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Catalytic Site Atlas

CSA LITERATURE entry for 1mhy

E.C. namemethane monooxygenase (soluble)
SpeciesMethylosinus trichosporium ()
E.C. Number (IntEnz) 1.14.13.25
CSA Homologues of 1mhyThere are 27 Homologs
CSA Entries With UniProtID P27353
CSA Entries With EC Number 1.14.13.25
PDBe Entry 1mhy
PDBSum Entry 1mhy
MACiE Entry 1mhy

Literature Report

IntroductionMethyl monooxygenase (MMO) catalyses the conversion of methane to methanol coupled with reduction of oxygen and oxidation of NADH. Methanotrophic bacteria play an essential part in cycling carbon in the biosphere by consuming methane produced in anaerobic sediments and by limiting its flux to the atmosphere where it acts as a greenhouse gas. They have been used as a basis for biomimetic catalysts to convert methane in to the easily transportable liquid form of methanol for use as a fuel.
MechansimThe catalytic mechanism is likely similar to other members of this superfamily, binding of dioxygen by the di-iron centre and subsequent activation leading to hydroxylation of the methane. Cysteine 151 occupies the same position as the tyrosine in ribonucleotide reductase active site which suggests a redox role for the residue via hydrogen abstraction on methane. Threonine 213 occupies a position where it could supply protons needed during catalysis in analogy with a threonine in cytochrome P450.
Reaction

Catalytic Sites for 1mhy

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
CysD151151macie:sideChainRedox role via hydrogen abstraction.
ThrD213213macie:sideChainProton donor during catalysis.

Literature References

Notes:Not really enough information about this specific enzyme itself evidence based on homology.
Elango N
Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b.
Protein Sci 1997 6 556-568
PubMed: 9070438
Nordlund P
The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductase.
FEBS Lett 1992 307 257-262
PubMed: 1644180
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