메뉴 건너뛰기




Volumn 43, Issue 18, 2004, Pages 5494-5502

Further Insights into Quinone Cofactor Biogenesis: Probing the Role of mauG in Methylamine Dehydrogenase Tryptophan Tryptophylquinone Formation

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; ELECTROPHORESIS; GENETIC ENGINEERING; HYDROXYLATION;

EID: 2442582496     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049863l     Document Type: Article
Times cited : (72)

References (23)
  • 2
    • 0034797851 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase
    • Davidson, V. L. (2001) Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase, Adv. Protein Chem. 58, 95-140.
    • (2001) Adv. Protein Chem. , vol.58 , pp. 95-140
    • Davidson, V.L.1
  • 3
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role
    • Husain, M., and Davidson, V. L. (1985) An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role, J. Biol. Chem. 260, 14626-14629.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidson, V.L.2
  • 4
    • 0024968255 scopus 로고
    • Cytochrome c-550 mediates electron transfer from inducible periplasmic c-type cytochromes to the cytoplasmic membrane of Paracoccus denitrificans
    • Davidson, V. L., and Kumar, M. A. (1989) Cytochrome c-550 mediates electron transfer from inducible periplasmic c-type cytochromes to the cytoplasmic membrane of Paracoccus denitrificans, FEBS Lett. 245, 271-273.
    • (1989) FEBS Lett. , vol.245 , pp. 271-273
    • Davidson, V.L.1    Kumar, M.A.2
  • 5
    • 0022998580 scopus 로고
    • Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans
    • Husain, M., and Davidson, V. L. (1986) Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans, J. Biol. Chem. 261, 8577-8580.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8577-8580
    • Husain, M.1    Davidson, V.L.2
  • 6
    • 0035227063 scopus 로고    scopus 로고
    • Mechanisms of biosynthesis of protein-derived redox cofactors
    • Schwartz, B., and Klinman, J. P. (2001) Mechanisms of biosynthesis of protein-derived redox cofactors, Vitam. Horm. 61, 219-239.
    • (2001) Vitam. Horm. , vol.61 , pp. 219-239
    • Schwartz, B.1    Klinman, J.P.2
  • 7
    • 0033942582 scopus 로고    scopus 로고
    • Novel cofactors via posttranslational modifications of enzyme active sites
    • Okeley, N. M., and van der Donk, W. A. (2000) Novel cofactors via posttranslational modifications of enzyme active sites, Chem. Biol. 7, R159-171.
    • (2000) Chem. Biol. , vol.7
    • Okeley, N.M.1    Van Der Donk, W.A.2
  • 8
    • 0028605705 scopus 로고
    • Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase
    • Cai, D., and Klinman, J. P. (1994) Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase, J. Biol. Chem. 269, 32039-32042.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32039-32042
    • Cai, D.1    Klinman, J.P.2
  • 9
    • 0031058899 scopus 로고    scopus 로고
    • Mechanistic studies of topa quinone biogenesis in phenylethylamine oxidase
    • Ruggiero, C. E., Smith, J. A., Tanizawa, K., and Dooley, D. M. (1997) Mechanistic studies of topa quinone biogenesis in phenylethylamine oxidase, Biochemistry 36, 1953-1959.
    • (1997) Biochemistry , vol.36 , pp. 1953-1959
    • Ruggiero, C.E.1    Smith, J.A.2    Tanizawa, K.3    Dooley, D.M.4
  • 10
    • 0027965409 scopus 로고
    • Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue
    • Matsuzaki, R., Fukui, T., Sato, H., Ozaki, Y., and Tanizawa, K. (1994) Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue, FEBS Lett. 351, 360-364.
    • (1994) FEBS Lett. , vol.351 , pp. 360-364
    • Matsuzaki, R.1    Fukui, T.2    Sato, H.3    Ozaki, Y.4    Tanizawa, K.5
  • 11
    • 0025785660 scopus 로고
    • A new cofactor in a prokaryotic enzyme: Tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase
    • McIntire, W. S., Wemmer, D. E., Chistoserdov, A., and Lidstrom, M. E. (1991) A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase, Science 252, 817-824.
    • (1991) Science , vol.252 , pp. 817-824
    • McIntire, W.S.1    Wemmer, D.E.2    Chistoserdov, A.3    Lidstrom, M.E.4
  • 12
    • 0037465763 scopus 로고    scopus 로고
    • Understanding quinone cofactor biogenesis in methylamine dehydrogenase through novel cofactor generation
    • Pearson, A. R., Jones, L. H., Higgins, L., Ashcroft, A. E., Wilmot, C. M., and Davidson, V. L. (2003) Understanding quinone cofactor biogenesis in methylamine dehydrogenase through novel cofactor generation, Biochemistry 42, 3224-3230.
    • (2003) Biochemistry , vol.42 , pp. 3224-3230
    • Pearson, A.R.1    Jones, L.H.2    Higgins, L.3    Ashcroft, A.E.4    Wilmot, C.M.5    Davidson, V.L.6
  • 13
    • 0026720414 scopus 로고
    • The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans
    • Chistoserdov, A. Y., Boyd, J., Mathews, F. S., and Lidstrom, M. E. (1992) The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans, Biochem. Biophys. Res. Commun. 184, 1181-1189.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1181-1189
    • Chistoserdov, A.Y.1    Boyd, J.2    Mathews, F.S.3    Lidstrom, M.E.4
  • 14
    • 0028216615 scopus 로고
    • Genetic organization of the mau gene cluster in Methylobacterium extorquens AMI: Complete nucleotide sequence and generation and characteristics of mau mutants
    • Chistoserdov, A. Y., Chistoserdova, L. V., McIntire, W. S., and Lidstrom, M. E. (1994) Genetic organization of the mau gene cluster in Methylobacterium extorquens AMI: complete nucleotide sequence and generation and characteristics of mau mutants, J. Bacteriol. 176, 4052-4065.
    • (1994) J. Bacteriol. , vol.176 , pp. 4052-4065
    • Chistoserdov, A.Y.1    Chistoserdova, L.V.2    McIntire, W.S.3    Lidstrom, M.E.4
  • 16
    • 0038070331 scopus 로고    scopus 로고
    • MauG, a novel dibeme protein required for tryptophan tryptophylquinone biogenesis
    • Wang, Y., Graichen, M. E., Liu, A., Pearson, A. R., Wilmot, C. M., and Davidson, V. L. (2003) MauG, a novel dibeme protein required for tryptophan tryptophylquinone biogenesis, Biochemistry 42, 7318-7325.
    • (2003) Biochemistry , vol.42 , pp. 7318-7325
    • Wang, Y.1    Graichen, M.E.2    Liu, A.3    Pearson, A.R.4    Wilmot, C.M.5    Davidson, V.L.6
  • 17
    • 0032788792 scopus 로고    scopus 로고
    • Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides
    • Graichen, M. E., Jones, L. H., Sharma, B. V., van Spanning, R. J., Hosler, J. P., and Davidson, V. L. (1999) Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides, J. Bacteriol. 181, 4216-4222.
    • (1999) J. Bacteriol. , vol.181 , pp. 4216-4222
    • Graichen, M.E.1    Jones, L.H.2    Sharma, B.V.3    Van Spanning, R.J.4    Hosler, J.P.5    Davidson, V.L.6
  • 18
    • 0034254541 scopus 로고    scopus 로고
    • Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridge
    • Zhu, Z., Jones, L. H., Graichen, M. E., and Davidson, V. L. (2000) Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridge, Biochemistry 39, 8830-8836.
    • (2000) Biochemistry , vol.39 , pp. 8830-8836
    • Zhu, Z.1    Jones, L.H.2    Graichen, M.E.3    Davidson, V.L.4
  • 19
    • 0028923873 scopus 로고
    • An enhanced broad-host-range vector for gram-negative bacteria: Avoiding tetracycline phototoxicity during the growth of photosynthetic bacteria
    • Mather, M. W., McReynolds, L. M., and Yu, C. A. (1995) An enhanced broad-host-range vector for gram-negative bacteria: avoiding tetracycline phototoxicity during the growth of photosynthetic bacteria, Gene 156, 85-88.
    • (1995) Gene , vol.156 , pp. 85-88
    • Mather, M.W.1    McReynolds, L.M.2    Yu, C.A.3
  • 20
    • 0025026513 scopus 로고
    • Methylamine dehydrogenases from methylotrophic bacteria
    • Davidson, V. L. (1990) Methylamine dehydrogenases from methylotrophic bacteria, Methods Enzymol. 188, 241-246.
    • (1990) Methods Enzymol. , vol.188 , pp. 241-246
    • Davidson, V.L.1
  • 21
    • 0026643221 scopus 로고
    • Cofactor-directed inactivation by nucleophilic amines of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
    • Davidson, V. L., and Jones, L. H. (1992) Cofactor-directed inactivation by nucleophilic amines of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans, Biochim. Biophys. Acta 1121, 104-110.
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 104-110
    • Davidson, V.L.1    Jones, L.H.2
  • 22
    • 0036279657 scopus 로고    scopus 로고
    • Lysozyme-osmotic shock methods for localization of periplasmic redox proteins in bacteria
    • Davidson, V. L., and Sun, D. (2002) Lysozyme-osmotic shock methods for localization of periplasmic redox proteins in bacteria, Methods Enzymol. 353, 121-130.
    • (2002) Methods Enzymol. , vol.353 , pp. 121-130
    • Davidson, V.L.1    Sun, D.2
  • 23
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., Priefer, U., and Puhler, A. (1983) A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria, Bio/Technology 1, 784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.