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Electron microscopic analysis and structural characterization of novel NADP(H)-containing methanol:N,N'-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19

(1993) JOURNAL OF BACTERIOLOGY. 175(6). p.1814-1822
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Abstract
The quaternary protein structure of two methanol:N,N'-dimethyl-4-nitrosoaniline (NDMA) oxidoreductases purified from Amycolatopsis methanolica and Mycobacterium gastri MB19 was analyzed by electron microscopy and image processing. The enzymes are decameric proteins (displaying fivefold symmetry) with estimated molecular masses of 490 to 500 kDa based on their subunit molecular masses of 49 to 50 kDa. Both methanol:NDMA oxidoreductases possess a tightly but noncovalently bound NADP(H) cofactor at an NADPH-to-subunit molar ratio of 0.7. These cofactors are redox active toward alcohol and aldehyde substrates. Both enzymes contain significant amounts of Zn2+ and Mg2+ ions. The primary amino acid sequences of the A. methanolica and M. gastri MB19 methanol:NDMA oxidoreductases share a high degree of identity, as indicated by N-terminal sequence analysis (63% identity among the first 27 N-terminal amino acids), internal peptide sequence analysis, and overall amino acid composition. The amino acid sequence analysis also revealed significant similarity to a decameric methanol dehydrogenase of Bacillus methanolicus C1.
Keywords
ZYMOMONAS-MOBILIS, ALCOHOL-DEHYDROGENASE, ESCHERICHIA-COLI, BIOLOGICAL MACROMOLECULES, SACCHAROMYCES-CEREVISIAE, THERMOTOLERANT BACILLUS, PROTEIN, IMAGES, GENE, PARTICLES

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Chicago
Bystrykh, Leonid V, Janet Vonck, Ernst FJ van Bruggen, Jozef Van Beeumen, Bart Samyn, Natalya I Govorukhina, Nico Arfman, Johannis A Duine, and Lubbert Dijkhuizen. 1993. “Electron Microscopic Analysis and Structural Characterization of Novel NADP(H)-containing methanol:N,N’-dimethyl-4-nitrosoaniline Oxidoreductases from the Gram-positive Methylotrophic Bacteria Amycolatopsis Methanolica and Mycobacterium Gastri MB19.” Journal of Bacteriology 175 (6): 1814–1822.
APA
Bystrykh, L. V., Vonck, J., van Bruggen, E. F., Van Beeumen, J., Samyn, B., Govorukhina, N. I., Arfman, N., et al. (1993). Electron microscopic analysis and structural characterization of novel NADP(H)-containing methanol:N,N’-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19. JOURNAL OF BACTERIOLOGY, 175(6), 1814–1822.
Vancouver
1.
Bystrykh LV, Vonck J, van Bruggen EF, Van Beeumen J, Samyn B, Govorukhina NI, et al. Electron microscopic analysis and structural characterization of novel NADP(H)-containing methanol:N,N’-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19. JOURNAL OF BACTERIOLOGY. 1993;175(6):1814–22.
MLA
Bystrykh, Leonid V, Janet Vonck, Ernst FJ van Bruggen, et al. “Electron Microscopic Analysis and Structural Characterization of Novel NADP(H)-containing methanol:N,N’-dimethyl-4-nitrosoaniline Oxidoreductases from the Gram-positive Methylotrophic Bacteria Amycolatopsis Methanolica and Mycobacterium Gastri MB19.” JOURNAL OF BACTERIOLOGY 175.6 (1993): 1814–1822. Print.
@article{201171,
  abstract     = {The quaternary protein structure of two methanol:N,N'-dimethyl-4-nitrosoaniline (NDMA) oxidoreductases purified from Amycolatopsis methanolica and Mycobacterium gastri MB19 was analyzed by electron microscopy and image processing. The enzymes are decameric proteins (displaying fivefold symmetry) with estimated molecular masses of 490 to 500 kDa based on their subunit molecular masses of 49 to 50 kDa. Both methanol:NDMA oxidoreductases possess a tightly but noncovalently bound NADP(H) cofactor at an NADPH-to-subunit molar ratio of 0.7. These cofactors are redox active toward alcohol and aldehyde substrates. Both enzymes contain significant amounts of Zn2+ and Mg2+ ions. The primary amino acid sequences of the A. methanolica and M. gastri MB19 methanol:NDMA oxidoreductases share a high degree of identity, as indicated by N-terminal sequence analysis (63\% identity among the first 27 N-terminal amino acids), internal peptide sequence analysis, and overall amino acid composition. The amino acid sequence analysis also revealed significant similarity to a decameric methanol dehydrogenase of Bacillus methanolicus C1.},
  author       = {Bystrykh, Leonid V and Vonck, Janet and van Bruggen, Ernst FJ and Van Beeumen, Jozef and Samyn, Bart and Govorukhina, Natalya I and Arfman, Nico and Duine, Johannis A and Dijkhuizen, Lubbert},
  issn         = {0021-9193},
  journal      = {JOURNAL OF BACTERIOLOGY},
  keyword      = {ZYMOMONAS-MOBILIS,ALCOHOL-DEHYDROGENASE,ESCHERICHIA-COLI,BIOLOGICAL MACROMOLECULES,SACCHAROMYCES-CEREVISIAE,THERMOTOLERANT BACILLUS,PROTEIN,IMAGES,GENE,PARTICLES},
  language     = {eng},
  number       = {6},
  pages        = {1814--1822},
  title        = {Electron microscopic analysis and structural characterization of novel NADP(H)-containing methanol:N,N'-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19},
  url          = {http://jb.asm.org/cgi/content/abstract/175/6/1814},
  volume       = {175},
  year         = {1993},
}