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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

Leonid V Bystrykh, Janet Vonck, Ernst FJ van Bruggen, Jozef Van Beeumen, Bart Samyn UGent, Natalya I Govorukhina, Nico Arfman, Johannis A Duine and Lubbert Dijkhuizen (1993) JOURNAL OF BACTERIOLOGY. 175(6). p.1814-1822
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
ZYMOMONAS-MOBILIS, ALCOHOL-DEHYDROGENASE, ESCHERICHIA-COLI, BIOLOGICAL MACROMOLECULES, SACCHAROMYCES-CEREVISIAE, THERMOTOLERANT BACILLUS, PROTEIN, IMAGES, GENE, PARTICLES
journal title
JOURNAL OF BACTERIOLOGY
J. Bacteriol.
volume
175
issue
6
pages
1814-1822 pages
Web of Science type
Article
ISSN
0021-9193
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
201171
handle
http://hdl.handle.net/1854/LU-201171
alternative location
http://jb.asm.org/cgi/content/abstract/175/6/1814
date created
2004-01-14 13:42:00
date last changed
2016-12-19 15:38:46
@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},
}

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.