Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase

Biochemical and Biophysical Research Communications

Volumn 371, Issue 1, 2008, Pages 149-153

  Chang, Hung Kuang ^a   Zylstra, Gerben J ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

3 Aminophenol; Comamonas testosteroni; Directed evolution; m Hydroxybenzoate hydroxylase; Phenol; Substituted catechol; Substrate specificity

Indexed keywords

3 AMINOPHENOL; 3 CHLOROPHENOL; 4 CHLOROPHENOL; 4 CHLORORESORCINOL; 4 HYDROXYBENZOIC ACID; 4 NITROPHENOL; CATECHOL; GENTISIC ACID; HYDROQUINONE; HYDROXYBENZOIC ACID; OXYGENASE; PHENOL; PROTOCATECHUIC ACID; RESORCINOL; UNSPECIFIC MONOOXYGENASE;

ARTICLE; CONTROLLED STUDY; IN VITRO STUDY; MUTAGENESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINOPHENOLS; BACTERIAL PROTEINS; CLONING, MOLECULAR; COMAMONAS TESTOSTERONI; DIRECTED MOLECULAR EVOLUTION; MIXED FUNCTION OXYGENASES; MOLECULAR SEQUENCE DATA; MUTATION; OXIDATION-REDUCTION; PHENOL; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

COMAMONAS TESTOSTERONI;

EID: 42749084315     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.04.032     Document Type: Article

References (15)

1. Harayama S., Kok M., and Neidle E.L. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46 (1992) 565-601
2. Schreuder H.A., Prick P.A., Wierenga R.K., Vriend G., Wilson K.S., Hol W.G., and Drenth J. Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes. J. Mol. Biol. 208 (1989) 679-696
3. Enroth C. High-resolution structure of phenol hydroxylase and correction of sequence errors. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 1597-1602
4. Kalin M., Neujahr H.Y., Weissmahr R.N., Sejlitz T., Johl R., Fiechter A., and Reiser J. Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli. J. Bacteriol. 174 (1992) 7112-7120
5. Goyal A.K., and Zylstra G.J. Molecular cloning of novel genes for polycyclic aromatic hydrocarbon degradation from Comamonas testosteroni GZ39. Appl. Environ. Microbiol. 62 (1996) 230-236
6. Hiromoto T., Fujiwara S., Hosokawa K., and Yamaguchi H. Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site. J. Mol. Biol. 364 (2006) 878-896
7. Chang H.K., and Zylstra G.J. Novel organization of the genes for phthalate degradation from Burkholderia cepacia DBO1. J. Bacteriol. 180 (1998) 6529-6537
8. Parke D. Application of p-toluidine in chromogenic detection of catechol and protocatechuate, diphenolic intermediates in catabolism of aromatic compounds. Appl. Environ. Microbiol. 58 (1992) 2694-2697
9. Kok R.G., Young D.M., and Ornston L.N. Phenotypic expression of PCR-generated random mutations in a Pseudomonas putida gene after its introduction into an Acinetobacter chromosome by natural transformation. Appl. Environ. Microbiol. 65 (1999) 1675-1680
10. Bradford M.M. A rapid and sensitive methods for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
11. Michalover J.L., Ribbons D.W., and Hughes H. 3-Hydroxybenzoate 4-hydroxylase from Pseudomonas testosteroni. Biochem. Biophys. Res. Commun. 55 (1973) 888-896
12. Martz E. Protein Explorer: easy yet powerful macromolecular visualization. Trends Biochem. Sci. 27 (2002) 107-109. http://proteinexplorer.org
13. Xu D., Ballou D.P., and Massey V. Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met. Biochemistry 40 (2001) 12369-12378
14. Meyer A., Schmid A., Held M., Westphal A.H., Rothlisberger M., Kohler H.P., van Berkel W.J., and Witholt B. Changing the substrate reactivity of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica HBP1 by directed evolution. J. Biol. Chem. 277 (2002) 5575-5582
15. Boekelheide K., Graham D.G., Mize P.D., and Jeffs P.W. The metabolic pathway catalyzed by the tyrosinase of Agaricus bisporus. J. Biol. Chem. 255 (1980) 4766-4771