Enhancement of l-tryptophan 5-hydroxylation activity by structure-based modification of l-phenylalanine 4-hydroxylase from Chromobacterium violaceum

Journal of Bioscience and Bioengineering

Volumn 108, Issue 3, 2009, Pages 184-189

  Kino, Kuniki ^a   Hara, Ryotaro ^a   Nozawa, Ai ^a  

^a WASEDA UNIVERSITY   (Japan)

Author keywords

5 Hydroxy l tryptophan; Aromatic amino acid hydroxylase; Chromobacterium violaceum; l Phenylalanine 4 hydroxylase; Saturation mutagenesis

Indexed keywords

5-HYDROXY-L-TRYPTOPHAN; AROMATIC AMINO ACID HYDROXYLASE; CHROMOBACTERIUM VIOLACEUM; L-PHENYLALANINE 4-HYDROXYLASE; SATURATION MUTAGENESIS;

AMINATION; AMINES; AROMATIC COMPOUNDS; HYDROXYLATION; MUTAGENESIS; ORGANIC ACIDS;

AMINO ACIDS;

PHENYLALANINE 4 MONOOXYGENASE; TRYPTOPHAN HYDROXYLASE;

AMINO ACID SEQUENCE; ARTICLE; CHROMOBACTERIUM VIOLACEUM; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SYNTHESIS; LIGHT ABSORPTION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS;

AMINO ACID SEQUENCE; ANIMALS; CATALASE; CATTLE; CHROMOBACTERIUM; HYDROXYLATION; KINETICS; MOLECULAR SEQUENCE DATA; MUTATION; PHENYLALANINE; PHENYLALANINE HYDROXYLASE; PROTEIN CONFORMATION; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; TRYPTOPHAN; TYROSINE;

CHROMOBACTERIUM VIOLACEUM;

EID: 67949088278     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2009.04.002     Document Type: Article

References (18)

1. Nakazawa H., Enei H., Okumura S., Yoshida H., and Yamada H. Enzymatic preparation of l-tryptophan and 5-hydroxy-l-tryptophan. FEBS Lett. 25 (1972) 43-45
2. Nakata H., Yamauchi T., and Fujisawa H. Phenylalanine hydroxylase from Chromobacterium violaceum, purification and characterization. J. Biol. Chem. 254 (1979) 1829-1833
3. Erlandsen H., Bjorgo E., Flatmark T., and Stevens R.C. Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase. Biochemistry 39 (2000) 2208-2217
4. Bjørgo E., Knappskog P.M., Martinez A., Stevens R.C., and Flatmark T. Partial characterization and three-dimensional-structural localization of eight mutations in exon 7 of the human phenylalanine hydroxylase gene associated with phenylketonuria. Eur. J. Biochem. 257 (1998) 1-10
5. Erlandsen H., Kim J.Y., Patch M.G., Han A., Volner A., Abu-Omar M.M., and Stevens R.C. Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates. J. Mol. Biol. 320 (2002) 645-661
6. Wang L., Erlandsen H., Haavik J., Knappskog P.M., and Stevens R.C. Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. Biochemistry 41 (2002) 12569-12574
7. McKinney J., Teigen K., Froystein N.A., Salaun C., Knappskog P.M., Haavik J., and Martinez A. Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase, important role of Phe313 in substrate specificity. Biochemistry 40 (2001) 15591-15601
8. Daubner S.C., Moran G.R., and Fitzpatrick P.F. Role of tryptophan hydroxylase Phe313 in determining substrate specificity. Biochem. Biophys. Res. Commun. 292 (2002) 639-641
9. Sambrook J., and Russel D.W. Molecular Cloning: A Laboratory Manual. 3rd ed. (2001), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
10. Quintana M.G., Didion C., and Dalton H. Colorimetric method for a rapid detection of oxygenated aromatic biotransformation products. Biotechnol. Techniques 11 (1997) 585-587
11. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
12. Koehntop K.D., Emerson J.P., and Que Jr. L. The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J. Biol. Inorg. Chem. 10 (2005) 87-93
13. Erlandsen H., Patch M.G., Gamez A., Straub M., and Stevens R.C. Structural studies on phenylalanine hydroxylase and implications toward understanding and treating phenylketonuria. Pediatrics 112 (2003) 1557-1565
14. Han S., Eltis L.D., Timmis K.N., Muchmore S.W., and Bolin J.T. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270 (1995) 976-980
15. Kauppi B., Lee K., Carredano E., Parales R.E., Gibson D.T., Eklund H., and Ramaswamy S. Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase. Structure 6 (1998) 571-586
16. Valegard K., van Scheltinga A.C., Lloyd M.D., Hara T., Ramaswamy S., Perrakis A., Thompson A., Lee H.J., Baldwin J.E., Schofield C.J., Hajdu J., and Andersson I. Structure of a cephalosporin synthase. Nature 394 (1998) 805-809
17. Erlandsen H., Fusetti F., Martinez A., Hough E., Flatmark T., and Stevens R.C. Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat. Struct. Biol. 4 (1997) 995-1000
18. Jiang G.C., Yohrling IV G.J., Schmitt J.D., and Vrana K.E. Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling. J. Mol. Biol. 302 (2000) 1005-1017