.J.A. (1979) TIBS, 4, N133.
Henis, Y.I., Levitzki, A. & Gafni, A. (1979) Eur. J. Biochem., 97, 519–528.
Hijazi, N.H. & Laidler, K.J. (1973) Can. J. Biochem., 51, 832–840.
Hillman, J.D. (1979) Biochem. J., 179, 99–107.
Hochreiter, M.C., Patek, D.R. & Schellenberg, K.A. (1972) J. Biol. Chem., 247, 6271–6276.
Hocking, J.D. & Harris, J.I. (1976) In “Enzymes and proteins from thermophilic microorganisms”, ( Zuber, H., ed.), Birkhauser Verlag, Basel.
Horn, A. & Börnig, H. (1969) FEBS Letters, 3, 325–329.
Hou, C.T., Patel, R.N., Laskin, A.I., Barnabe, N. & Marczak, I. (1979) FEBS Letters, 101, 179–183.
Huijing, F. (1979) TIBS, 4, N132.
Hurst, R.O. (1969) Can. J. Biochem., 47, 941–944.
Ingraham, L.I. & Makower, B. (1954) J. Phys. Chem., 58, 266–270.
Inoue, K., Nishimukai, H. & Yamasawa, K. (1979) Biochim. Biophys. Acta, 569, 117–123.
Jaenicke, R., Rudolph, R. & Heider, I. (1979) Biochemistry, 18, 1217–1223.
Jarabak, J. & Sack, G.H. (1969) Biochemistry, 8, 2203–2212.
Johansen, G. & Lumry, R. (1961) Compt. Rend. Tray. Lab. Carlsberg, 32, 185–214.
Jones, G.M.T. & Harris, J.I. (1972) FEBS Lett., 22, 185–189.
Karavolas, H.J., Baedecker, M.L. & Engel, L.L. (1970) J. Biol. Chem., 245, 4948–4952.
Kegeles, G. (1979) FEBS Letters, 103, 5–6.
Kellershohn, N. & Seydoux, F.J. (1979) Biochemistry, 18, 2465–2470.
Kimball, D.F. (1977) Ph.D. dissertation, University of Oregon.
Kimball, D.F., Peterson, L., McLoughlin, D.J. & Wolfe, R.G. (1979) Arch. Biochem. Biophys., 195, 66–73.
King, E.L. & Altman, C. (1956) J. Phys. Chem., 60, 1375–1378.
Kirschner, K., Eigen, M., Bittman, R. & Voight, B. (1966) Proc. Nat. Acad. Sci., U.S.A., 56, 1661–1667.
Kirtley, M.E. & Koshland, D.E. (1967) J. Biol. Chem., 242, 4192–4205.
Klinman, J.P. (1972) J. Biol. Chem., 247, 7977–7987.
Klinman, J.P. (1978) Adv. Enzymol., 46, 415–494.
Knowles, J.R. (1976) Critical Reviews of Biochemistry, 4, 165–173.
Kordal, R.J. & Parsons, S.M. (1979) Arch. Biochem. Biophys., 194, 439–448.
Koshland, D.E. Jr. (1953) Biol. Revs., 28, 416–436.
Koshland, D.E. Jr. (1955) Discuss. Faraday Soc., 20, 142–148.
Koshland, D.E. Jr. (1956) J. Cell. comp. Physiol., 47, Suppl. 1, 217–234.
Koshland, D.E. Jr. (1970) In “The enzymes”, ( Boyer, P.D., ed.), 3rd edn., pp. 342–396 Academic Press, New York.
Koshland, D.E. Jr., Nemethy, G. & Filmer, D. (1966) Biochemistry 5, 365–385.
Krause, J., Bohner, M. & Sund, H. (1974) Eur. J. Biochem., 41, 593–602.
Kuehn, G.D., Barnes, L.D. & Atkinson, D.E. (1971) Biochemistry, 10, 3945–3951.
Kvassman, J.. & Pettersson, G. (1976) Eur. J. Biochem., 69, 279–287.
Kvassman, J. & Pettersson, G. (1978) Eur. J. Biochem., 87, 417–427.
Laidler, K.J. (1955a) Trans. Faraday Soc., 51, 528–539.
Laidler, K.J. (1955b) Discuss Faraday Soc., 20, 83–96.
Laidler, K.J. (1956) Trans. Faraday Soc., 52, 1374–1382.
Lazdunski, M. (1974) Progress in Bioorganic Chemistry, 3, 81–140.
Leibman, D.Y. & Nesterov, U.P. (1979) Int. J. Biochem., 10, 645–649.
Levitzki, A. & Koshland, D.E. (1976) Current Topics in Cellular Regulation, 10, 1–40.
Lewis, E.S. & Robinson, J.K. (1968) J. Am. Chem. Soc., 90, 4337–4344.
Luisi, P.L. & Bignetti, E. (1974) J. Mol. Biol., 88, 653–670.
Luisi, P.L. & Favilla, R. (1972) Biochemistry, 11, 2303–2310.
Lutstorf, U.M., Schdürch, P.M. & von Wartburg, J.P. (1970) Eur. J. Biochem., 17, 497–508.
McFarland, J. & Bernhard, S.A. (1972) Biochemistry, 11, 1486–1493.
McFarland, J.T. & Chu, Y.-H. (1975) Biochemistry, 14, 1140–1146.
McFarland, J.T., Chu, Y.-H. & Jacobs, J.W. (1974) Biochemistry, 13, 65–69.
MacGibbon, A.K.H., Motion, R.L., Crow, K.E., Buckley, P.D. & Blackwell, L.F. (1979) Eur. J. Biochem., 96, 585–595.
Meier, F.K. (1975) Doctoral Diss. ETH 5559, ZĂĽrich.
Meunier, J.-C. & Dalziel, K. (1978) Eur. J. Biochem., 82, 483–492.
Monneuse-Doublet, M.-O., Olomucki, H. & Buc, J. (1978) Eur. J. Biochem., 84, 441–448.
Monod, J., Wyman, J. & Changeux, J. (1965) J. Mol. Biol., 12, 88–118.
Moon, K., Piszkiewicz, D. & Smith, E.L. (1972) Proc. Natl. Acad. Sci., U.S.A., 69, 1380–1383.
Northrop, D.B. (1975) Biochemistry, 14, 2644–2651.
Orsi, B.A. & Cleland, W.W. (1972) Biochemistry, 11, 102–109.
Pal, K.P. & Colman, R.F. (1979) Biochemistry, 18, 838–845.
Paul, F., Coulet, P.R., Gautheron, D.C. & Engasser, J.-M. (1978) Biotechnology & Bioengineering, 22, 1785–1796.
Paulus, H. & DeRiel, J.K. (1975) J. Mol. Biol., 97, 667–671.
Pettersson, G. (1969) Acta Chem. Scand., 23, 2717–2726.
Pettersson, G. (1970) Acta Chem. Scand., 24, 1271–1274.
Pettersson, G. (1972) In “Structure and Function of Oxidation-Reduction Enzymes”, ( Rkeson, R. & Ehrenberg, A., eds.), pp. 739–743, Pergamon Press, Oxford.
Pettersson, G. (1974) Eur. J. Biochem., 46, 1–4.
Pettersson, G. (1976) Eur. J. Biochem., 69, 273–278.
Pettersson, G. (1977) Biochem. Biophys. Acta, 484, 199–207.
Pettersson, G. (1978) Acta Chem. Scand., B32, 437–446.
Pietruszko, R., Clark, A., Graves, J.M.H. & Ringold, H.J. (1966) Biochem. Biophys. Res. Comm., 23, 526–534.
Plapp, B.U., Brooks, R.L. & Shore, J.D. (1973) J. Biol. Chem., 248, 3470–3475.
Plowman, K.M. (1972) In “Enzyme kinetics”, pp. 76–90, McGraw Hill Book Co., New York.
Porter, W.R. & Trager, W.F. (1977) Biochem. J., 161, 293–302.
Raval, D.N. & Wolfe, R.G. (1962a) Biochemistry, 1, 263–269.
Raval, D.N. & Wolfe, R.G. (1962b) Biochemistry, 1, 1112–1117.
Rose, I.A. (1961) J. Biol. Chem., 236, 603–609.
Rosemblatt, M.S., Callewaert, D.M.. & Tchen, T.T. (1973) J. Biol. Chem., 248, 6014–6018.
Scheek, R.M. & Slater, E.C. (1978) Biochim. Biophys. Acta, 526, 13–24.
Scheek, R.M., Berden, J.A., Hooghiemstra, R., & Slater, E.C. (1979) Biochim. Biophys. Acta, 569, 124–134.
Schimerlik, M.I., Rife, J.E. & Cleland, W.W. (1975) Biochemistry, 14, 5347–5354.
Segal, H.L. & Boyer, P.D. (1953) J. Biol. Chem., 204, 262–272.
Seydoux, F. & Bernhard, S.A. (1974) Biophys. Chem. 1, 161–174.
Seydoux, F., Malhorta, O.P. & Bernhard, S.A. (1974) Critical Reviews in Biochemistry, 2, 227–257.
Shaw, M.A. & Jeffery, J. (1978) Biochem. Soc. Trans., 6, 205–207.
Shikita, M. & Tsuneoka, K. (1976). FEBS Letters, 66, 4–7.
Shore, J.D. & Gutfreund, H. (1970) Biochemistry, 9, 4655–4659.
Siano, D.B., Zyskind, J.W. & Fromm, H.J. (1975) Arch. Biochem. Biophys., 170, 587–600.
Silverstein, E. & Boyer, P.D. (1964a) J. Biol. Chem., 239, 3901–3907.
Silverstein, E. & Boyer, P.D. (1964b) J. Biol. Chem., 239, 3908–3914.
Silverstein, E. & Boyer, P.D. (1966) In “Biochemical Preparations”, ( Maehly, A.C., ed.), Vol. 11, pp. 8995, John Wiley, New York.
Silverstein, E. & Sulebele, G. (1969) Biochemistry, 8, 2543–2550.
Simon, H. & Palm, D. (1966) Angew. Chem. Int. Ed. Engl., 5, 920–933.
Skâlhegg, B.A. (1974) Eur. J. Biochem., 46, 117–125.
Skâlhegg, B.A. (1975) Eur. J. Biochem., 50, 603–609.
Smith, H. (1968) J. Reprod. Fert. Suppl., 5, 3–12.
Smith, M.G. (1962) Biochem. J., 83, 135–144.
Smith, C.M. & Velick, S.F. (1972) J. Biol. Chem., 247, 273–284.
Smith, E.L., Austen, B.M., Blumenthal, K.M. & Nyc. J.F. (1975) In “The Enzymes”, (Boyer, P.D. ed.) 3rd edn., Vol. 11, pp. 294–367, Academic Press, New York.
Squire, P.G., Delin, S. & Porath, J. (1964) Biochim. Biophys. Acta, 89, 409–421.
Storer, A.C., Darlison, M.G. & Cornish-Bowden, A. (1975) Biochem. J., 151, 361–367.
Sund, H., Markau, K. & Koberstein, R. (1975) In “Biological macromolecules, subunits in biological systems, part C”, ( Timasheff, S.N. & Fasman, G.D., eds.), Vol. 7, pp. 225–287 Marcel Dekker, New York.
Svasti, J. (1979) TIBS, 4, N133 - N134.
Takenaka, Y. & Schwert, G.W. (1956) J. Biol. Chem., 223, 157–170
Theorell, H. & Chance, B. (1951) Acta Chem. Scand., 5, 1127–1144.
Toews, C.J. (1967) Biochem. J., 105, 1067–1073.
Tomkins, G.M., Yielding, K.L., Curran, J.F., Summers, M.R. & Bitensky, M.W. (1965) J. Biol. Chem., 240, 3793–3798.
Ureta, T. (1978) Current Topics in Cellular Regulation, 13, 233–258.
Velick, S.F., Hayes, J.E. & Harting, J. (1953) J. Biol. Chem., 203, 527–544.
Walsall, E.P., Lyons, S.A. & Metzger, R.P. (1978) Comp. Biochem. Physiol., 59B, 213–218.
Warren, J.C. & Crist, R.D. (1967) Arch. Biochem. Biophys., 118, 577–584.
Weidig, C.F., Halvorson, H.R. & Shore, J.D. (1977) Biochemistry, 16, 2916–2922.
Wermuth, B., Munch, J.D.B., & von Wartburg, J.-P. (1977) J. Biol. Chem., 252, 3821–3828.
Westheimer, F.H. (1961) Chem. Rev., 61, 265–273.
Whitehead, E.P. & Egmond, M.R. (1979) Biochem. J., 177, 631–639.
Wiberg, K.B. & Motell, E.L. (1963) Tetrahedron, 19, 2009–2023.
Wilkinson, G.N. (1961) Biochem. J., 80, 324–332.
Wong, J.T.-F. & Hanes, C.S. (1962) Canad. J. Biochem. & Physiol., 40, 763–804.
Wright, I.P. & Sundaram, T.K. (1979) Biochem. J., 177, 441–448.
Wyrambic, D. & Grisebach, H. (1979) Eur. J. Biochem., 97, 503–509.
Zantema, A., Vogel, H.J. & Robillard, G.T. (1979) Eur. J. Biochem., 96, 453–463.
Zewe, V. & Fromm, H.J. (1962) J. Biol. Chem., 237, 1668–1675.
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Jeffery, J. (1980). Kinetic Aspects of Soluble Dehydrogenases Requiring Nicotinamide Coenzymes. In: Jeffery, J. (eds) Dehydrogenases. Experientia Supplementum, vol 36. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-5419-1_1
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