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sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
mechanism
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
mechanism
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
mechanism
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
ping-pong bi-bi mechanism
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
modified ping-pong-mechanism in which oxygen reacts with EredP prior to the dissociation of the imino acid product
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
enzyme forms a charge-transfer Michaelis complex with sarcosine, kinetics of formation of the Michaelis charge transfer complex can be directly monitored at 5°C. No redox intermediate is detectable during sarcosine oxidation
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
L-proline is the ionizable group in the ES complex. Y317 may play a role in substrate activation and optimizing of binding
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
mechanism suggested
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
mechanism suggested
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
mechanism suggested
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
molecular dynamics investigation by random acceleration molecular dynamics simulations with an ensemble made of the bacterial monomeric sarcosine oxidase (2GF3), O2, and the inhibitor furoic acid to mimic sarcosine
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
molecular dynamics simulation study for the heterotetrameric sarcosine oxidase-dimethylglycine complex gives insight to understand the dynamics of the enzyme. A cluster analysis on the small rectangular cells with high water probabilities results in the detection of eleven water channels. CH1, CH2, CH3, and CH4 correspond to the tunnels from the large cavity in the previous study. CH6, CH7, and the combined CH8 and CH9 are narrow channels from the large cavity. CH5 and the combined CH10 and CH11 are not connected with the cavity. No permeation of water molecules between the channels is found except in the combined channels. The results of the present analysis are consistent with the selective transport hypothesis
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
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
-
sarcosine + H2O + O2 = glycine + formaldehyde + H2O2
-
-
-
-
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2-isopropyl-4-(methylaminomethyl)thiazole + O2 + H2O
formaldehyde + 2-isopropyl-4-(aminomethyl)thiazole + H2O2
4-(ethylaminomethyl)pyridine + O2 + H2O
acetaldehyde + 4-(aminomethyl) pyridine + H2O2
L-proline + O2 + H2O
?
-
less than 1% the rate of sarcosine
-
-
r
L-proline + O2 + H2O
? + H2O2
-
-
-
?
N-ethylglycine + O2 + H2O
acetaldehyde + glycine + H2O2
-
-
-
-
?
N-methyl-D-proline + O2 + H2O
formaldehyde + D-proline + H2O2
-
-
-
?
N-methyl-DL-alanine + O2 + H2O
formaldehyde + DL-alanine + H2O2
N-methyl-DL-valine + O2 + H2O
formaldehyde + DL-valine + H2O2
N-methyl-L-alanine + O2 + H2O
formaldehyde + L-alanine + H2O2
N-methyl-L-aspartate + O2 + H2O
formaldehyde + L-aspartate + H2O2
-
-
-
?
N-methyl-L-leucine + O2 + H2O
formaldehyde + L-leucine + H2O2
N-methyl-L-phenylalanine + O2 + H2O
formaldehyde + L-phenylalanine + H2O2
-
-
-
?
N-methyl-L-tryptophan + O2 + H2O
formaldehyde + L-tryptophan + H2O2
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + formaldehyde + H2O2
sarcosine + H2O + 2,6-dichlorophenolindophenol
glycine + formaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
sarcosine + H2O + phenazine methosulfate
glycine + formaldehyde + reduced phenazine methosulfate
-
-
-
-
r
sarcosine + H2O + potassium ferricyanide
glycine + formaldehyde + potassium ferrocyanide
-
-
-
-
r
sarcosine + H2O2 + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + O2 + H2O
formaldehyde + glycine + H2O2
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
additional information
?
-
2-isopropyl-4-(methylaminomethyl)thiazole + O2 + H2O
formaldehyde + 2-isopropyl-4-(aminomethyl)thiazole + H2O2
-
-
-
?
2-isopropyl-4-(methylaminomethyl)thiazole + O2 + H2O
formaldehyde + 2-isopropyl-4-(aminomethyl)thiazole + H2O2
-
-
-
?
4-(ethylaminomethyl)pyridine + O2 + H2O
acetaldehyde + 4-(aminomethyl) pyridine + H2O2
-
-
-
?
4-(ethylaminomethyl)pyridine + O2 + H2O
acetaldehyde + 4-(aminomethyl) pyridine + H2O2
-
-
-
?
N-methyl-DL-alanine + O2 + H2O
formaldehyde + DL-alanine + H2O2
-
-
-
-
?
N-methyl-DL-alanine + O2 + H2O
formaldehyde + DL-alanine + H2O2
-
-
-
-
?
N-methyl-DL-alanine + O2 + H2O
formaldehyde + DL-alanine + H2O2
-
-
-
-
?
N-methyl-DL-alanine + O2 + H2O
formaldehyde + DL-alanine + H2O2
-
-
-
-
?
N-methyl-DL-alanine + O2 + H2O
formaldehyde + DL-alanine + H2O2
-
-
-
-
?
N-methyl-DL-alanine + O2 + H2O
formaldehyde + DL-alanine + H2O2
-
-
-
-
?
N-methyl-DL-alanine + O2 + H2O
formaldehyde + DL-alanine + H2O2
-
-
-
-
?
N-methyl-DL-valine + O2 + H2O
formaldehyde + DL-valine + H2O2
-
-
-
-
?
N-methyl-DL-valine + O2 + H2O
formaldehyde + DL-valine + H2O2
-
-
-
-
?
N-methyl-DL-valine + O2 + H2O
formaldehyde + DL-valine + H2O2
-
-
-
-
?
N-methyl-DL-valine + O2 + H2O
formaldehyde + DL-valine + H2O2
-
-
-
-
?
N-methyl-L-alanine + O2 + H2O
formaldehyde + L-alanine + H2O2
-
-
-
-
r
N-methyl-L-alanine + O2 + H2O
formaldehyde + L-alanine + H2O2
-
-
-
?
N-methyl-L-alanine + O2 + H2O
formaldehyde + L-alanine + H2O2
-
-
-
?
N-methyl-L-leucine + O2 + H2O
formaldehyde + L-leucine + H2O2
-
-
-
-
?
N-methyl-L-leucine + O2 + H2O
formaldehyde + L-leucine + H2O2
-
-
-
-
?
N-methyl-L-leucine + O2 + H2O
formaldehyde + L-leucine + H2O2
-
-
-
-
?
N-methyl-L-leucine + O2 + H2O
formaldehyde + L-leucine + H2O2
-
-
-
-
?
N-methyl-L-leucine + O2 + H2O
formaldehyde + L-leucine + H2O2
-
-
-
?
N-methyl-L-leucine + O2 + H2O
formaldehyde + L-leucine + H2O2
-
-
-
?
N-methyl-L-tryptophan + O2 + H2O
formaldehyde + L-tryptophan + H2O2
-
-
-
?
N-methyl-L-tryptophan + O2 + H2O
formaldehyde + L-tryptophan + H2O2
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + H2O + O2
?
-
involved in creatinine catabolism
-
-
?
sarcosine + H2O + O2
?
-
involved in creatinine catabolism
-
-
?
sarcosine + H2O + O2
?
-
involved in creatinine catabolism
-
-
?
sarcosine + H2O + O2
?
-
sarcosine degradation when sarcosine is sole source of carbon, nitrogen and energy
-
-
?
sarcosine + H2O + O2
?
-
involved in glyphosate catabolism
-
-
?
sarcosine + H2O + O2
?
-
involved in creatinine catabolism
-
-
?
sarcosine + H2O + O2
?
-
involved in creatinine catabolism
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
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
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
molecular dynamics investigation by random acceleration molecular dynamics simulations with an ensemble made of the bacterial monomeric sarcosine oxidase (2GF3), O2, and the inhibitor furoic acid to mimic sarcosine. The ensemble is solvated by in a periodic box, while an external tiny force acts randomly to expel O2 from the center of activation, located between residue K265 and the si face of the flavin ring of the flavin adenine dinucleotide cofactor, moving it toward the solvent
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
formaldehyde + glycine + H2O2
-
-
-
-
?
sarcosine + O2 + H2O
formaldehyde + glycine + H2O2
-
-
-
?
sarcosine + O2 + H2O
formaldehyde + glycine + H2O2
-
-
-
-
?
sarcosine + O2 + H2O
formaldehyde + glycine + H2O2
-
-
-
?
sarcosine + O2 + H2O
formaldehyde + glycine + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
glycine + formaldehyde + H2O2
-
-
-
?
additional information
?
-
-
betaine
-
-
?
additional information
?
-
-
dimethylglycine
-
-
?
additional information
?
-
-
not: beta-alanine, N-methylalanine, 1,3-dimethylurea, 1-methylguanidine, methoxyacetate, creatine, creatinine
-
-
?
additional information
?
-
also oxidizes other amino acids containing a secondary amino group e.g. L-proline, and N-methyl-L-alanine
-
-
?
additional information
?
-
-
not: beta-alanine, N-methylalanine, 1,3-dimethylurea, 1-methylguanidine, methoxyacetate, creatine, creatinine
-
-
?
additional information
?
-
-
flavin and cytochromes of the c and b or o type function as electron carriers
-
-
?
additional information
?
-
-
very specific for oxygen as acceptor, oxygen can be replaced by 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide, much smaller Vmax/Km values than for O2
-
-
?
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
-
-
?
additional information
?
-
-
no substrate: choline,betaine, dimethylglycine and N-methyl amino acids
-
-
?
additional information
?
-
-
no substrate: choline,betaine, dimethylglycine and N-methyl amino acids
-
-
?
additional information
?
-
-
the alpha subunit shows sarcosine oxidase and L-proline dehydrogenase activity, while the beta subunit displays both sarcosine oxidase and L-proline dehydrogenase activity, but not NADH dehydrogenase activity, measurement of L-proline dehydrogenase activity with 2,6-dichloroindophenol as cofactor. Dye-linked NADH dehydrogenase activity is assayed with NADH, FAD and 2,6-dichloroindophenol
-
-
?
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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
-
-
FAD
-
noncovalently bound
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
-
covalent and non-covalent
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 beta subunit contains FAD
FAD
-
the enzyme contains two mol FAD per mol enzyme (one covalently-bound and one none-covalently-bound)
flavin
-
-
flavin
-
associated with 45000 Da subunit
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
flavin
-
flavoenzyme with noncovalently bound flavin
FMN
-
-
FMN
-
1 molecle covalently bound to the tetrameric 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
FMN
-
the beta subunit contains FMN
NAD+
-
-
NAD+
-
1 mol of noncovalently bound NAD+ per mol of enzyme
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
NAD+
-
the alpha subunit contains NAD+
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1.5.3.1 sarcosine oxidase (formaldehyde-forming)
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