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Volumn 44, Issue 41, 2005, Pages 13467-13476

Mutagenesis of glycine 179 modulates both catalytic efficiency and reduced pyridine nucleotide specificity in cytochrome b5 reductase

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CYTOLOGY; ENZYMES; OXIDATION; REDUCTION; STOICHIOMETRY;

EID: 26644470345     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051165t     Document Type: Article
Times cited : (14)

References (47)
  • 4
    • 0014980147 scopus 로고
    • 5 in fatty acid desaturation by rat liver microsomes
    • 5 in fatty acid desaturation by rat liver microsomes, J. Biochem. 69, 155-167.
    • (1971) J. Biochem. , vol.69 , pp. 155-167
    • Oshino, N.1    Imai, Y.2    Sato, R.3
  • 5
    • 0017391211 scopus 로고
    • Mechanism of C-5 double bond introduction in the biosynthesis of cholesterol by rat liver microsomes
    • Reddy, V., Kupfer, D., and Capsi, E. (1977) Mechanism of C-5 double bond introduction in the biosynthesis of cholesterol by rat liver microsomes, J. Biol. Chem. 252, 2797-2801.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2797-2801
    • Reddy, V.1    Kupfer, D.2    Capsi, E.3
  • 8
    • 0017360738 scopus 로고
    • Direct desaturation of eicosatrienoyl lecithin to arachidonoyl lecithin by rat liver microsomes
    • Pugh, E. L., and Kates, M. (1977) Direct desaturation of eicosatrienoyl lecithin to arachidonoyl lecithin by rat liver microsomes, J. Biol. Chem. 252, 68-73.
    • (1977) J. Biol. Chem. , vol.252 , pp. 68-73
    • Pugh, E.L.1    Kates, M.2
  • 9
    • 0032881906 scopus 로고    scopus 로고
    • 5 reductase gene from an arachidonic acid-producing fungus, Mortierella alpina 1S-4, by sequencing of the encoding cDNA and heterologous expression in a fungus, Aspergillus oryzae
    • 5 reductase gene from an arachidonic acid-producing fungus, Mortierella alpina 1S-4, by sequencing of the encoding cDNA and heterologous expression in a fungus, Aspergillus oryzae, Appl. Environ. Microbiol. 65, 3873-3879.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3873-3879
    • Sakuradani, E.1    Kobayashi, M.2    Shimizu, S.3
  • 14
    • 26644465161 scopus 로고    scopus 로고
    • Direct Submission BC045880
    • Strausberg, R. (2003) GenBank Direct Submission BC045880.
    • (2003) GenBank
    • Strausberg, R.1
  • 21
    • 0027365610 scopus 로고
    • Structural prototypes for an extended family of flavoprotein reductase: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin
    • Correll, C. C., Ludwig, M. L., Bruns, C. M., and Karplus, P. A. (1993) Structural prototypes for an extended family of flavoprotein reductase: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin, Protein Sci. 2, 2112-2133.
    • (1993) Protein Sci. , vol.2 , pp. 2112-2133
    • Correll, C.C.1    Ludwig, M.L.2    Bruns, C.M.3    Karplus, P.A.4
  • 22
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym, O., and Eisenberg, D. (2001) Sequence-structure analysis of FAD-containing proteins, Protein Sci. 10, 1712-1728.
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 24
    • 0027940215 scopus 로고
    • 5 reductase to two different submitochondrial compartments
    • 5 reductase to two different submitochondrial compartments, Cell 79, 829-839.
    • (1994) Cell , vol.79 , pp. 829-839
    • Hahne, K.1    Haucke, V.2    Ramage, L.3    Schatz, G.4
  • 26
    • 0034595224 scopus 로고    scopus 로고
    • Interaction of NADP-(H) with oxidized and reduced P450 reductase during catalysis. Studies with nucleotide analogs
    • Murataliev, M. B., and Feyereisen, R. (2000) Interaction of NADP-(H) with oxidized and reduced P450 reductase during catalysis. Studies with nucleotide analogs, Biochemistry 39, 5066-5074.
    • (2000) Biochemistry , vol.39 , pp. 5066-5074
    • Murataliev, M.B.1    Feyereisen, R.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0035476429 scopus 로고    scopus 로고
    • Assimilatory nitrate reductase: Lysine 741 participates in pyridine nucleotide binding via charge complementarity
    • Barber, M. J., Desai, S. K., and Marohnic, C. C. (2001) Assimilatory nitrate reductase: Lysine 741 participates in pyridine nucleotide binding via charge complementarity, Arch. Biochem. Biophys. 394, 99-110.
    • (2001) Arch. Biochem. Biophys. , vol.394 , pp. 99-110
    • Barber, M.J.1    Desai, S.K.2    Marohnic, C.C.3
  • 31
    • 0002435359 scopus 로고
    • A simple method for the determination of redox potentials
    • (Curti, B., Ronchi, S., and Zanetti, G., Eds.), de Gruyter, Berlin, Germany
    • Massey, V. (1991) A simple method for the determination of redox potentials, in Flavin and Flavoproteins 1990 (Curti, B., Ronchi, S., and Zanetti, G., Eds.) pp 59-66, de Gruyter, Berlin, Germany.
    • (1991) Flavin and Flavoproteins 1990 , pp. 59-66
    • Massey, V.1
  • 33
    • 0001826757 scopus 로고
    • Free flavins: Syntheses, chemical, and physical properties
    • (Müller, F., Ed.), CRC Press, Boca Raton, FL
    • Müller, F. (1991) Free flavins: Syntheses, chemical, and physical properties, in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) Vol. 1, pp 1-60, CRC Press, Boca Raton, FL.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , pp. 1-60
    • Müller, F.1
  • 34
    • 2442736277 scopus 로고    scopus 로고
    • Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site
    • Kuchler, B., Abdel-Ghany, A. G., Bross, P., Nandy, A., Rasched, I., and Ghisla, S. (1999) Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site, Biochem. J. 337, 225-230.
    • (1999) Biochem. J. , vol.337 , pp. 225-230
    • Kuchler, B.1    Abdel-Ghany, A.G.2    Bross, P.3    Nandy, A.4    Rasched, I.5    Ghisla, S.6
  • 35
    • 0242653652 scopus 로고    scopus 로고
    • 5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site
    • 5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site, Biochemistry 42, 13145-13151.
    • (2003) Biochemistry , vol.42 , pp. 13145-13151
    • Bewley, M.C.1    Davis, C.A.2    Marohnic, C.C.3    Taormina, D.4    Barber, M.J.5
  • 37
    • 0037423305 scopus 로고    scopus 로고
    • 5 reductase in catalysis and control of the rate-limiting step in electron transfer
    • 5 reductase in catalysis and control of the rate-limiting step in electron transfer, J. Biol. Chem. 278, 3580-3589.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3580-3589
    • Kimura, S.1    Kawamura, M.2    Iyanagi, T.3
  • 38
    • 16544368613 scopus 로고    scopus 로고
    • 5 reductase; the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159*
    • 5 reductase; the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159*, Arch. Biochem. Biophys. 431, 233-244.
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 233-244
    • Davis, C.A.1    Crowley, L.J.2    Barber, M.J.3
  • 40
    • 0025773635 scopus 로고
    • 5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential
    • 5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential, J. Biol. Chem. 266, 7531-7536.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7531-7536
    • Shirabe, K.1    Yubisui, T.2    Nishino, T.3    Takeshita, M.4
  • 42
    • 0037073754 scopus 로고    scopus 로고
    • Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in vivo
    • Elmore, C. L., and Porter, T. D. (2002) Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in vivo, J. Biol. Chem. 277, 48960-48964.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48960-48964
    • Elmore, C.L.1    Porter, T.D.2
  • 43
    • 0032188938 scopus 로고    scopus 로고
    • Engineering of pyridine nucleotide specificity of nitrate reductase: Mutagenesis of recombinant cytochrome b reductase fragment of Neurospora crassa NADPH:Nitrate reductase
    • Shiraishi, N., Croy, C, Kaur, J., and Campbell, W. H. (1998) Engineering of pyridine nucleotide specificity of nitrate reductase: Mutagenesis of recombinant cytochrome b reductase fragment of Neurospora crassa NADPH:Nitrate reductase, Arch. Biochem. Biophys. 358, 104-115.
    • (1998) Arch. Biochem. Biophys. , vol.358 , pp. 104-115
    • Shiraishi, N.1    Croy, C.2    Kaur, J.3    Campbell, W.H.4
  • 44
    • 25944466965 scopus 로고    scopus 로고
    • Altered pyridine nucleotide specificity of spinach nitrate reductase
    • Barber, M. J. (2000) Altered pyridine nucleotide specificity of spinach nitrate reductase, FASEB J. 14, A1416.
    • (2000) FASEB J. , vol.14
    • Barber, M.J.1
  • 45
    • 0036845955 scopus 로고    scopus 로고
    • Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae
    • Serov, A. E., Popova, A. S., Fedorchuk, V. V., and Tishkov, V. I. (2002) Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae, Biochem. J. 367, 841-847.
    • (2002) Biochem. J. , vol.367 , pp. 841-847
    • Serov, A.E.1    Popova, A.S.2    Fedorchuk, V.V.3    Tishkov, V.I.4
  • 46
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools, Nucleic Acids Res. 24, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.