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MetaCyc Chimeric Pathway: superpathway of C1 compounds oxidation to CO2

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/Assimilation C1 Compounds Utilization and Assimilation
Superpathways

Some taxa known to possess parts of the pathway include ? : Methylobacillus flagellatus , Methylobacterium extorquens AM1 , Methylobacterium organophilum , Methylococcus capsulatus , Methylomonas aminofaciens 77a , Methylophilus methylotrophus W3A1 , Methylosinus trichosporium , Paracoccus denitrificans

Expected Taxonomic Range: Bacteria

Note: This is a chimeric pathway, comprising reactions from multiple organisms, and typically will not occur in its entirety in a single organism. The taxa listed here are likely to catalyze only subsets of the reactions depicted in this pathway.

Summary:
Methylotrophic bacteria are aerobic bacteria that utilize one-carbon compounds more reduced than formate as sources of carbon and energy, and assimilate formaldehyde as a major source of cellular carbon [Hanson96]. Methylotrophic bacteria utilize a variety of different one-carbon compounds including methane (see methane oxidation to methanol I), methanol, methylated amines, halomethanes and methylated compounds containing sulfur.

The common product of these oxidation reactions is formaldehyde, which is either oxidized to CO2 via formate, or assimilated (see formaldehyde assimilation and formaldehyde oxidation pathways).

Please note: This superpathway integrates several base pathways that are found in different methylotrophic bacteria, for the purpose of displaying the different routes found in the biosphere in a single general diagram. There may be no single organism that possesses all of these pathways.

For more information about the pathways and enzymes shown in here, please see the individual pathways that make up this superpathway.

Subpathways: methane oxidation to methanol I , formate oxidation to CO2 , formaldehyde oxidation V (H4MPT pathway) , formaldehyde oxidation IV (thiol-independent) , formaldehyde oxidation II (glutathione-dependent) , methanol and methylamine oxidation to formaldehyde , methylamine degradation I , methanol oxidation to formaldehyde I

Credits:
Created 09-Sep-2004 by Caspi R , SRI International
Revised 21-Aug-2007 by Caspi R , SRI International


References

Hanson96: Hanson RS, Hanson TE (1996). "Methanotrophic bacteria." Microbiol Rev 60(2);439-71. PMID: 8801441

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

Acharya05: Acharya P, Goenrich M, Hagemeier CH, Demmer U, Vorholt JA, Thauer RK, Ermler U (2005). "How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1." J Biol Chem 280(14);13712-9. PMID: 15632161

Ambler89: Ambler RP, Tobari J (1989). "Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J." Biochem J 261(2);495-9. PMID: 2505762

Anderson88b: Anderson DJ, Lidstrom ME (1988). "The moxFG region encodes four polypeptides in the methanol-oxidizing bacterium Methylobacterium sp. strain AM1." J Bacteriol 170(5);2254-62. PMID: 3129405

Anderson90: Anderson DJ, Morris CJ, Nunn DN, Anthony C, Lidstrom ME (1990). "Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and moxJ genes involved in methanol oxidation." Gene 90(1);173-6. PMID: 2116368

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

Anthony86: Anthony C (1986). "Bacterial oxidation of methane and methanol." Adv Microb Physiol 27;113-210. PMID: 3020939

Anthony92: Anthony C (1992). "The structure of bacterial quinoprotein dehydrogenases." Int J Biochem 24(1);29-39. PMID: 1316294

Asano88: Asano Y, Sekigawa T, Inukai H, Nakazawa A (1988). "Purification and properties of formate dehydrogenase from Moraxella sp. strain C-1." J Bacteriol 170(7);3189-93. PMID: 3384805

Bamforth78: Bamforth CW, Quayle JR (1978). "Aerobic and anaerobic growth of Paracoccus denitrificans on methanol." Arch Microbiol 119(1);91-7. PMID: 718372

Barber96: Barber RD, Rott MA, Donohue TJ (1996). "Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides." J Bacteriol 178(5);1386-93. PMID: 8631716

Bastien89: Bastien, C, Machlin, S, Zhang, Y, Donaldson, K, Hanson, RS "Organization of genes required for the oxidation of methanol to formaldehyde in three type II methylotrophs." Appl. Environ. Microbiol. 1989 55:3124-3130.

BeardmoreGray82: Beardmore-Gray M, O'Keeffe DT, Anthony C (1982). "The autoreducible cytochromes c of the methylotrophs Methylophilus methylotrophus and Pseudomonas AM1." Biochem J 207(1);161-5. PMID: 6295363

Bowman95: Bowman JP, Sly LI, Stackebrandt E (1995). "The phylogenetic position of the family Methylococcaceae." Int J Syst Bacteriol 45(1);182-5. PMID: 7857800

Breitung90: Breitung J, Thauer RK (1990). "Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanosarcina barkeri. Identification of N5-formyltetrahydromethanopterin as the product." FEBS Lett 1990;275(1-2);226-30. PMID: 2261993

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Bystrykh93: Bystrykh LV, Vonck J, van Bruggen EF, van Beeumen J, Samyn B, Govorukhina NI, Arfman N, Duine JA, Dijkhuizen L (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." J Bacteriol 175(6);1814-22. PMID: 8449887

Chistoserdov92: Chistoserdov AY, Boyd J, Mathews FS, Lidstrom ME (1992). "The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans." Biochem Biophys Res Commun 184(3);1181-9. PMID: 1590782

Chistoserdov94: Chistoserdov AY, McIntire WS, Mathews FS, Lidstrom ME (1994). "Organization of the methylamine utilization (mau) genes in Methylophilus methylotrophus W3A1-NS." J Bacteriol 176(13);4073-80. PMID: 8021188

Chistoserdov94a: Chistoserdov AY, Chistoserdova LV, McIntire WS, Lidstrom ME (1994). "Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants." J Bacteriol 176(13);4052-65. PMID: 8021187

Chistoserdova03: Chistoserdova L, Chen SW, Lapidus A, Lidstrom ME (2003). "Methylotrophy in Methylobacterium extorquens AM1 from a genomic point of view." J Bacteriol 185(10);2980-7. PMID: 12730156

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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 SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, BIOCYC14B.