Methane monooxygenase (particulate)

Methane monooxygenase (particulate)
Methane monooxygenase (particulate)
	Particulate methane monooxygenase hexa-heterotrimer, Methylococcus capsulatus
Identifiers
EC no.	1.14.18.3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Methane monooxygenase (particulate) (EC 1.14.18.3) is an enzyme with systematic name methane,quinol:oxygen oxidoreductase.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

\rightleftharpoons

Methane monooxygenase contains copper. It is membrane-bound enzyme present in methanotrophs.

References

^ Shiemke AK, Cook SA, Miley T, Singleton P (August 1995). "Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors". Archives of Biochemistry and Biophysics. 321 (2): 421–8. doi:10.1006/abbi.1995.1413. PMID 7646068.
^ Basu P, Katterle B, Andersson KK, Dalton H (January 2003). "The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein". The Biochemical Journal. 369 (Pt 2): 417–27. doi:10.1042/BJ20020823. PMC 1223091. PMID 12379148.
^ Kitmitto A, Myronova N, Basu P, Dalton H (August 2005). "Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)". Biochemistry. 44 (33): 10954–65. doi:10.1021/bi050820u. PMID 16101279.
^ Balasubramanian R, Rosenzweig AC (July 2007). "Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase". Accounts of Chemical Research. 40 (7): 573–80. doi:10.1021/ar700004s. PMID 17444606.

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron–sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)