Molecular evolution of hydantoinases

Biological Chemistry

Volumn 379, Issue 6, 1998, Pages 743-747

  May, Oliver ^a   Habenicht, Andreas ^a   Mattes, Ralf ^a   Syldatk, Christoph ^a   Siemann, Martin ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

Author keywords

Amidase; Amino acid production; Bioconversion; Enantioselectivity; Hydantoin amidohydrolase; Superfamily

Indexed keywords

BACTERIAL ENZYME; DIHYDROPYRIMIDINASE;

AMINO ACID SEQUENCE; ARTHROBACTER; ARTICLE; DATA BASE; ENZYME STRUCTURE; EVOLUTION; MULTIGENE FAMILY; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; PRIORITY JOURNAL; PROTEIN FAMILY; SEQUENCE HOMOLOGY;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; ANIMALS; ARTHROBACTER; MOLECULAR SEQUENCE DATA;

ARCHAEA; ARTHROBACTER; ARTHROBACTER AURESCENS; BACTERIA (MICROORGANISMS); EUKARYOTA; PROKARYOTA;

EID: 0031817075     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (17)

1. Hamajima, N., Matsuda, K., Sakata, S., Tamaki, N., Sasaki, M., and Nonaka, M. (1996). A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution. Gene 180, 157-163.
2. Hassall, H., and Greenberg, D.M. (1963). The bacterial metabolism of L-hydantoin-5-propionic acid to carbamoylglutamic acid and glutamic acid. J. Biol. Chem. 238, 3325-3329.
3. Holm, L., and Sander, C. (1997). An evolutionary treasure: Unifaction of a broad set of amidohydrolases related to ureases. Proteins 28, 72-82.
4. Ishikawa, T., Watabe, K., Mukohara, Y., and Nakamura, H. (1997). Mechanism of stereospecific conversion of DL-5-subsituted hydantoins to the corresponding L-amino acids by Pseudomonas sp. strain NS671. Biosci. Biotech. Biochem. 61, 185-187.
5. May, O., Siemann, M., Pietzsch, M., Kiess, M., Mattes, R., and Syldatk, C. (1998a). A novel hydantoinase from Arthrobacter aurescens DSM 3745 and its relation to other amidases. J. Biotechnol., in press.
6. May, O., Siemann, M., and Syldatk, C. (1998b). Structural and catalytic function of zinc for the hydantoinase from Arthrobacter aurescens DSM 3745. J. Mol. Catal. B-Enzym., in press.
7. Ogawa, J., Kim, J.M., Nirdnoy, W., Amano, Y., Yamada, H., and Shimizu, S. (1995). Purification and characterization of an ATP-dependent amidohydrolase, N-methylhydantoin amidohydrolase, fromPseudomonasputida 77. Eur. J. Biochem. 229, 284-290.
8. Park, I.S., and Hausinger, R.P. (1993). Site-directed mutagenesis of Klebsiella aemgenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding and catalysis. Protein Sci. 2, 1034-1041.
9. Runser, S.M., and Meyer, P.C. (1993). Purification and biochemical characterization of the hydantoin hydrolyzing enzyme from Agrobacterium sp: A hydantoinase with no 5, 6-dihydropyrimidine amidohydrolase activity. Eur. J. Biochem. 273, 1315-1324.
10. Saitou, N., and Nei, M. (1987). The neighbour-joining method, A new method for constructing phylogenetic trees. Mol. Biol. Evol. 4, 406-625.
11. Strimmer, K. (1997). Maximum Likelihood Methods in Molecular Phylogeneics (München, Germany: Herbert Utz Verlag).
12. Syldatk, C., and Pietzsch, M. (1995). Hydrolysis and formation of hydantoins (Chpt. B 2.4). In: Enzyme Catalysis in Organic Synthesis, K. Drauz, and H. Waldmann, eds. (Weinheim, Germany. VCH-Verlag), pp. 409-431.
13. Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). CLUSTAL W. Improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position specific gap penalties and weight matrix choice. Nucleic Acids Research 22, 4673-4680.
14. Wallach, D.P., and Grisolia, S. (1957). The purification and properties of hydropyrimidine hydrase, J. Biol. Chem. 226, 277-288.
15. Webb, E.C. (1992). Enzyme nomenclature 1992: Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes (San Diego, USA; Academic Press).
16. Yamashiro, A., Kubota, K., and Yokozeki, K. (1988). Mechanism of stereospecific production of L-amino acids from the corresponding 5-substituted hydantoins by Bacillus brevis. Agric. Biol. Chem. 52, 2857-2863.
17. Zimmermann, B.H., Kemling, N.M., and Evans, D.R. (1995). Function of conserved histidine residues in mammalian dihydroorotase, Biochemistry 34, 7038-7046.