Biological Nitrogen Removal Database
A manually curated data resource for microbial nitrogen removal
Biological Nitrogen Removal Database
A manually curated data resource for microbial nitrogen removal
| Enzyme name | particulate methane monooxygenase |
| Synonyms | methane monooxygenase (particulate); copper-containing membrane monooxygenase; CuMMO; particulate methane mono-oxygenase; particulate methane monooxygenase A; pMMO hydroxylase; pMMO-H; membrane-associated methane monooxygenase; copper-containing membrane-bound monooxygenase |
| Gene cluster | pmoCAB |
| Classification | Oxidoreductases |
| Genes | pmoA; pmoB; pmoC |
| Pathway | Nitrogen metabolism: nitrite-dependent anaerobic methane oxidation (N-DAMO): Methane hydroxylation to methanol |
| Substrate | methane; quinol; oxygen |
| Product | methanol; quinone; water |
| Mechanism | Link |
| Subunit | |
| Gene Protein name Organism Status Accession Number (Genbank) Accession Number (GenPept) Accession Number (UniProt) |
pmoA Particulate methane monooxygenase alpha subunit Methylococcus capsulatus str. Bath Reviewed L40804 AAB49820.1 G1UBD1 |
| Gene Protein name Organism Status Accession Number (Genbank) Accession Number (GenPept) Accession Number (UniProt) |
pmoB Particulate methane monooxygenase beta subunit Methylococcus capsulatus str. Bath Reviewed L40804 AAB49821.1 Q607G3 |
| Gene Protein name Organism Status Accession Number (Genbank) Accession Number (GenPept) Accession Number (UniProt) |
pmoC Particulate methane monooxygenase, C subunit Methylococcus capsulatus str. Bath Unreviewed L40804 AAB49820.1 P97047 |
| Reference | |
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Authors Title PubMed ID Full research link |
Ward et al., 2004 Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath) |
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Authors Title PubMed ID Full research link |
Chistoserdova et al., 2005 A genomic view of methane oxidation by aerobic bacteria and anaerobic archaea |
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Authors Title PubMed ID Full research link |
Nguyen et al., 1998 The particulate methane monooxygenase from methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization |
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Authors Title PubMed ID Full research link |
Lieberman and Rosenzweig. 2005 Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane |
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Authors Title PubMed ID Full research link |
Semrau et al., 1995 Particulate methane monooxygenase genes in methanotrophs |
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Authors Title PubMed ID Full research link |
Kitmitto et al., 2005 Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath) |