Amino acid dehydrogenases

Industrial Enzymes: Structure, Function and Applications

Volumn , Issue , 2007, Pages 489-504

  Seah, Stephen Y K ^a  

^a UNIVERSITY OF GUELPH   (Canada)

Author keywords

[No Author keywords available]

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EID: 84856292380     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/1-4020-5377-0_28     Document Type: Chapter

References (59)

1. Asano, Y., Nakazawa, A. and Endo, K. (1987a). Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization. J. Biol. Chem. 262, 10346-10354.
2. Asano, Y., Nakazawa, A., Endo, K., Hibino, Y., Ohmori, M., Numao, N. and Kondo, K. (1987b). Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning. Eur. J. Biochem. 168, 153-159.
3. Baker, P.J., Turnbull, A.P., Sedelnikova, S.E., Stillman, T.J. and Rice, D.W. (1995). A role for quaternary structure in the substrate specificity of leucine dehydrogenase. Structure. 3, 693-705.
4. Baker, P.J., Waugh, M.L., Wang, X.G., Stillman, T.J., Turnbull, A.P., Engel, P.C. and Rice, D.W. (1997). Determinants of substrate specificity in the superfamily of amino acid dehydrogenases. Biochemistry 36, 16109-16115.
5. Bhuiya, M.W., Sakuraba, H., Ohshima, T., Imagawa, T., Katunuma, N. and Tsuge, H. (2005). The first crystal structure of hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. 2005. J Mol Biol. 345, 325-337.
6. Britton, K.L., Baker, P.J., Engel, P.C., Rice, D.W. and Stillman, T.J. (1993). Evolution of substrate diversity in the superfamily of amino acid dehydrogenases. Prospects for rational chiral synthesis. J. Mol. Biol. 234, 938-945.
7. Britton, K.L., Stillman, T.J., Yip, K.S., Forterre, P., Engel, P.C. and Rice, D.W. (1998). Insights into the molecular basis of salt tolerance from the study of glutamate dehydrogenase from Halobacterium salinarum. J. Biol. Chem. 273, 9023-9030.
8. Britton, K.L., Yip, K.S., Sedelnikova, S.E., Stillman, T.J., Adams, M.W., Ma, K., Maeder, D.L., Robb, F.T., Tolliday, N., Vetriani, C., Rice, D.W. and Baker, P.J. (1999). Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus. J. Mol. Biol. 293, 1121-1132.
9. Brunhuber, N.M. and Blanchard, J.S. (1994). The biochemistry and enzymology of amino acid dehydrogenases. Crit. Rev. Biochem. Mol. Biol. 29, 415-467.
10. Brunhuber, N.M., Thoden, J.B., Blanchard, J.S. and Vanhooke, J.L. (2000). Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity. Biochemistry. 39, 9174-9187.
11. Busca, P., Paradisi, F., Moynihan, E., Maguirem, A.R. and Engel, P.C. (2004). Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis. Org. Biomol. Chem. 2, 2684-2691.
12. Dean, J.L., Wang, X.G., Teller, J.K., Waugh, M.L., Britton, K.L., Baker, P.J., Stillman, T.J., Martin, S.R., Rice, D.W. and Engel, P.C. (1994). The catalytic role of aspartate in the active site of glutamate dehydrogenase. Biochem. J. 301, 13-16.
13. Elcock, A.H. (1998). The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J. Mol. Biol. 284, 489-502.
14. Galkin, A., Kulakova, L., Yoshimura, T., Soda, K. and Esaki, N. (1997). Synthesis of optically active amino acids from alpha-keto acids with Escherichia coli cells expressing heterologous genes. Appl. Environ. Microbiol. 63, 4651-4656.
15. Guthrie, R. and Susi, A. 1963. A simple phenylalanine method for detecting phenylketonuria in large populations of newborn infants. Pediatrics. 32, 338-343.
16. Hayden, B.M., Dean, J.L., Martin, S.R. and Engel, P.C. (1999). Chemical rescue of the catalytically disabled clostridial glutamate dehydrogenase mutant D165S by fluoride ion. Biochem. J. 340, 555-560.
17. Huang, T., Warsinkem, A., Kuwana, T. and Scheller, F.W. (1998). Determination of L-phenylalanine based on an NADH-detecting biosensor. Anal. Chem. 70, 991-997.
18. Hudson, R.C. and Daniel, R.M. (1993) L-glutamate dehydrogenases: distribution, properties and mechanism. Comp. Biochem. Physiol. 106B, 767-792.
19. Hummel, W., Schutte, H. and Kula, M.R. (1988). Enzymatic determination of L-phenylalanine and phenylpyruvate with L-phenylalanine dehydrogenase. Anal. Biochem. 170, 397-401.
20. Hummel, W. and Kula, M.-R. (1989). Dehydrogenases for the synthesis of chiral compounds. Eur. J. Biochem. 184, 1-13.
21. Hummel, W., Kuzu, M. and Geueke, B. (2003). An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-leucine. Org. Lett. 5, 3649-3650.
22. Hyun, C.G., Kim, S.S., Park, K.H. and Suh, J.W. (2000). Valine dehydrogenase from Streptomyces albus: gene cloning, heterologous expression and identification of active site by site-directed mutagenesis. FEMS Microbiol. Lett. 182, 29-34.
23. Kataoka, K., Tanizawa, K., Fukui, T., Ueno, H., Yoshimura, T., Esaki, N. and Soda, K. (1994). Identification of active site lysyl residues of phenylalanine dehydrogenase by chemical modification with methyl acetyl phosphate combined with site-directed mutagenesis. J. Biochem. 116, 1370-1376.
24. Knapp, S., de Vos, W.M., Rice, D. and Ladenstein, R. (1997). Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0A resolution. J. Mol. Biol. 267, 916-932.
25. Lebbink, J.H., Knapp, S., van der Oost, J., Rice, D., Ladenstein, R. and de Vos, W.M. (1998). Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region. J. Mol. Biol. 280, 287-296.
26. Lebbink, J.H., Knapp, S., van der Oost, J., Rice, D., Ladenstein, R. and de Vos, W.M. (1999). Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface. J. Mol. Biol. 289, 357-369.
27. Leiser, A., Birch, A. and Robinson, J.A. (1996). Cloning, sequencing, overexpression in Escherichia coli, and inactivation of the valine dehydrogenase gene in the polyether antibiotic producer Streptomyces cinnamonensis. Gene 177, 217-222.
28. Livesey, G. and Lund, P. (1988). Determination of branched-chain amino and keto acids with leucine dehydrogenase. Methods Enzymol. 166, 3-10.
29. Massey, L.K., Sokatch, J.R. and Conrad, R.S. (1976). Branched-chain amino acid catabolism in bacteria. Bacteriol. Rev. 40, 42-54.
30. Miñambres, B., Olivera, E.R., Jensen, R.A. and Luengo, J.M. (2000). A new class of glutamate dehydrogenases (GDH). Biochemical and genetic characterization of the first member, the AMP-requiring NAD-specific GDH of Streptomyces clavuligerus. J. Biol. Chem. 275, 39529-39542.
31. Morishita, Y., Nakane, K., Fukatsu, T., Nakashima, N., Tsuji, K., Soya, Y., Yoneda, K., Asano, S. and Kawamura, Y. (1997). Kinetic assay of serum and urine for urea with use of urease and leucine dehydrogenase. Clin. Chem. 43, 1932-1936.
32. Naruse, H., Ohashi, Y.Y., Tsujii, A., Maeda, M., Nakamura, K., Fujii, T., Yamaguchi, A., Matsumoto, M. and Shibata, M. (1992). A method of PKU screening using phenylalanine dehydrogenase and microplate system. Screening 1, 63-66.
33. Ohshima, T., Nishida, N., Bakthavatsalam, S., Kataoka, K., Takada, H., Yoshimura, T., Esaki, N. and Soda K. (1994). The purification, characterization, cloning and sequencing of the gene for a halostable and thermostable leucine dehydrogenase from Thermoactinomyces intermedius. Eur. J. Biochem. 222, 305-312.
34. Oikawa, T., Yamanaka, K., Kazuoka, T., Kanzawa, N. and Soda, K. (2001). Psychrophilic valine dehydrogenase of the antarctic psychrophile, Cytophaga sp. KUC-1: purification, molecular characterization and expression. Eur. J. Biochem. 268, 4375-4383.
35. Patel, R.N. (2001). Enzymatic synthesis of chiral intermediates for Omapatrilat, an antihypertensive drug. Biomol. Eng. 17, 167-182.
36. Peterson, P.E. and Smith, T.J. (1999). The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery. Structure Fold. Des. 7, 769-782.
37. Rice, D.W., Hornby, D.P. and Engel, P.C. (1985). Crystallization of an NAD+-dependent glutamate dehydrogenase from Clostridium symbiosum. J. Mol. Biol. 181, 147-149.
38. Rife, J.E. and Cleland, W.W. (1980). Determination of the chemical mechanism of glutamate dehydrogenase from pH studies. Biochemistry 19, 2328-2333.
39. Roch-Ramel, F. (1967). An enzymic and fluorophotometric method for estimating urea concentrations in nanoliter specimens. Anal. Biochem. 21, 372-381.
40. Seah, S.Y.K., Britton, K.L., Baker, P.J., Rice, D.W., Asano, Y. and Engel, P.C. (1995). Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis. FEBS Lett. 370, 93-96.
41. Seah, S.Y.K., Britton, K.L., Rice, D.W., Asano, Y. and Engel, P.C. (2002). Single amino acid substitution in Bacillus sphaericus phenylalanine dehydrogenase dramatically increases its discrimination between phenylalanine and tyrosine substrates. Biochemistry 41, 11390-11397.
42. Seah, S.Y.K., Britton, K.L., Rice, D.W., Asano, Y. and Engel, P.C. (2003). Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase activity with guidance from homology-based modelling. Eur. J. Biochem. 270, 4628-4634.
43. Sekimoto, T., Matsuyama, T., Fukui, T. and Tanizawa, K. (1993). Evidence for lysine 80 as general base catalyst of leucine dehydrogenase. J. Biol. Chem. 268, 27039-27045.
44. Schütte, H., Hummel, W., Tsai, H. and Kula, M.R. (1985). L-leucine dehydrogenase from Bacillus cereus - production, large-scale purification and protein characterization. Appl. Microbiol. Biotechnol. 22, 306-317.
45. Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. (1975). In The Enzymes (Boyer, PD ed.) VolXI, pp. 293-367 Academic Press, New York.
46. Smith, T.J., Schmidt, T., Fang, J., Wu, J., Siuzdak, G. and Stanley, C.A. (2002). The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J. Mol. Biol. 318, 765-777.
47. Stillman, T.J., Baker, P.J., Britton, K.L. and Rice, D.W. (1993). Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J. Mol. Biol. 234, 1131-1139.
48. Syed, S.E.-H. (1987). Beef liver glutamate dehydrogenase: studies of substrate specificity and relationship between the catalytic sites. Ph.D. Thesis. University of Sheffield, UK.
49. Takada, H., Yoshimura, T., Ohshima, T., Esaki, N. and Soda, K. (1991). Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: cloning, expression, and sequencing of its gene. J. Biochem. 109, 371-376.
50. Tang, L., Zhang, Y.H. and Hutchinson, C.R. (1994). Amino acid catabolism and antibiotic synthesis: valine is a source of precursors for macrolide biosynthesis in Streptomyces ambofaciens and Streptomyces fradiae. J. Bacteriol. 176, 6107-6119.
51. Turnbull, A.P., Baker, P.J. and Rice, D.W. (1997). Analysis of the quaternary structure, substrate specificity, and catalytic mechanism of valine dehydrogenase. J. Biol. Chem. 272, 25105-25111.
52. Vancura, A., Vancurova, I., Volc, J., Fussey, S.P., Flieger, M., Neuzil, J., Marsalek, J. and Behal, V. (1988). Valine dehydrogenase from Streptomyces fradiae: purification and properties. J. Gen. Microbiol. 134, 3213-3219.
53. Vanhooke, J.L., Thoden, J.B., Brunhuber, N.M., Blanchard, J.S. and Holden, H.M. (1999). Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism. Biochemistry. 38, 2326-2339.
54. Vetriani, C., Maeder, D.L., Tolliday, N., Yip, K.S., Stillman, T.J., Britton, K.L., Rice, D.W., Klump, H.H. and Robb, F.T. (1998). Protein thermostability above 100 degrees C: a key role for ionic interactions. Proc. Natl. Acad. Sci. U.S.A. 95, 12300-12305.
55. Wang, X.G., Britton, K.L., Baker, P.J., Martin, S., Rice, D.W. and Engel, P.C. (1995). Alteration of the amino acid substrate specificity of clostridial glutamate dehydrogenase by site-directed mutagenesis of an active-site lysine residue. Protein Eng. 8, 147-152.
56. Wendel, U., Gonzales, J. and Hummel, W. (1993). Neonatal screening for maple syrup urine disease by an enzyme-mediated colorimetric method. Clin. Chim. Acta. 219, 105-111.
57. Werner, C., Stubbs, M.T., Krauth-Siegel, R.L. and Klebe, G. (2005). The crystal structure of Plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs. J. Mol. Biol. 349, 597-607.
58. Yip, K.S., Britton, K.L., Stillman, T.J., Lebbink, J., de Vos, W.M., Robb, F.T., Vetriani, C., Maeder, D. and Rice, D.W. (1998). Insights into the molecular basis of thermal stability from the analysis of ion-pair networks in the glutamate dehydrogenase family. Eur. J. Biochem. 255, 336-346.
59. Yip, K.S., Stillman, T.J., Britton, K.L., Artymiuk, P.J., Baker, P.J., Sedelnikova, S.E., Engel, P.C., Pasquo, A., Chiaraluce, R. and Consalvi, V. (1995). The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure. 3, 1147-1158.