Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: Its structure comparison with other quinoproteins

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1647, Issue 1-2, 2003, Pages 185-192

  Yamada, Mamoru ^a   Elias, M D ^a   Matsushita, Kazunobu ^a   Migita, Catharina T ^a   Adachi, Osao ^a  

^a YAMAGUCHI UNIVERSITY   (Japan)

Author keywords

Bound quinone; Domain structure; Glucose dehydrogenase; Molecular evolution; PQQ semiquinone; Quinoprotein

Indexed keywords

1,4 BENZOQUINONE; ALCOHOL DEHYDROGENASE; AMINO ACID; GLUCOSE DEHYDROGENASE; IDITOL DEHYDROGENASE; LUPANINE HYDROXYLASE; METHANOL DEHYDROGENASE; POLYVINYL ALCOHOL DEHYDROGENASE; PROTEIN; PYRROLOQUINOLINEQUINONE; QUINATE DEHYDROGENASE; RADICAL; TETRAHYDROFURFURYL ALCOHOL DEHYDROGENASE; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; GLUCOSE DEHYDROGENASE (PYRROLOQUINOLINE QUINONE); GLUCOSE DEHYDROGENASE (PYRROLOQUINOLINE-QUINONE); PROTEIN SUBUNIT; QUINOLONE DERIVATIVE; QUINONE DERIVATIVE;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFERENCE PAPER; ELECTRON TRANSPORT; ESCHERICHIA COLI; MOLECULAR EVOLUTION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REACTION ANALYSIS; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; TRANSPORT KINETICS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; REVIEW;

ESCHERICHIA COLI; NEGIBACTERIA;

BINDING SITES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUCOSE DEHYDROGENASES; MODELS, MOLECULAR; PQQ COFACTOR; PROTEIN SUBUNITS; QUINOLONES; QUINONES;

EID: 0038312036     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00100-6     Document Type: Conference Paper

References (40)

1. Matsushita K., Toyama H., Yamada M., Adachi O. Quinoproteins: structure, function, and biotechnological applications. Appl. Microbiol. Biotechnol. 58:2002;13-22.
2. Anthony C., Ghosh M., Blake C.C.F. The structure and function of methanol dehydrogenase and related PQQ-containing quinoproteins. J. Biochem. 304:1994;665-674.
3. Groen B.W., Frank J., Duine J.A. Quinoprotein alcohol dehydrogenase from ethanol-grown Pseudomonas aeruginosa. J. Biochem. 223:1984;921-924.
4. de Jong G.A., Geerlof A., Stoorvogel J., Jongejan J.A., de Vries S., Duine J.A. Quinoprotein ethanol dehydrogenase from Comamonas testosteroni. Purification, characterization, and reconstitution of the apoenzyme with pyrroloquinoline quinone analogues. Eur. J. Biochem. 230:1995;899-905.
5. Toyama H., Fujii A., Matsushita K., Shinagawa E., Ameyama M., Adachi O. Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols. J. Bacteriol. 177:1995;2442-2450.
6. Matsushita K., Toyama H., Adachi O. Respiratory chain and bioenergetics of acetic acid bacteria. Adv. Microb. Physiol. 39:1994;247-301.
7. Matsushita K., Yakushi T., Toyama H., Shinagawa E., Adachi O. Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase cytochrome c complex of Gluconobacter suboxydans. J. Biol. Chem. 271:1996;4850-4857.
8. Cleton-Jansen A.-M., Goosen N., Fayet O., Van de Putte P. Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase. J. Bacteriol. 172:1990;6308-6315.
9. Yamada M., Asaoka S., Saier M.H. Jr., Yamada Y. Characterization of the gcd gene from Escherichia coli K-12 W3110 and regulation of its expression. J. Bacteriol. 175:1993;568-571.
10. Elsemore D.A., Ornston L.N. The pca-pob supraoperonic cluster of Acinetobacter calcoaceticus contains quiA, the structural gene for quinate-shikimate dehydrogenase. J. Bacteriol. 176:1994;7659-7666.
11. Miyazaki T., Tomiyama N., Shinjoh M., Hoshino T. Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxidans IFO 3255 which requires Pyrroloquinoline quinone and hydrophobic protein SldB for the activity development in E. coli. Biosci. Biotechnol. Biochem. 66:2002;262-270.
12. Adachi O., Fujii Y., Ghaly M.F., Toyama H., Shinagawa E., Matsushita K. Membrane-bound quinoprotein D-arabitol dehydrogenase of Gluconobacter suboxydans IFO 3257: a versatile enzyme for the oxidative fermentation of various ketoses. Biosci. Biotechnol. Biochem. 65:2001;2755-2762.
13. Xia Z.-X., Dai W.-W., Xiong J.-P., Hao Z.-P., Davidson V.L., White S., Mathews F.S. The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.61°A resolution. J. Biol. Chem. 267:1992;22289-22297.
14. Xia Z., Dai W., Zhang Y., White S.A., Boyd G.D., Mathews F.S. Determination of the gene sequence and the three-dimensional structure at 2 angstrom resolution of methanol dehydrogenase from Methylophilus W3A1. J. Mol. Biol. 259:1996;480-501.
15. Ghosh M., Anthony C., Harlos K., Goodwin M.G., Blake C.C.F. The Methylobacterium extorquens at 1.94°A. Structure. 3:1995;177-187.
16. Keitel T., Diehl A., Knaute T., Stezowski J.J., Hohne W., Gorisch H. X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity. J. Mol. Biol. 297:2000;961-974.
17. Zhi-wei C., Baruch P., Mathews F.S., Matsushita K., Yamashita T., Toyama H., Adachi O. Crystallization and preliminary diffraction studies of two quinoprotein alcohol dehydrogenases (ADHs): a soluble monomeric ADH from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from Gluconobacter suboxydans (ADH-GS). Acta Crystallogr., D. 55:1999;1933-1936.
18. Cleton-Jansen A.-M., Goosen N., Wenzel T.J., van de Putte P. Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme. J. Bacteriol. 170:1988;2121-2125.
19. Oubrie A., Rozeboom H.J., Kalk K.H., Olsthoorm A.J.J., Duine J.A., Dijkstra B.W. Structure and mechanism of soluble quinoprotein glucose dehydrogenase. EMBO J. 18:1999;5187-5194.
20. Cozier G.E., Anthony C. Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens. J. Biochem. 312:1995;679-685.
21. Cozier G.E., Giles I.G., Anthony C. The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem. J. Biochem. 307:1995;375-379.
22. Elias M.D., Tanaka M., Sakai M., Toyama H., Matsushita K., Adachi O., Yamada M. C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone. J. Biol. Chem. 276:2001;48356-48361.
23. Anthony C. The c-type cytochromes of methylotrophic bacteria. Biochim. Biophys. Acta. 1099:1992;1-15.
24. Matsushita K., Yamashita T., Aoki N., Toyama H., Adachi O. Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5. Biochemistry. 38:1999;6111-6118.
25. Matsushita K., Takaki Y., Shinagawa E., Ameyama M., Adachi O. Ethanol oxidase respiratory chain of acetic acid bacteria - reactivity with ubiquinone of pyrroloquinoline quinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans. Biosci. Biotechnol. Biochem. 56:1992;304-310.
26. Yamada M., Sumi K., Matsushita K., Adachi O., Yamada Y. Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site. J. Biol. Chem. 268:1993;12812-12817.
27. Friedrich T., Strohdeicher M., Hofhaus G., Preis D., Sahm H., Weiss H. The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase. FEBS Lett. 265:1990;37-40.
28. Elias M.D., Tanaka M., Izu H., Matsushita K., Adachi O., Yamada M. Functions of amino acid residues in the active site of Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase. J. Biol. Chem. 275:2000;7321-7326.
29. Cozier G.E., Salleh R.A., Anthony C. Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine. J. Biochem. 340:1999;639-647.
30. Yamada M., Inbe H., Tanaka M., Sumi K., Matsushita K., Adachi O. Mutant isolation of the Escherichia coli quinoprotein glucose dehydrogenase and analysis of crucial residues Asp-730 and His-775 for its function. J. Biol. Chem. 273:1998;22021-22027.
31. Okuda J., Yoshida H., Kojima K., Himi M., Sode K. The role of conserved His775/781 in membrane-binding PQQ glucose dehydrogenase of Escherichia coli and Acinetobacter calcoaceticus. J. Biochem. Mol. Biol. Biophys. 4:2000;415-422.
32. Matsushita K., Arents J.C., Bader R., Yamada M., Adachi O., Postma P.W. Escherichia coli is unable to produce pyrroloquinoline quinone (PQQ). Microbiology. 143:1997;3149-3156.
33. de Beer R., Duine J.A., Frank J., Westerling J. The role of pyrrolo-quinoline semiquinone forms in the mechanism of action of methanol dehydrogenase. Eur. J. Biochem. 130:1983;105-109.
34. Anthony C. Sinnot M. Quinoprotein-Catalysed Reaction. 1998;155-180 Academic Press, London.
35. 2+ stabilizes the semiquinone radical of pyrroloquinoline quinone. J. Biochem. 357:2001;893-898.
36. Sato-Watanabe M., Mogi T., Ogura T., Kitagawa T., Miyoshi H., Iwamura H., Anraku Y. Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli. J. Biol. Chem. 269:1994;28908-28912.
37. Collins M.D., Jones D. Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implications. Microbiol. Rev. 45:1981;316-354.
38. Frank J., van Krimpen S.H., Verwiel P.E.J., Jongejan J.A., Mulder A.C., Duine J.A. On the mechanism of inhibition of methanol dehydrogenase by cyclopropane-derived inhibitors. Eur. J. Biochem. 184:1989;187-195.
39. Jongejan A., Jongejan J.A., Hagen W.R. 3rd International Symposium on Vitamin B6, PQQ, Carbonyl Catalysis and Quinoproteins. 2002;54.
40. Goodwin P.M., Anthony C. The biochemistry, physiology and genetics of PQQ and PQQ-containing enzymes. Adv. Microbiol. Physiol. 40:1998;1-80.