This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zarnt, G. Articles by Andreesen, J. R. Search for Related Content PubMed PubMed Citation Articles by Zarnt, G. Articles by Andreesen, J. R. Agricola Articles by Zarnt, G. Articles by Andreesen, J. R.

 Previous Article  |  Next Article 

Appl. Environ. Microbiol., Dec 1997, 4891-4898, Vol 63, No. 12
Copyright © 1997, American Society for Microbiology

Degradation of tetrahydrofurfuryl alcohol by Ralstonia eutropha is initiated by an inducible pyrroloquinoline quinone-dependent alcohol dehydrogenase

G Zarnt, T Schrader and JR Andreesen
Institut fur Mikrobiologie, Martin-Luther-Universitat Halle, Germany.

An organism tentatively identified as Ralstonia eutropha was isolated from enrichment cultures containing tetrahydrofurfuryl alcohol (THFA) as the sole source of carbon and energy. The strain was able to tolerate up to 200 mM THFA in mineral salt medium. The degradation was initiated by an inducible ferricyanide-dependent alcohol dehydrogenase (ADH) which was detected in the soluble fraction of cell extracts. The enzyme catalyzed the oxidation of THFA to the corresponding tetrahydrofuran-2-carboxylic acid. Studies with n-pentanol as the substrate revealed that the corresponding aldehyde was released as a free intermediate. The enzyme was purified 211-fold to apparent homogeneity and could be identified as a quinohemoprotein containing one pyrroloquinoline quinone and one covalently bound heme c per monomer. It was a monomer of 73 kDa and had an isoelectric point of 9.1. A broad substrate spectrum was obtained for the enzyme, which converted different primary alcohols, starting from C2 compounds, secondary alcohols, diols, polyethylene glycol 6000, and aldehydes, including formaldehyde. A sequence identity of 65% with a quinohemoprotein ADH from Comamonas testosteroni was found by comparing 36 N-terminal amino acids. The ferricyanide-dependent ADH activity was induced during growth on different alcohols except ethanol. In addition to this activity, an NAD-dependent ADH was present depending on the alcohol used as the carbon source.

This article has been cited by other articles:

• Hirota-Mamoto, R., Nagai, R., Tachibana, S., Yasuda, M., Tani, A., Kimbara, K., Kawai, F. (2006). Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase. Microbiology 152: 1941-1949 [Abstract] [Full Text]  
• Vangnai, A. S., Sayavedra-Soto, L. A., Arp, D. J. (2002). Roles for the Two 1-Butanol Dehydrogenases of Pseudomonas butanovora in Butane and 1-Butanol Metabolism. J. Bacteriol. 184: 4343-4350 [Abstract] [Full Text]  
• Vangnai, A. S., Arp, D. J., Sayavedra-Soto, L. A. (2002). Two Distinct Alcohol Dehydrogenases Participate in Butane Metabolism by Pseudomonas butanovora. J. Bacteriol. 184: 1916-1924 [Abstract] [Full Text]  
• Oubrie, A., Rozeboom, H. J., Kalk, K. H., Huizinga, E. G., Dijkstra, B. W. (2002). Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni. STRUCTURAL BASIS FOR SUBSTRATE OXIDATION AND ELECTRON TRANSFER. J. Biol. Chem. 277: 3727-3732 [Abstract] [Full Text]  
• Schrader, T., Zarnt, G., Andreesen, J. R. (2001). NAD(P)-Dependent Aldehyde Dehydrogenases Induced during Growth of Ralstonia eutropha Strain Bo on Tetrahydrofurfuryl Alcohol. J. Bacteriol. 183: 7408-7411 [Abstract] [Full Text]  
• Zarnt, G., Schräder, T., Andreesen, J. R. (2001). Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo. J. Bacteriol. 183: 1954-1960 [Abstract] [Full Text]  
• Vangnai, A. S., Arp, D. J. (2001). An inducible 1-butanol dehydrogenase, a quinohaemoprotein, is involved in the oxidation of butane by 'Pseudomonas butanovora'. Microbiology 147: 745-756 [Abstract] [Full Text]