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MetaCyc Pathway: formaldehyde oxidation IV (thiol-independent)
Inferred from experiment

Pathway diagram: formaldehyde oxidation IV (thiol-independent)

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/AssimilationC1 Compounds Utilization and AssimilationFormaldehyde Oxidation

Some taxa known to possess this pathway include : Pseudomonas putida

Expected Taxonomic Range: Proteobacteria

General Background

The detoxification of the highly toxic formaldehyde is a major biochemical necessity for most life forms. In the case of methylotrophic bacteria, formaldehyde is not just a toxic compound, but also a central intermediate. It has been suggested that the formaldehyde concentration in the cytoplasm of a methylotroph would rise to 100mM in less than 1 minute if formaldehyde consumption would stop [Vorholt00]. Several different pathways for Formaldehyde Oxidation are known in bacteria, encoded by unrelated or distantly related genes.

About This Pathway

This pathway involves a formaldehyde dehydrogenase that does not require a thiol cofactor for its activity. This enzyme has been purified from Pseudomonas putida [Tanaka02], and homologs of this enzyme were found in the genomes of several organisms [Speer94].

Superpathways: superpathway of C1 compounds oxidation to CO2

Variants: formaldehyde oxidation I, formaldehyde oxidation II (glutathione-dependent), formaldehyde oxidation III (mycothiol-dependent), formaldehyde oxidation V (H4MPT pathway)

Created 28-Aug-2003 by Arnaud M, SRI International
Revised 11-Jul-2004 by Caspi R, SRI International


Hanson96: Hanson, RS, Hanson, ET "Methanotrophic bacteria." Microbiological Reviews(1996) 60(2):439-471.

Speer94: Speer BS, Chistoserdova L, Lidstrom ME (1994). "Sequence of the gene for a NAD(P)-dependent formaldehyde dehydrogenase (class III alcohol dehydrogenase) from a marine methanotroph Methylobacter marinus A45." FEMS Microbiol Lett 121(3);349-55. PMID: 7926692

Tanaka02: Tanaka N, Kusakabe Y, Ito K, Yoshimoto T, Nakamura KT (2002). "Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases." J Mol Biol 324(3);519-33. PMID: 12445786

Vorholt00: Vorholt JA, Marx CJ, Lidstrom ME, Thauer RK (2000). "Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1 required for growth on methanol." J Bacteriol 182(23);6645-50. PMID: 11073907

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Ando79: Ando M, Yoshimoto T, Ogushi S, Rikitake K, Shibata S, Tsuru D (1979). "Formaldehyde dehydrogenase from Pseudomonas putida. Purification and some properties." J Biochem (Tokyo) 85(5);1165-72. PMID: 571868

Ito94: Ito K, Takahashi M, Yoshimoto T, Tsuru D (1994). "Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida." J Bacteriol 176(9);2483-91. PMID: 8169197

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lessmeier13: Lessmeier L, Hoefener M, Wendisch VF (2013). "Formaldehyde degradation in Corynebacterium glutamicum involves acetaldehyde dehydrogenase and mycothiol-dependent formaldehyde dehydrogenase." Microbiology 159(Pt 12);2651-62. PMID: 24065717

Ogushi84: Ogushi S, Ando M, Tsuru D (1984). "Formaldehyde dehydrogenase from Pseudomonas putida: a zinc metalloenzyme." J Biochem (Tokyo) 96(5);1587-91. PMID: 6526822

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue May 3, 2016, biocyc13.