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Literature summary for 1.5.3.1 extracted from

  • Saito, M.; Itoh, A.; Suzuki, H.
    Deuterium kinetic isotope effects in heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96: the anionic form of the substrate in the enzyme-substrate complex is a reactive species (2012), J. Biochem., 151, 633-642.
    View publication on PubMed
Search for more literature for 1.5.3.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics relative to pH, stopped-flow spectroscopy Corynebacterium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Corynebacterium sp. heterotetrameric sarcosine oxidase is a flavoprotein that catalyses the oxidative demethylation of sarcosine to generate glycine, hydrogen peroxide and formaldehyde or 5,10-methylenetetrahydrofolate, depending on the availability of tetrahydrofolate. The amine proton of sarcosine is transferred to the unprotonated Lys residue in the enzyme-substrate complex ?
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information heterotetrameric sarcosine oxidase is a flavoprotein that catalyses the oxidative demethylation of sarcosine to generate glycine, hydrogen peroxide and formaldehyde or 5,10-methylenetetrahydrofolate, depending on the availability of tetrahydrofolate. The amine proton of sarcosine is transferred to the unprotonated Lys residue in the enzyme-substrate complex Corynebacterium sp. ?
-
 ?

Subunits

Subunits Comment Organism
heterotetramer
-
 Corynebacterium sp.

Synonyms

Synonyms Comment Organism
SO-U96
-
 Corynebacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9
-
 Corynebacterium sp.

pH Range

pH Minimum pH Maximum Comment Organism
5.8 10.5 activity range Corynebacterium sp.

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein, rate of FAD reduction, overview. Reduction of the bound FAD cofactor occurs, the electron transfers from the reduced FAD to the bound FMN cofactor, then the oxidized FAD is reduced again following EoxS complex formation Corynebacterium sp.
FMN flavoprotein, overview. Reduction of the bound FAD cofactor occurs, the electron transfers from the reduced FAD to the bound FMN cofactor, then the oxidized FAD is reduced again following EoxS complex formation Corynebacterium sp.