Phenoxazinone synthase: what's in a name?

Trends in Biotechnology

Volumn 27, Issue 4, 2009, Pages 248-258

  Le Roes Hill, Marilize ^a   Goodwin, Candice ^a   Burton, Stephanie ^a  

^a UNIVERSITY OF CAPE TOWN   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOPHENOLS; CLASSIFICATION ,; CONVERGENT EVOLUTIONS; COPPER PROTEINS; OXIDATIVE COUPLINGS; OXIDOREDUCTASE; POTENTIAL APPLICATIONS; STREPTOMYCES GRISEUS; SYNTHASE;

ANTIBIOTICS; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; OXYGEN;

ENZYMES;

ANTIBIOTIC AGENT; CHANDRANANIMYCIN; COPPER OXIDASE; DACTINOMYCIN; ELLOXAZINONE; EXFOLIAZONE; GLUCOSYLQUESTIOMYCIN; GRIXAZONE; MICHIGAZONE; OXIDOREDUCTASE; PHENOXAZINONE ANTIBIOTIC; PHENOXAZINONE SYNTHASE; TEXAZONE; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; BACTERIUM ISOLATE; DRUG MANUFACTURE; ENZYME MECHANISM; ENZYME STRUCTURE; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; REVIEW; STREPTOMYCES ANTIBIOTICUS;

ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; OXIDOREDUCTASES; STREPTOMYCES ANTIBIOTICUS; STREPTOMYCES GRISEUS;

STREPTOMYCES ANTIBIOTICUS; STREPTOMYCES GRISEUS SUBSP. GRISEUS;

EID: 62749159054     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2009.01.001     Document Type: Review

References (76)

1. Marsden R.L., et al. Exploiting protein structure data to explore the evolution of protein function and biological complexity. Philos. Trans. R. Soc. Lond. B Biol. Sci. 361 (2006) 425-440
2. Nakamura K., and Go N. Function and molecular evolution of multicopper blue proteins. Cell. Mol. Life Sci. 62 (2005) 2050-2066
3. Suzuki H., et al. A novel o-aminophenol oxidase responsible for formation of the phenoxazinone chromophore of grixazone. J. Biol. Chem. 281 (2006) 824-833
4. Jones G.H. Actinomycin production persists in a strain of Streptomyces antibioticus lacking phenoxazinone synthase. Antimicrob. Agents Chemother. 44 (2000) 1322-1327
5. Smith A.W., et al. Structure of phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center. Biochemistry 45 (2006) 4378-4387
6. Weissbach H., and Katz E. Studies on the biosynthesis of actinomycin: enzymic synthesis of the phenoxazone chromophore. J. Biol. Chem. 236 (1961) PC16-PC18
7. Golub E.E., and Nishimura J.S. Phenoxazinone synthetase from Streptomyces antibioticus: multiple activities of the enzyme. J. Bacteriol. 112 (1972) 1353-1357
8. Solomon E.I., et al. Multicopper oxidases and oxygenases. Chem. Rev. 96 (1996) 2563-2605
9. Barry III C.E., et al. Phenoxazinone synthase: mechanism for the formation of the phenoxazinone chromophore of actinomycin. Biochemistry 28 (1989) 6323-6333
10. Osiadacz J., et al. On the use of Trametes versicolor laccase for the conversion of 4-methyl-3-hydroxyanthranilic acid to actinocin chromophore. J. Biotechnol. 72 (1999) 141-149
11. Rescigno A., et al. Effect of 3-hydroxyanthranilic acid on mushroom tyrosinase activity. Biochim. Biophys. Acta 1384 (1998) 268-276
12. Puiu M., et al. Oxidase-peroxidase reaction: kinetics of peroxidase-catalysed oxidation of 2-aminophenol. Bioprocess Biosyst. Eng. 31 (2008) 579-586
13. Christen S., et al. Oxidation of 3-hydroxyanthranilic acid to the phenoxazinone cinnabarinic acid by peroxyl radicals and by compound I of peroxidases or catalase. Biochemistry 31 (1992) 8090-8097
14. Akazawa M., et al. Oscillatory oxido-reductive reaction of intracellular hemoglobin in human erythrocyte incubated with o-aminophenol. Tohoku J. Exp. Med. 192 (2000) 301-312
15. Mukherjee C., et al. Mimicking the function of amine oxidases and phenoxazinone synthase by a manganese(IV)-monoradical complex. C. R. Chim. 10 (2007) 313-325
16. Kaizer J., et al. Catechol oxidase and phenoxazinone synthase activity of a manganese(II) isoindoline complex. J. Inorg. Biochem. 102 (2008) 773-780
17. Nair P.M., and Vaidyanathan C.S. Isophenoxazine synthase. Biochim. Biophys. Acta 81 (1964) 507-516
18. Rao P.V.S., and Vaidyanathan C.S. Studies on the metabolism of o-aminophenol. Purification and properties of isophenoxazine synthase from Bauhenia monandra. Arch. Biochem. Biophys 118 (1967) 388-394
19. Nair P.M., and Vining I.C. Esophenoxazine synthase apoenzyme from Pycnoporus coccineus. Biochim. Biophys. Acta 96 (1965) 318-327
20. Rasgon J.L., and Scott T.W. Crimson: a novel sex-linked eye color mutant of Culex pipiens L. (Diptera: Culicidae). J. Med. Entomol 41 (2004) 385-391
21. Savage N., and Prinz W. Cinnabarinate synthase from baboon (Papio ursinus) liver. Identity with catalase. Biochem. J 161 (1977) 551-554
22. Rao P.V.S., and Vaidyanathan C.S. Enzymic conversion of 3-hydroxyanthranilic acid into cinnabarinic acid. Partial purification and properties of rat-liver cinnabarinate synthase. Biochem. J 99 (1966) 317-322
23. Morgan Jr. L.R., et al. Oxidation of 3-hydroxyanthranilic acid by a soluble liver fraction from poikilothermic vertebrates. Biochim. Biophys. Acta 100 (1965) 393-402
24. Morgan Jr. L.R., and Weimorts D.M. The conversion of 3-hydroxyanthranilic acid to 2-aminophenoxazin-3-one-1,8-dicarboxylic acid by extracts of acetone powders of poikilothermic animal livers. Biochim. Biophys. Acta 82 (1964) 645-646
25. Ogawa H., et al. Cinnabarinate formation in malpighian tubules of the silkworm. Bombyx mori: reaction mechanism of cinnabarinate formation in the presence of catalase and manganese ions. Hoppe Seylers Z. Physiol. Chem. 364 (1983) 1507-1518
26. Rosenzweig A.C., and Sazinsky M.H. Structural insights into dioxygen-activating copper enzymes. Curr. Opin. Struct. Biol. 16 (2006) 729-735
27. Bento I., et al. Reduction of dioxygen by enzymes containing copper. J. Biol. Inorg. Chem. 11 (2006) 539-547
28. Hoegger P.J., et al. Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences. FEBS J. 273 (2006) 2308-2326
29. Suzuki T., et al. A thermostable laccase from Streptomyces lavendulae REN-7: purification, characterization, nucleotide sequence, and expression. Biosci. Biotechnol. Biochem. 67 (2003) 2167-2175
30. Altschul S.F., et al. Protein database searches using compositionally adjusted substitution matrices. FEBS J. 272 (2005) 5101-5109
31. Smith A.W., et al. Crystallization and initial X-ray analysis of phenoxazinone synthase from Streptomyces antibioticus. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1453-1455
32. Hakulinen N., et al. A near atomic resolution of a Melanocarpus albomyces laccase. J. Struct. Biol. 162 (2008) 29-39
33. Choy H.A., and Jones G.H. Phenoxazinone synthase from Streptomyces antibioticus: purification of the large and small enzyme forms. Arch. Biochem. Biophys. 211 (1981) 55-65
34. Claus H., and Decker H. Bacterial tyrosinases. Syst. Appl. Microbiol. 29 (2006) 3-14
35. Solano F., et al. Dimethoxyphenol oxidase activity of different microbial blue multicopper proteins. FEMS Microbiol. Lett. 204 (2001) 175-181
36. Jones G.H. Regulation of phenoxazinone synthase expression in Streptomyces antibioticus. J. Bacteriol. 163 (1985) 1215-1221
37. Kelly K.S., et al. Pleiotropic effects of a relC mutation in Streptomyces antibioticus. J. Bacteriol. 173 (1991) 2297-2300
38. Hoyt S., and Jones G.H. relA is required for actinomycin production in Streptomyces antibioticus. J. Bacteriol. 181 (1999) 3824-3829
39. Ohnishi Y., et al. Structures of grixazone A and B, A-factor-dependent yellow pigments produced under phosphate depletion by Streptomyces griseus. J. Antibiot. (Tokyo) 57 (2004) 218-223
40. Higashi T., et al. A-factor and phosphate depletion signals are transmitted to the grixazone biosynthesis genes via the pathway-specific transcriptional activator GriR. J. Bacteriol. 189 (2007) 3515-3524
41. Horinouchi S. Mining and polishing of the treasure trove in the bacterial genus Streptomyces. Biosci. Biotechnol. Biochem. 71 (2007) 283-299
42. 4 primary metabolites by two enzymes. J. Biol. Chem. 281 (2006) 36944-36951
43. Suzuki H., et al. GriC and GriD constitute a carboxylic acid reductase involved in the grixazone biosynthesis in Streptomyces griseus. J. Antibiot. (Tokyo) 60 (2007) 380-387
44. Gerber N.N., and Lechevalier M.P. Phenazines and phenoxazinones from Waksmania aerata sp. nov. and Pseudomonas iodina. Biochemistry 3 (1964) 598-602
45. Gerber N.N. Phenazines and phenoxazinones from some novel Nocardiaceae. Biochemistry 5 (1966) 3824-3829
46. Gerber N.N. Phenazines, phenoxazinones, and dioxopiperazines from Streptomyces thioluteus. J. Org. Chem. 32 (1967) 4055-4057
47. Igarashi Y., et al. Glucosylquestiomycin, a novel antibiotic from Microbispora sp. TP-A0184: fermentation, isolation, structure determination, synthesis and biological activities. J. Antibiot. (Tokyo) 51 (1998) 915-920
48. Maskey R.P., et al. Chandrananimycins A-C: production of novel anticancer antibiotics from a marine Actinomadura sp. isolate M048 by variation of medium composition and growth conditions. J. Antibiot. (Tokyo) 56 (2003) 622-629
49. Liu W.-H., et al. Cytotoxic metabolites of Streptimonospora salina [sic]. Chem. Nat. Compd. 44 (2008) 503-505
50. Graf E., et al. Elloxazinones A and B, new aminophenoxazinones from Streptomyces griseus Acta 2871. J. Antibiot. (Tokyo) 60 (2007) 277-284
51. Zeeck, A. et al. (1989) Hoechst Aktiengesellschaft. Pharmacological use of phenoxazinones, US patent 4,861,775
52. Aulinger K., et al. Metabolites of 2-aminophenol from fruit bodies of Lepiota americana (Agaricales). Z. Naturforsch. [C] 55 (2000) 481-484
53. Zikmundová M., et al. Hydroxylated 2-amino-3H-phenoxazin-3-one derivatives as products of 2-hydroxy-1,4-benzoxazin-3-one (HBOA) biotransformation by Chaetosphaeria sp., an endophytic fungus from Aphelandra tetragona. Z. Naturforsch. [C] 57 (2002) 660-665
54. Bitzer J., et al. New aminophenoxazinones from a marine Halomonas sp.: fermentation, structure elucidation, and biological activity. J. Antibiot. (Tokyo) 59 (2006) 86-92
55. Hayashi K., et al. Phenoxazine derivatives inactivate human cytomegalovirus, herpes simplex virus-1, and herpes simplex virus-2 in vitro. J. Pharmacol. Sci. 106 (2008) 369-375
56. Gao S., et al. A novel phenoxazine derivative suppresses IgM expression in DT40 B cell line. Br. J. Pharmacol. 137 (2002) 749-755
57. Hendrich A.B., et al. A study on the perturbation of model lipid membranes by phenoxazines. Bioorg. Med. Chem. 14 (2006) 5948-5954
58. Shimizu S., et al. Phenoxazine compounds produced by the reactions with bovine hemoglobin show antimicrobial activity against non-tuberculosis mycobacteria. Tohoku J. Exp. Med. 203 (2004) 47-52
59. Challis G.L., and Hopwood D.A. Chemical biotechnology: bioactive small molecules - targets and discovery technologies. Curr. Opin. Biotechnol. 18 (2007) 475-477
60. Baltz R.H. Renaissance in antibacterial discovery from actinomycetes. Curr. Opin. Pharmacol. 8 (2008) 557-563
61. Hopwood D.A. Antibiotics: opportunities for genetic manipulation. Philos. Trans. R. Soc. Lond. B Biol. Sci. 324 (1989) 549-562
62. Bull A.T., et al. Biocatalysts for clean industrial products and processes. Curr. Opin. Microbiol. 2 (1999) 246-251
63. Burton S.G., et al. The search for an ideal biocatalyst. Nat. Biotechnol. 20 (2002) 37-45
64. Nakashima N., et al. Actinomycetes as host cells for production of recombinant proteins. Microb. Cell Fact. 4 (2005) 7-11
65. Bolognese A., et al. Antitumor agents. 1. Synthesis, biological evaluation, and molecular modelling of 5H-pyrido[3,2-a]phenoxazin-5-one, a compound with potent antiproliferative activity. J. Med. Chem. 45 (2002) 5205-5216
66. Rich J.O., et al. Combinatorial biocatalysis. Curr. Opin. Chem. Biol. 6 (2002) 161-167
67. Tomich P.K. Streptomyces cloning: possible construction of novel compounds and regulation of antibiotic biosynthetic genes. Antimicrob. Agents Chemother. 32 (1988) 1472-1476
68. McLeod M.P., et al. The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse. Proc. Natl. Acad. Sci. U. S. A 103 (2006) 15582-15587
69. Mikolasch A., et al. Novel penicillins synthesised by biotransformation using laccase from Trametes spec. Chem. Pharm. Bull. (Tokyo) 54 (2006) 632-638
70. Eggert C., et al. Laccase-mediated formation of the phenoxazinone derivative, cinnabarinic acid. FEBS Lett. 376 (1995) 202-206
71. Burton S.G., and Le Roes-Hill M. Oxidizing enzymes in multi-step biotransformation processes. In: Garcia-Junceda E. (Ed). Multi-step Enzyme Catalysis: Biotransformations and Chemoenzymatic Synthesis (2008), Wiley-VCH 41-60
72. Katz E., and Weissbach H. Biosynthesis of the actinomycin chromophore; enzymatic conversion of 4-methyl-3-hydroxyanthranilic acid to actinocin. J. Biol. Chem. 237 (1962) 882-886
73. Porcal G.V., et al. Photophysics of the phenoxazine dyes resazurin and resorufin in direct and reverse micelles. Dyes Pigments 80 (2009) 206-211
74. Zaytsev A.V., et al. Synthesis and testing of chromogenic phenoxazinone substrates for β-alanyl aminopeptidase. Org. Biomol. Chem. 6 (2008) 682-692
75. Grigg G.W., et al. Amplifications of phleomycin and bleomycin-induced antibiotic activity in Escherichia coli by aromatic cationic compounds. J. Antibiot. (Tokyo) 30 (1977) 870-878
76. Hughes M.A., et al. Accumulation of 2-aminophenoxazin-3-one-7-carboxylate during growth of Pseudomonase putida TW3 on 4-nitro-substituted substrates requires 4-hydroxylaminobenzoate lyase (PnbB). Appl. Environ. Microbiol. 68 (2002) 4965-4970