Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.25 extracted from

  • Wang, W.; Lippard, S.J.
    Diiron oxidation state control of substrate access to the active site of soluble methane monooxygenase mediated by the regulatory component (2014), J. Am. Chem. Soc., 136, 2244-2247 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.25

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Iron non-heme diiron active site in the alpha-subunit. The regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tail not found in regulatory proteins of other bacterial multicomponent monooxygenases. This N-terminal tail is indispensable for proper function, yet its solution structure and role in catalysis remain elusive. The oxidation state of the hydroxylase component, MMOH, modulates the conformation of the N-terminal tail in the MMOH-2MMOB complex, which in turn facilitates catalysis. The N-terminal tail switches from a relaxed, flexible conformational state to an ordered state upon MMOH reduction from the diiron(III) to the diiron(II) state Methylococcus capsulatus

Organism

Organism UniProt Comment Textmining
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. 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)
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tail not found in regulatory proteins of other bacterial multicomponent monooxygenases. This N-terminal tail is indispensable for proper function, yet its solution structure and role in catalysis remain elusive. The oxidation state of the hydroxylase component, MMOH, modulates the conformation of the N-terminal tail in the MMOH-2MMOB complex, which in turn facilitates catalysis. The N-terminal tail switches from a relaxed, flexible conformational state to an ordered state upon MMOH reduction from the diiron(III) to the diiron(II) state Methylococcus capsulatus ?
-
 ?
additional information the regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tail not found in regulatory proteins of other bacterial multicomponent monooxygenases. This N-terminal tail is indispensable for proper function, yet its solution structure and role in catalysis remain elusive. The oxidation state of the hydroxylase component, MMOH, modulates the conformation of the N-terminal tail in the MMOH-2MMOB complex, which in turn facilitates catalysis. The N-terminal tail switches from a relaxed, flexible conformational state to an ordered state upon MMOH reduction from the diiron(III) to the diiron(II) state Methylococcus capsulatus Bath. ?
-
 ?

Synonyms

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