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Literature summary for 1.14.13.25 extracted from

  • Shinohara, Y.; Uchiyama, H.; Yagi, O.; Kusakabe, I.
    Purification and characterization of component B of a soluble methane monooxygenase from Methylocystis sp. M (1998), J. Ferment. Bioeng., 85, 37-42.
No PubMed abstract available
Search for more literature for 1.14.13.25

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Iron component B of sMMO Methylocystis sp.
additional information sMMO contains no metal ions 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.
15100
-
 component B: 2 * 15100, SDS-PAGE Methylocystis sp.
32000
-
 component B Methylocystis sp.

Organism

Organism UniProt Comment Textmining
Methylocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
component B of sMMO Methylocystis sp.

Subunits

Subunits Comment Organism
?
-
 Methylocystis sp.
dimer component B: 2 * 15100, SDS-PAGE Methylocystis sp.
More sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase Methylocystis sp.

Synonyms

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 N-terminal truncated sMMO component B increases the heat stability of the sMMO hydroxylase Methylocystis sp.

Cofactor

Cofactor Comment Organism Structure
additional information component B has no prosthetic group Methylocystis sp.