Discovery of a Eukaryotic Pyrroloquinoline Quinone-Dependent oxidoreductase belonging to a new auxiliary activity family in the database of carbohydrate-active enzymes

PLoS ONE

Volumn 9, Issue 8, 2014, Pages

  Matsumura, Hirotoshi ^a,d   Umezawa, Kiwamu ^b   Takeda, Kouta ^b   Sugimoto, Naohisa ^a   Ishida, Takuya ^a,c   Samejima, Masahiro ^a   Ohno, Hiroyuki ^b   Yoshida, Makoto ^b   Igarashi, Kiyohiko ^a,c   Nakamura, Nobuhumi ^b,c  

^a UNIVERSITY OF TOKYO   (Japan)

^b TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

OXIDOREDUCTASE; PRIMER DNA; PYRROLOQUINOLINEQUINONE;

AMINO ACID SEQUENCE; BASIDIOMYCETES; CALORIMETRY; CHEMISTRY; ENZYMOLOGY; GENETICS; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYLOGENY; PICHIA; PROTEIN DATABASE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BASE SEQUENCE; BASIDIOMYCOTA; CALORIMETRY; DATABASES, PROTEIN; DNA PRIMERS; MOLECULAR SEQUENCE DATA; OXIDOREDUCTASES; PHYLOGENY; PICHIA; PQQ COFACTOR; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84905994561     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0104851     Document Type: Article

References (36)

1. Hauge JG (1964) Glucose Dehydrogenase of Bacterium Anitratum: An enzyme with a novel prosthetic group. J Biol Chem 239: 3630-3639.
2. Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979) A novel coenzyme from bacterial primary alcohol dehydrogenases. Nature 280: 843-844. (Pubitemid 9254046)
3. Anthony C, Ghosh M (1998) The structure and function of the PQQ-containing quinoprotein dehydrogenases. Prog Biophys Mol Biol 69: 1-21. (Pubitemid 28257706)
4. Anthony C (2001) Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes. Antioxid Redox Signal 3: 757-774.
5. Matsushita K, Toyama H, Yamada M, Adachi O (2002) Quinoproteins: structure, function, and biotechnological applications. Appl Microbiol Biotechnol 58: 13-22. (Pubitemid 34143298)
6. Choi O, Kim J, Kim JG, Jeong Y, Moon JS, et al. (2008) Pyrroloquinoline quinone is a plant growth promotion factor produced by Pseudomonas fluorescens B16. Plant Physiol 146: 657-668. (Pubitemid 351230794)
7. Killgore J, Smidt C, Duich L, Romero-Chapman N, Tinker D, et al. (1989) Nutritional importance of pyrroloquinoline quinone. Science 245: 850-852. (Pubitemid 19223660)
8. Stites TE, Mitchell AE, Rucker RB (2000) Physiological importance of quinoenzymes and the O-quinone family of cofactors. J Nutr 130: 719-727. (Pubitemid 30173652)
9. Misra HS, Rajpurohit YS, Khairnar NP (2012) Pyrroloquinoline-quinone and its versatile roles in biological processes. J Biosci 37: 313-325.
10. Harris CB, Chowanadisai W, Mishchuk DO, Satre MA, Slupsky CM, et al. (2013) Dietary pyrroloquinoline quinone (PQQ) alters indicators of inflammation and mitochondrial-related metabolism in human subjects. J Nutr Biochem 24: 2076-2084.
11. Levasseur A, Drula E, Lombard V, Coutinho PM, Henrissat B (2013) Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes. Biotechnol Biofuels 6: 41.
12. Ayers AR, Ayers SB, Eriksson KE (1978) Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum. Eur J Biochem 90: 171-181. (Pubitemid 9013140)
13. Hallberg BM, Bergfors T, Backbro K, Pettersson G, Henriksson G, et al. (2000) A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase. Structure 8: 79-88. (Pubitemid 30051344)
14. Yanagi SO, Kawasumi T, Takebe I, Takemaru T (1988) Genetic analyses of Coprinus cinereus strains derived through intraspecific protoplast fusion. Agricultural and Biological Chemistry 52: 281-284.
15. 2. Eur J Biochem 205: 133-138.
16. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215: 403-410.
17. Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402. (Pubitemid 27359211)
18. Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
19. Kelley LA, Sternberg MJ (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4: 363-371.
20. Gouet P, Courcelle E, Stuart DI, Metoz F (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308. (Pubitemid 29213756)
21. 562 from the white-rot fungus Phanerochaete chrysosporium. Appl Environ Microbiol 71: 4548-4555.
22. Yoshida M, Ohira T, Igarashi K, Nagasawa H, Aida K, et al. (2001) Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris. Biosci Biotechnol Biochem 65: 2050-2057. (Pubitemid 33667824)
23. Samejima M, Eriksson KE (1992) A comparison of the catalytic properties of cellobiose:quinone oxidoreductase and cellobiose oxidase from Phanerochaete chrysosporium. Eur J Biochem 207: 103-107.
24. Igarashi K, Verhagen MF, Samejima M, Schulein M, Eriksson KE, et al. (1999) Cellobiose dehydrogenase from the fungi Phanerochaete chrysosporium and Humicola insolens. A flavohemoprotein from Humicola insolens contains 6-hydroxy-FAD as the dominant active cofactor. J Biol Chem 274: 3338-3344. (Pubitemid 29077170)
25. Jongejan JA (1989) Chemistry of PQQ. Delft, The Netherlands: Delft University of Technology.
26. Katoh K, Misawa K, Kuma K, Miyata T (2002) MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res 30: 3059-3066. (Pubitemid 34851225)
27. Katoh K, Standley DM (2013) MAFFT multiple sequence alignment software version 7: improvements in performance and usability. Mol Biol Evol 30: 772-780.
28. Igarashi S, Hirokawa T, Sode K (2004) Engineering PQQ glucose dehydrogenase with improved substrate specificity. Site-directed mutagenesis studies on the active center of PQQ glucose dehydrogenase. Biomol Eng 21: 81-89. (Pubitemid 38534485)
29. Toyama H, Mathews FS, Adachi O, Matsushita K (2004) Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology. Arch Biochem Biophys 428: 10-21. (Pubitemid 38844905)
30. Oubrie A, Rozeboom HJ, Kalk KH, Olsthoorn AJ, Duine JA, et al. (1999) Structure and mechanism of soluble quinoprotein glucose dehydrogenase. EMBO J 18: 5187-5194. (Pubitemid 29465569)
31. Oubrie A, Rozeboom HJ, Kalk KH, Duine JA, Dijkstra BW (1999) The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat. J Mol Biol 289: 319-333. (Pubitemid 29278385)
32. Oubrie A, Rozeboom HJ, Dijkstra BW (1999) Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex. Proc Natl Acad Sci U S A 96: 11787-11791. (Pubitemid 29502810)
33. Sakuraba H, Yokono K, Yoneda K, Watanabe A, Asada Y, et al. (2010) Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum. Arch Biochem Biophys 502: 81-88.
34. Southall SM, Doel JJ, Richardson DJ, Oubrie A (2006) Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed active site conferring broad substrate specificity. J Biol Chem 281: 30650-30659. (Pubitemid 44582120)
35. Bishop B, Aricescu AR, Harlos K, O'Callaghan CA, Jones EY, et al. (2009) Structural insights into hedgehog ligand sequestration by the human hedgehog-interacting protein HHIP. Nat Struct Mol Biol 16: 698-703.
36. Kasahara T, Kato T (2003) Nutritional biochemistry: A new redox-cofactor vitamin for mammals. Nature 422: 832. (Pubitemid 36520027)