1.5.3.1: sarcosine oxidase (formaldehyde-forming)
This is an abbreviated version!
For detailed information about sarcosine oxidase (formaldehyde-forming), go to the full flat file.
Word Map on EC 1.5.3.1
-
1.5.3.1
-
flavin
-
fad
-
heterotetrameric
-
n-methylglycine
-
creatininase
-
amidinohydrolase
-
n-methyltryptophan
-
corynebacterial
-
flavinylation
-
diagnostics
-
analysis
-
medicine
- 1.5.3.1
- flavin
- fad
-
heterotetrameric
- n-methylglycine
- creatininase
-
amidinohydrolase
- n-methyltryptophan
-
corynebacterial
-
flavinylation
- diagnostics
- analysis
- medicine
Reaction
Synonyms
heterotetrameric sarcosine oxidase, L-pipecolate oxidase, L-pipecolic acid oxidase, monomeric sarcosine oxidase, MSOX, PSO, sarcosine : oxygen oxidoreductase (demethylating), sarcosine oxidase, sarcosine: O2 oxidoreductase, sarcosine:oxygen oxidoreductase (demethylating), SO, SO-U96, SOX, SoxA, trd_1773, TSOX
ECTree
Advanced search results
Cofactor
Cofactor on EC 1.5.3.1 - sarcosine oxidase (formaldehyde-forming)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
additional information
reconstructed SOX with a ligand modified at the 7- or 8-position, i.e. by a halogen atom, shows significantly different Km, kcat, relative specificity, optimal reaction temperature, and pH adaptability values compared with refolded SOX-FAD
-
FAD
-
1 mol of covalently bound and 1 mol of noncovalently bound FAD per mol of enzyme
FAD
-
covalent flavin is 8alpha-(s-cysteinyl)FAD attached to Cys315
FAD
-
covalently bound to wild-type. Production of soluble apoenzyme lacking FAD by controlled expression in Escherichia coli. Reconstitution of enzyme by incubation with FAD. Autoflavinylation occurs in a reaction that proceeds via reduced flavin intermediate and requires only apoenzyme and FAD
FAD
wild-type enzyme, noncovalently bound, recombinant enzyme, covalently bound
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
FAD
-
flavoenzyme. The simulation method of Markovian milestoning molecular dynamics simulations is used to compute the entry and exit kinetics of O2 in the enzyme. The rate of flavin oxidation by O2 is likely not strongly limited by diffusion from the solvent to the active site. The predicted faster entry and slower exit of O2 for the bound state indicate a longer residence time within the enzyme, increasing the likelihood of collisions with the flavin isoalloxazine ring, a step required for reduction of molecular O2 and subsequent reoxidation of the flavin
FAD
flavoprotein. The flavin is both covalently and non-covalently bound in a molar ratio of 1:1
FAD
binds both FAD and FMN. Residue Phe 339 is the cofactor binding site
FAD
-
contains 1 mol of noncovalently bound Flavin and 1 mol of covalently bound flavin per mole of enzyme
FAD
-
the enzyme contains two mol FAD per mol enzyme (one covalently-bound and one none-covalently-bound)
flavin
-
1 mol of covalently bound FMN and 1 mol of noncovalently bound FAD per mol of enzyme
flavin
-
1 mol of covalently bound and 1 mol of noncovalently bound flavin per mol of enzyme
FMN
-
present as covalent adduct with sulfide, probably a 4alpha-sulfide adduct stabilized by nearby residues. Model of the adduct and proposed mechanism
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
FMN
binds both FAD and FMN. Residue Phe 339 is the cofactor binding site
NAD+
NAD+ is not involved in sarcosine oxidation or in redox equilibrium with the flavins. However, it has a critical effect on the folding and/or stability of the alpha subunit