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Literature summary for 1.14.13.25 extracted from

  • Merkx, M.; Lippard, S.J.
    Why orfY? Characterization of MMOD, a long overlooked component of the soluble methane monooxygenase from Methylococcus capsulatus (Bath) (2002), J. Biol. Chem., 277, 5858-5865.
    View publication on PubMed
Search for more literature for 1.14.13.25

Cloned(Commentary)

Cloned (Comment) Organism
DNA sequence analysis Methylococcus capsulatus
overexpression of an additional protein component D of sMMO encoded by orfY as thioredoxin-fusion protein with His-Tag in Escherichia coli, protein component D is termed MMOD Methylococcus capsulatus

General Stability

General Stability Organism
sMMO is more stable and easier to purify than pMMO Methylococcus capsulatus

Inhibitors

Inhibitors Comment Organism Structure
additional information sMMO is completely inhibited by monomeric component D, but not by dimeric, monomeric MMOD is interfering with the catalytically active complex between component A hydroxylase and component protein B Methylococcus capsulatus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm cytoplasmatic, soluble enzyme form termed sMMO Methylococcus capsulatus 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
12000
-
 component D of sMMO: 2 * 12000, SDS-PAGE Methylococcus capsulatus
24000
-
 component D of sMMO, forms homodimers, gel filtration Methylococcus capsulatus

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
-
 Bath
-
Methylococcus capsulatus Bath
-
 Bath
-

Purification (Commentary)

Purification (Comment) Organism
component D of sMMO recombinant from Escherichia coli as His-tagged thioredoxin-fusion protein, the thioredoxin is cleaved off during purification by factor Xa Methylococcus capsulatus

Reaction

Reaction Comment Organism Reaction ID
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O modeling of interaction between the different protein components of sMMO Methylococcus capsulatus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + NAD(P)H + O2
-
 Methylococcus capsulatus methanol + NAD(P)+ + H2O
-
 ?
methane + NAD(P)H + O2
-
 Methylococcus capsulatus Bath methanol + NAD(P)+ + H2O
-
 ?
propylene + NAD(P)H + O2 enzyme form sMMO Methylococcus capsulatus propylene oxide + NADP+ + H2O
-
 ?
propylene + NAD(P)H + O2 enzyme form sMMO Methylococcus capsulatus Bath propylene oxide + NADP+ + H2O
-
 ?

Subunits

Subunits Comment Organism
?
-
 Methylococcus capsulatus
dimer component D of sMMO: 2 * 12000, SDS-PAGE Methylococcus capsulatus
More sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D Methylococcus capsulatus

Synonyms

Synonyms Comment Organism
MMO
-
 Methylococcus capsulatus
pMMO particulate, membrane-bound enzyme form Methylococcus capsulatus
sMMO soluble, cytoplasmic enzyme form Methylococcus capsulatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Methylococcus capsulatus
25
-
 enzyme form sMMO Methylococcus capsulatus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Methylococcus capsulatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Methylococcus capsulatus
7
-
 enzyme form sMMO Methylococcus capsulatus

Cofactor

Cofactor Comment Organism Structure
FAD protein C, reductase component: contains 1 mol FAD per mol protein Methylococcus capsulatus
additional information component D contains no metal ions or organic cofactors Methylococcus capsulatus
NADH
-
 Methylococcus capsulatus