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Gene Review

PP_3839  -  alcohol dehydrogenase

Pseudomonas putida KT2440

Synonyms: adhA, adhP
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Disease relevance of PP_3839


High impact information on PP_3839


Chemical compound and disease context of PP_3839


Biological context of PP_3839

  • We have identified an alcohol dehydrogenase activity in Pseudomonas putida strains carrying the CAM-OCT degradative plasmid that were grown on octane [7].
  • Mutant isolation confirms the presence of an alcohol dehydrogenase locus on the OCT plasmid and indicated the presence of multiple alcohol and aldehyde dehydrogenase loci on the P. putida chromosome [11].
  • Analysis of P. putida KT2440 genome sequence data indicated the presence of two PQQ-linked alcohol dehydrogenase-encoding genes [12].
  • Five out of seven cysteine residues found in the enzyme were concluded to coordinate with an active site zinc (Cys-46) and structural zinc atoms (Cys-97, -100, -103, and -111) from the sequence comparison with other Zn-containing medium-chain alcohol dehydrogenase homologues [13].
  • The observed stereoselectivity of the side-chain hydroxylation process in P. putida UV4 was complicated by the action of an alcohol dehydrogenase enzyme in the organism which slowly leads to epimerisation of the initial (R)-alcohol bioproducts by dehydrogenation to the corresponding ketones followed by stereoselective reduction to the (S)-alcohols [14].

Associations of PP_3839 with chemical compounds


Analytical, diagnostic and therapeutic context of PP_3839

  • A DNA fragment, containing an alcohol dehydrogenase gene (adh1), was isolated using a combination of degenerate PCR and inverse PCR [10].
  • Transcription analysis using RT-PCR showed that adh1 is cotranscribed with the putative acyl-CoA synthetase and esterase genes during growth on OPEO(n) [10].


  1. Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase ADH-IIG from Pseudomonas putida HK5. Toyama, H., Chen, Z.W., Fukumoto, M., Adachi, O., Matsushita, K., Mathews, F.S. J. Mol. Biol. (2005) [Pubmed]
  2. Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase. Hirota-Mamoto, R., Nagai, R., Tachibana, S., Yasuda, M., Tani, A., Kimbara, K., Kawai, F. Microbiology (Reading, Engl.) (2006) [Pubmed]
  3. Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5. Matsushita, K., Yamashita, T., Aoki, N., Toyama, H., Adachi, O. Biochemistry (1999) [Pubmed]
  4. Proton transfer in benzyl alcohol dehydrogenase during catalysis: alternate proton-relay routes. Inoue, J., Tomioka, N., Itai, A., Harayama, S. Biochemistry (1998) [Pubmed]
  5. The aromatic alcohol dehydrogenases in Pseudomonas putida N.C.I.B. 9869 grown on 3,5-xylenol and p-cresol. Keat, M.J., Hopper, D.J. Biochem. J. (1978) [Pubmed]
  6. Regulation of membrane peptides by the Pseudomonas plasmid alk regulon. Benson, S., Oppici, M., Shapiro, J., Fennewald, M. J. Bacteriol. (1979) [Pubmed]
  7. Plasmid-determined alcohol dehydrogenase activity in alkane-utilizing strains of Pseudomonas putida. Benson, S., Shapiro, J. J. Bacteriol. (1976) [Pubmed]
  8. Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5. Chen, Z.W., Matsushita, K., Yamashita, T., Fujii, T.A., Toyama, H., Adachi, O., Bellamy, H.D., Mathews, F.S. Structure (Camb.) (2002) [Pubmed]
  9. Crystal structure of glutathione-independent formaldehyde dehydrogenase. Tanaka, N., Kusakabe, Y., Ito, K., Yoshimoto, T., Nakamura, K.T. Chem. Biol. Interact. (2003) [Pubmed]
  10. Isolation and Characterization of an Alcohol Dehydrogenase Gene from the Octylphenol Polyethoxylate Degrader Pseudomonas putida S-5. Tasaki, Y., Yoshikawa, H., Tamura, H. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  11. Regulation of alkane oxidation in Pseudomonas putida. Grund, A., Shapiro, J., Fennewald, M., Bacha, P., Leahy, J., Markbreiter, K., Nieder, M., Toepfer, M. J. Bacteriol. (1975) [Pubmed]
  12. Identification and characterization of the AgmR regulator of Pseudomonas putida: role in alcohol utilization. Vrionis, H.A., Daugulis, A.J., Kropinski, A.M. Appl. Microbiol. Biotechnol. (2002) [Pubmed]
  13. Glutathione-independent formaldehyde dehydrogenase from Pseudomons putida: survey of functional groups with special regard for cysteine residues. Tsuru, D., Oda, N., Matsuo, Y., Ishikawa, S., Ito, K., Yoshimoto, T. Biosci. Biotechnol. Biochem. (1997) [Pubmed]
  14. Biotransformation of substituted pyridines with dioxygenase-containing microorganisms. Garrett, M.D., Scott, R., Sheldrake, G.N., Dalton, H., Goode, P. Org. Biomol. Chem. (2006) [Pubmed]
  15. Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica. Van Ophem, P.W., Van Beeumen, J., Duine, J.A. Eur. J. Biochem. (1993) [Pubmed]
  16. Sequence of the gene for a NAD(P)-dependent formaldehyde dehydrogenase (class III alcohol dehydrogenase) from a marine methanotroph Methylobacter marinus A45. Speer, B.S., Chistoserdova, L., Lidstrom, M.E. FEMS Microbiol. Lett. (1994) [Pubmed]
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