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Literature summary for 1.14.13.25 extracted from

  • Grosse, S.; Laramee, L.; Wendlandt, K.D.; McDonald, I.R.; Miguez, C.B.; Kleber, H.P.
    Purification and characterization of the soluble methane monooxygenase of the type II methanotrophic bacterium Methylocystis sp. strain WI 14 (1999), Appl. Environ. Microbiol., 65, 3929-3935.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.25

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, determination of complete sMMO DNA gene sequence, phylogenetic analysis Methylocystis sp.

General Stability

General Stability Organism
Fe2+ stabilizes component C of sMMO Methylocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
Co2+ slightly, sMMO Methylocystis sp.
Cu2+ causes protein aggregation Methylocystis sp.
Hg2+ complete inhibition at 0.01 mM Methylocystis sp.
Ni2+ causes protein aggregation; sMMO Methylocystis sp.
Zn2+ causes protein aggregation; sMMO Methylocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0064
-
 NADH sMMO component C reductase Methylocystis sp.
5.2
-
 NADPH sMMO component C reductase Methylocystis sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm enzyme from cells grown under conditions of low copper availability Methylocystis sp. 5737
-
cytoplasm cytoplasmatic, soluble enzyme form termed sMMO Methylocystis sp. 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron 3.6 mol of iron per mol of hydroxylase component A Methylocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase Methylocystis sp.
18000
-
 component protein B of sMMO Methylocystis sp.
23000
-
 component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE Methylocystis sp.
41000
-
 component C reductase of sMMO Methylocystis sp.
43000
-
 component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE Methylocystis sp.
57000
-
 component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE Methylocystis sp.
229000
-
 component A hydroxylase of sMMO Methylocystis sp.

Organism

Organism UniProt Comment Textmining
Methylocystis sp.
-
-
-
Methylocystis sp.
-
 enzyme form sMMO
-
Methylocystis sp.
-
 methanotroph type II
-
Methylocystis sp. WI 14
-
-
-

Purification (Commentary)

Purification (Comment) Organism
sMMO with all components Methylocystis sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 component protein B is involved in enzyme regulation and enhances the activity 10fold Methylocystis sp.
0.0008
-
 sMMO, substrate chloronaphthalene Methylocystis sp.
0.0012
-
 sMMO, substrate naphthalene Methylocystis sp.
0.0039
-
 sMMO, substrate chloropentane Methylocystis sp.
0.0122
-
 sMMO, low copper growth concentration, growth substrate nitrate Methylocystis sp.
0.0191
-
 sMMO, substrate butylene Methylocystis sp.
0.0254
-
 sMMO, substrate propylene Methylocystis sp.
0.0336
-
 sMMO, substrate ethylene Methylocystis sp.
0.205
-
 sMMO, substrate diethylic ether Methylocystis sp.
0.334
-
 sMMO, substrate propane Methylocystis sp.

Storage Stability

Storage Stability Organism
4°C, sMMO component C reductase, 90% loss of activity after 120 h, can be restored by Fe2+ Methylocystis sp.
sMMO component A hydroxylase is very unstable, splits into inactive subunits when stored frozen even for short periods Methylocystis sp.
sMMO component protein B is stable when stored frozen Methylocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzene + NAD(P)H + H+ + O2
-
 Methylocystis sp. phenol + NAD(P)+ + H2O
-
 ?
bromobenzene + NAD(P)H + O2 sMMO Methylocystis sp. bromophenol + NAD(P)+ + H2O
-
 ?
butane + NAD(P)H + O2
-
 Methylocystis sp. 1-butanol + 2-butanol + NAD(P)+ + H2O only 2-butanol, sMMO ?
butylene + NAD(P)H + O2 sMMO Methylocystis sp. butylene oxide + NAD(P)+ + H2O
-
 ?
chlorobenzene + NAD(P)H + O2 sMMO Methylocystis sp. chlorophenol + NAD(P)+ + H2O
-
 ?
chloronaphthalene + NAD(P)H + O2 sMMO Methylocystis sp. chloronaphthol + NAD(P)+ + H2O
-
 ?
chloropentane + NAD(P)H + O2 sMMO Methylocystis sp. chloropentanol + NAD(P)+ + H2O
-
 ?
cyclohexane + NAD(P)H + O2 sMMO Methylocystis sp. cyclohexanol + NAD(P)+ + H2O
-
 ?
cytochrome c + NAD(P)H + O2 sMMO Methylocystis sp. reduced cytochrome c + NAD(P)+ + H2O
-
 ?
diethyl ether + NAD(P)H + O2 sMMO Methylocystis sp. ethanol + ethanal + NAD(P)+ + H2O
-
 ?
diethyl ether + NAD(P)H + O2 sMMO Methylocystis sp. WI 14 ethanol + ethanal + NAD(P)+ + H2O
-
 ?
ethene + NAD(P)H + O2 sMMO Methylocystis sp. epoxyethane + NAD(P)+ + H2O
-
 ?
ethene + NAD(P)H + O2 sMMO Methylocystis sp. WI 14 epoxyethane + NAD(P)+ + H2O
-
 ?
fluorobenzene + NAD(P)H + O2 sMMO Methylocystis sp. fluorophenol + NAD(P)+ + H2O
-
 ?
heptane + NAD(P)H + O2 sMMO Methylocystis sp. 1-heptanol + 2-heptanol + NAD(P)+ + H2O position of hydroxylation cannot be determined exactly ?
hexane + NAD(P)H + O2 sMMO Methylocystis sp. 1-hexanol + 2-hexanol + NAD(P)+ + H2O position of hydroxylation cannot be determined exactly ?
methane + NAD(P)H + O2
-
 Methylocystis sp. methanol + NAD(P)+ + H2O
-
 ?
methane + NAD(P)H + O2
-
 Methylocystis sp. WI 14 methanol + NAD(P)+ + H2O
-
 ?
methane + NADH + H+ + O2
-
 Methylocystis sp. methanol + NAD+ + H2O
-
 ?
additional information sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity Methylocystis sp. ?
-
 ?
additional information sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity Methylocystis sp. WI 14 ?
-
 ?
naphthalene + NAD(P)H + O2 sMMO Methylocystis sp. alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
 ?
pentane + NAD(P)H + O2 sMMO Methylocystis sp. 1-pentanol + 2-pentanol + NAD(P)+ + H2O position of hydroxylation cannot be determined exactly ?
propane + NAD(P)H + O2
-
 Methylocystis sp. 1-propanol + 2-propanol + NAD(P)+ + H2O only 2-propanol, sMMO ?
propane + NAD(P)H + O2
-
 Methylocystis sp. WI 14 1-propanol + 2-propanol + NAD(P)+ + H2O only 2-propanol, sMMO ?
propylene + NAD(P)H + O2 enzyme form sMMO Methylocystis sp. propylene oxide + NADP+ + H2O
-
 ?
toluene + NAD(P)H + H+ + O2 sMMO Methylocystis sp. cresol + NAD(P)+ + H2O
-
 ?
xylene + NAD(P)H + O2 sMMO Methylocystis sp. xylenol + NAD(P)+ + H2O
-
 ?

Subunits

Subunits Comment Organism
? component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE Methylocystis sp.

Synonyms

Synonyms Comment Organism
pMMO particulate, membrane-bound enzyme form Methylocystis sp.
sMMO soluble, cytoplasmic enzyme form Methylocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Methylocystis sp.

Cofactor

Cofactor Comment Organism Structure
NADH in vivo only NADH can be the electron donor Methylocystis sp.
NADPH only in vitro Methylocystis sp.