The growing VAO flavoprotein family

Archives of Biochemistry and Biophysics

Volumn 474, Issue 2, 2008, Pages 292-301

  Leferink, Nicole G H ^a   Heuts, Dominic P H M ^b   Fraaije, Marco W ^b   van Berkel, Willem J H ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

Alditol oxidase; Chitooligosaccharide oxidase; Covalent flavinylation; Eugenol oxidase; Flavoenzyme; l Galactono 1,4 lactone dehydrogenase; Vanillyl alcohol oxidase; VAO family; Vitamin C

Indexed keywords

ADENINE; ALDEHYDE; CHOLESTEROL OXIDASE; CYTOKININ; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; GULONOLACTONE OXIDASE; HEXOSE; LACTATE DEHYDROGENASE; LACTONE DERIVATIVE; MONOPHENOL MONOOXYGENASE; NICOTINE DERIVATIVE; OXIDOREDUCTASE; POLYPEPTIDE; QUERCETIN; RETICULINE; SYNTHETASE; URIDINE DIPHOSPHATE; VANILLIN DERIVATIVE; VANILLYL ALCOHOL OXIDASE; XYLITOL;

AMINO ACID SEQUENCE; ARTHROBACTER; BIOSYNTHESIS; CATALYSIS; COVALENT BOND; DETOXIFICATION; ENZYME ACTIVITY; MICROBIAL ACTIVITY; NUCLEOTIDE SEQUENCE; PENICILLIUM SIMPLICISSIMUM; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN ENGINEERING; PROTEIN FAMILY; PROTEIN STRUCTURE; REVIEW; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING;

ALCOHOL OXIDOREDUCTASES; BINDING SITES; CATALYSIS; CYTOCHROMES C; FLAVIN-ADENINE DINUCLEOTIDE; FLAVINS; FLAVOPROTEINS; MODELS, MOLECULAR; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PHYLOGENY; PROTEIN BINDING; SUBSTRATE SPECIFICITY;

EID: 44549085227     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.01.027     Document Type: Review

References (72)

1. Fraaije M.W., van Berkel W.J.H., Benen J.A.E., Visser J., and Mattevi A. Trends Biochem. Sci. 23 (1998) 206-207
2. Brandsch R., Bichler V., and Nagursky H. Eur. J. Biochem. 165 (1987) 559-564
3. Möhler H., Brühmüller M., and Decker K. Eur. J. Biochem. 29 (1972) 152-155
4. McIntire W., Edmondson D.E., Hopper D.J., and Singer T.P. Biochemistry 20 (1981) 3068-3075
5. Huang C.H., Lai W.L., Lee M.H., Chen C.J., Vasella A., Tsai Y.C., and Liaw S.H. J. Biol. Chem. 280 (2005) 38831-38838
6. Hefti M.H., Vervoort J., and van Berkel W.J.H. Eur. J. Biochem. 270 (2003) 4227-4242
7. Mewies M., McIntire W.S., and Scrutton N.S. Protein Sci. 7 (1998) 7-20
8. Decker K., and Brandsch R. Methods Enzymol. 280 (1997) 413-423
9. Edmondson D.E., and De Francesco R. In: Müller F. (Ed). Chemistry and Biochemistry of Flavoenzymes (1991), CRC Press Inc., Boca Raton, Florida 73-103
10. Halada P., Leitner C., Sedmera P., Haltrich D., and Volc J. Anal. Biochem. 314 (2003) 235-242
11. Hassan-Abdallah A., Zhao G., and Jorns M.S. Biochemistry 45 (2006) 9454-9462
12. Mauch L., Bichler V., and Brandsch R. FEBS Lett. 257 (1989) 86-88
13. Fraaije M.W., van den Heuvel R.H.H., van Berkel W.J.H., and Mattevi A. J. Biol. Chem. 274 (1999) 35514-35520
14. van den Heuvel R.H.H., Fraaije M.W., Mattevi A., and van Berkel W.J.H. J. Biol. Chem. 275 (2000) 14799-14808
15. Brandsch R., and Bichler V. J. Biol. Chem. 266 (1991) 19056-19062
16. Nagursky H., Bichler V., and Brandsch R. Eur. J. Biochem. 177 (1988) 319-325
17. Fraaije M.W., van den Heuvel R.H.H., van Berkel W.J.H., and Mattevi A. J. Biol. Chem. 275 (2000) 38654-38658
18. Kim J., Fuller J.H., Kuusk V., Cunane L., Chen Z.W., Mathews F.S., and McIntire W.S. J. Biol. Chem. 270 (1995) 31202-31209
19. Cunane L.M., Chen Z.W., McIntire W.S., and Mathews F.S. Biochemistry 44 (2005) 2963-2973
20. Mattevi A., Fraaije M.W., Mozzarelli A., Olivi L., Coda A., and van Berkel W.J.H. Structure 5 (1997) 907-920
21. Koetter J.W., and Schulz G.E. J. Mol. Biol. 352 (2005) 418-428
22. Coulombe R., Yue K.Q., Ghisla S., and Vrielink A. J. Biol. Chem. 276 (2001) 30435-30441
23. Malito E., Coda A., Bilyeu K.D., Fraaije M.W., and Mattevi A. J. Mol. Biol. 341 (2004) 1237-1249
24. Bae E., Bingman C.A., Bitto E., Aceti D.J., and Phillips Jr. G.N. Proteins 70 (2007) 303-306
25. Heuts D.P.H.M., van Hellemond E.W., Janssen D.B., and Fraaije M.W. J. Biol. Chem. 282 (2007) 20283-20291
26. Mathews F.S., Chen Z.W., Bellamy H.D., and McIntire W.S. Biochemistry 30 (1991) 238-247
27. Jin J., Mazon H., van den Heuvel R.H.H., Janssen D.B., and Fraaije M.W. FEBS J. 274 (2007) 2311-2321
28. Frébortová J., Fraaije M.W., Galuszka P., Šebela M., Peč P., Hrbáč J., Novák O., Bilyeu K.D., English J.T., and Frébort I. Biochem. J. 380 (2004) 121-130
29. Mattevi A. Trends Biochem. Sci. 31 (2006) 276-283
30. Hiraga K., Eto T., Yoshioka I., and Oda K. Biosci. Biotechnol. Biochem. 62 (1998) 347-353
31. Yamashita M., Omura H., Okamoto E., Furuya Y., Yabuuchi M., Fukahi K., and Murooka Y. J. Biosci. Bioeng. 89 (2000) 350-360
32. Forneris F., Heuts D.P.H.M., Delvecchio M., Rovida S., Fraaije M.W., and Mattevi A. Biochemistry 47 (2008) 978-985
33. McIntire W., Hopper D.J., and Singer T.P. Biochem. J. 228 (1985) 325-335
34. Furukawa H., Wieser M., Morita H., Sugio T., and Nagasawa T. Arch. Microbiol. 171 (1998) 37-43
35. Priefert H., Overhage J., and Steinbüchel A. Arch. Microbiol. 172 (1999) 354-363
36. Brandt K., Thewes S., Overhage J., Priefert H., and Steinbüchel A. Appl. Microbiol. Biotechnol. 56 (2001) 724-730
37. Rand T., Qvist K.B., Walter C.P., and Poulsen C.H. FEBS J. 273 (2006) 2693-2703
38. Winkler A., Hartner F., Kutchan T.M., Glieder A., and Macheroux P. J. Biol. Chem. 281 (2006) 21276-21285
39. Sirikantaramas S., Morimoto S., Shoyama Y., Ishikawa Y., Wada Y., and Taura F. J. Biol. Chem. 279 (2004) 39767-39774
40. Carter C.J., and Thornburg R.W. Plant Physiol. 134 (2004) 460-469
41. Custers J.H.H.V., Harrison S.J., Sela-Buurlage M.B., van Deventer E., Lageweg W., Howe P.W., van der Meijs P.J., Ponstein A.S., Simons B.H., Melchers L.S., and Stuiver M.H. Plant J. 39 (2004) 147-160
42. Xu F., Golightly E.J., Fuglsang C.C., Schneider P., Duke K.R., Lam L., Christensen S., Brown K.M., Jorgensen C.T., and Brown S.H. Eur. J. Biochem. 268 (2001) 1136-1142
43. Li Y.S., Ho J.Y., Huang C.C., Lyu S.Y., Lee C.Y., Huang Y.T., Wu C.J., Chan H.C., Huang C.J., Hsu N.S., Tsai M.D., and Li T.L. J. Am. Chem. Soc. 129 (2007) 13384-13385
44. Alexeev I., Sultana A., Mäntsälä P., Niemi J., and Schneider G. Proc. Natl. Acad. Sci. USA 104 (2007) 6170-6175
45. Heuts D.P.H.M., Janssen D.B., and Fraaije M.W. FEBS Lett. 581 (2007) 4905-4909
46. Kutchan T.M., and Dittrich H. J. Biol. Chem. 270 (1995) 24475-24481
47. Winkler A., Kutchan T.M., and Macheroux P. J. Biol. Chem. 282 (2007) 24437-24443
48. Razeto A., Mattiroli F., Carpanelli E., Aliverti A., Pandini V., Coda A., and Mattevi A. Structure 15 (2007) 683-692
49. Dym O., Pratt E.A., Ho C., and Eisenberg D. Proc. Natl. Acad. Sci. USA 97 (2000) 9413-9418
50. Benson T.E., Filman D.J., Walsh C.T., and Hogle J.M. Nat. Struct. Biol. 2 (1995) 644-653
51. Mapson L.W., and Breslow E. Biochem. J. 68 (1958) 395-406
52. Mutsuda M., Ishikkawa T., Takeda T., and Shigeoka S. Biosci. Biotechnol. Biochem. 59 (1995) 1983-1984
53. Ôba K., Ishikawa S., Nishikawa M., Mizuno H., and Yamamoto T. J. Biochem. (Tokyo) 117 (1995) 120-124
54. Imai T., Karita S., Shiratori G., Hattori M., Nunome T., Ôba K., and Hirai M. Plant Cell. Physiol. 39 (1998) 1350-1358
55. Siendones E., González-Reyes J.A., Santos-Ocaña C., Navas P., and Córdoba F. Plant Physiol. 120 (1999) 907-912
56. Østergaard J., Persiau G., Davey M.W., Bauw G., and van Montagu M. J. Biol. Chem. 272 (1997) 30009-30016
57. Yabuta Y., Yoshimura K., Takeda T., and Shigeoka S. Plant Cell. Physiol. 41 (2000) 666-675
58. Leferink N.G.H., Van den Berg W.A.M., and van Berkel W.J.H. FEBS J. 275 (2008) 713-726
59. Huh W.K., Lee B.H., Kim S.T., Kim Y.R., Rhie G.E., Baek Y.W., Hwang C.S., Lee J.S., and Kang S.O. Mol. Microbiol. 30 (1998) 895-903
60. Nishikimi M., Tolbert B.M., and Udenfriend S. Arch. Biochem. Biophys. 175 (1976) 427-435
61. Salusjärvi T., Kalkkinen N., and Miasnikov A.N. Appl. Environ. Microbiol. 70 (2004) 5503-5510
62. Wolucka B.A., and Communi D. FEBS J. 273 (2006) 4435-4445
63. Wilkinson S.R., Prathalingam S.R., Taylor M.C., Horn D., and Kelly J.M. Proc. Natl. Acad. Sci. USA 102 (2005) 11645-11650
64. Logan F.J., Taylor M.C., Wilkinson S.R., Kaur H., and Kelly J.M. Biochem. J. 407 (2007) 419-426
65. Huh W.K., Kim S.T., Yang K.S., Seok Y.J., Hah Y.C., and Kang S.O. Eur. J. Biochem. 225 (1994) 1073-1079
66. Nakagawa H., and Asano A. J. Biochem. (Tokyo) 68 (1970) 737-746
67. Heazlewood J.L., Howell K.A., and Millar A.H. Biochim. Biophys. Acta 1604 (2003) 159-169
68. Millar A.H., Mittova V., Kiddle G., Heazlewood J.L., Bartoli C.G., Theodoulou F.L., and Foyer C.H. Plant Physiol. 133 (2003) 443-447
69. de Jong E., van Berkel W.J.H., van der Zwan R.P., and de Bont J.A.M. Eur. J. Biochem. 208 (1992) 651-657
70. Kenney W.C., Edmondson D.E., Singer T.P., Nishikimi M., Noguchi E., and Yagi K. FEBS Lett. 97 (1979) 40-42
71. Kenney W.C., Edmondson D.E., and Singer T.P. Biochem. Biophys. Res. Commun. 71 (1976) 1194-1200
72. Harada Y., Shimizu M., Murakawa S., and Takahashi T. Agr. Biol. Chem. 43 (1979) 2635-2636