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Literature summary for 1.14.13.25 extracted from

  • Ross, M.O.; Rosenzweig, A.C.
    A tale of two methane monooxygenases (2017), J. Biol. Inorg. Chem., 22, 307-319 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.25

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme sMMO crystal structure analysis, PDB ID 1MTY Methylococcus capsulatus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Methylococcus capsulatus 5737
-
soluble
-
 Methylococcus capsulatus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme sMMO contains a non-heme diiron active site Methylococcus capsulatus
Iron the diiron active site of each homodimer is located in the alpha subunit, and no other metal centers are present. The resting state active site (MMOHox) consists of two Fe(III) ions coordinated by Glu114, His147, and a solvent molecule (Fe1), and Glu209, Glu243, and His246 (Fe2). The iron ions are 3.1 A apart, coordinated in pseudooctahedral fashion and bridged by two solvent molecules as well as Glu144 Methylococcus capsulatus
additional information the enzyme does not contain and require Cu2+ for activity Methylococcus capsulatus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
251000
-
-
 Methylococcus capsulatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methane + NADH + H+ + O2 Methylococcus capsulatus
-
 methanol + NAD+ + H2O
-
 ?
methane + NADH + H+ + O2 Methylococcus capsulatus Bath
-
 methanol + NAD+ + H2O
-
 ?
methane + NADH + H+ + O2 Methylococcus capsulatus Bath.
-
 methanol + NAD+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
-
-
-
Methylococcus capsulatus P22869 and P18798 and P11987 and P18797 and P22868 and P22867 P22869 (MmoX), P18798 (MmoY), P11987 (MmoZ), P18797 (MmoB), P22868 (MmoC), P22867 (MmoD). The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD)
-
Methylococcus capsulatus Bath
-
-
-
Methylococcus capsulatus Bath. P22869 and P18798 and P11987 and P18797 and P22868 and P22867 P22869 (MmoX), P18798 (MmoY), P11987 (MmoZ), P18797 (MmoB), P22868 (MmoC), P22867 (MmoD). The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD)
-

Reaction

Reaction Comment Organism Reaction ID
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O reaction mechanism and reaction cycle of enzyme sMMO, via O2 activation intermediates, detailed overview Methylococcus capsulatus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + NAD(P)H + H+ + O2
-
 Methylococcus capsulatus methanol + NAD(P)+ + H2O
-
 ?
methane + NAD(P)H + H+ + O2
-
 Methylococcus capsulatus Bath. methanol + NAD(P)+ + H2O
-
 ?
methane + NADH + H+ + O2
-
 Methylococcus capsulatus methanol + NAD+ + H2O
-
 ?
methane + NADH + H+ + O2
-
 Methylococcus capsulatus Bath methanol + NAD+ + H2O
-
 ?
methane + NADH + H+ + O2
-
 Methylococcus capsulatus Bath. methanol + NAD+ + H2O
-
 ?

Subunits

Subunits Comment Organism
More enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview Methylococcus capsulatus

Synonyms

Synonyms Comment Organism
sMMO
-
 Methylococcus capsulatus
soluble methane monooxygenase
-
 Methylococcus capsulatus

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Methylococcus capsulatus

General Information

General Information Comment Organism
evolution methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. Enzyme sMMO belongs to the larger bacterial multicomponent monooxygenase (BMM) family. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available Methylococcus capsulatus
additional information enzyme sMMO contains a non-heme diiron active site, active site structure, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview Methylococcus capsulatus