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Information on EC 1.5.3.1 - sarcosine oxidase (formaldehyde-forming)
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EC Tree
1.5.3.1 sarcosine oxidase (formaldehyde-forming)IUBMB Comments
The enzyme, reported from bacteria and fungi, catalyses the oxidative demethylation of sarcosine. It contains a FAD cofactor bound to an L-cysteine residue. cf. EC 1.5.3.24, sarcosine oxidase (5,10-methylenetetrahydrofolate-forming).
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Word Map
- 1.5.3.1
- flavin
- fad
-
heterotetrameric
- n-methylglycine
- creatininase
-
amidinohydrolase
- n-methyltryptophan
-
corynebacterial
-
flavinylation
- diagnostics
- analysis
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
sarcosine oxidase, monomeric sarcosine oxidase, l-pipecolic acid oxidase, heterotetrameric sarcosine oxidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
heterotetrameric sarcosine oxidase
L-pipecolate oxidase
-
-
-
-
L-pipecolic acid oxidase
-
-
-
-
monomeric sarcosine oxidase
MSOX
PSO
-
-
-
-
sarcosine oxidase
-
-
ambiguous
-
SOX
trd_1773
TSOX
MSOX
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
sarcosine:oxygen oxidoreductase (demethylating)
The enzyme, reported from bacteria and fungi, catalyses the oxidative demethylation of sarcosine. It contains a FAD cofactor bound to an L-cysteine residue. cf. EC 1.5.3.24, sarcosine oxidase (5,10-methylenetetrahydrofolate-forming).
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CAS REGISTRY NUMBER
COMMENTARY
9029-22-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-isopropyl-4-(methylaminomethyl)thiazole + O2 + H2O
formaldehyde + 2-isopropyl-4-(aminomethyl)thiazole + H2O2
L-proline + O2 + H2O
?
-
less than 1% the rate of sarcosine
-
-
r
N-methyl-D-proline + O2 + H2O
formaldehyde + D-proline + H2O2
-
-
-
?
N-methyl-L-aspartate + O2 + H2O
formaldehyde + L-aspartate + H2O2
-
-
-
?
N-methyl-L-phenylalanine + O2 + H2O
formaldehyde + L-phenylalanine + H2O2
-
-
-
?
sarcosine + H2O + 2,6-dichlorophenolindophenol
glycine + formaldehyde + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
sarcosine + H2O + phenazine methosulfate
glycine + formaldehyde + reduced phenazine methosulfate
-
-
-
-
r
sarcosine + H2O + potassium ferricyanide
glycine + formaldehyde + potassium ferrocyanide
-
-
-
-
r
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
Bacillus sp. (in: Bacteria) B-0618
-
-
-
-
?
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
Bacillus sp. (in: Bacteria) B-0618
-
-
-
-
?
N-methyl-DL-valine + O2 + H2O
formaldehyde + DL-valine + H2O2
-
-
-
-
?
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
Bacillus sp. (in: Bacteria) B-0618
-
-
-
-
?
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
?
-
sarcosine degradation when sarcosine is sole source of carbon, nitrogen and energy
-
-
?
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 + 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
-
-
-
?
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
?
-
Bacillus sp. (in: Bacteria) B-0618
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + H2O + O2
?
-
sarcosine degradation when sarcosine is sole source of carbon, nitrogen and energy
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
-
?
sarcosine + H2O + O2
glycine + formaldehyde + H2O2
-
-
-
?
sarcosine + O2 + H2O
formaldehyde + glycine + H2O2
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-deaza-FAD
-
competitive inhibition of flavinylation of apoenzyme
N-(cyclpopropyl)glycine
-
mechanism-based inhibitor, discussion of mechanism
N-cyclopropylglycine
reaction leads to an inactivated species. The polar mechanism is energetically the most favorable. The first rate-limiting step is the N-cyclopropylglycine binding to the flavin ring which simultaneously proceeds with the ring-opening of the N-cyclopropylglycine cyclopropyl group. This step corresponds to the nucleophilic attack of the cyclopropyl group (C3 atom) to the flavin ring (C4a atom)
-
sulfit
-
nearly complete inhibition (93%) of activity when assays are conducted in the presence of excess sulfite
-
iodoacetamide
-
inactivation by modification of 2 specific lysine residues, one of which is Lys358, pH-depedency of inactivation in presence and absence of competitive inhibitor acetate lowerig the pKa for the epsilon-amino groups, inactivation kinetics at different pH-values
methylthioacetate
-
comparison of complexes with wild-type and mutant Y317F
pyrrole-2-carboxylate
-
comparison of complexes with wild-type and mutant Y317F
additional information
-
no inhibition by Tween 20 and Triton X-100
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adrenoleukodystrophy
Adrenoleukodystrophy and other peroxisomal disorders that affect the nervous system, including new observations on L-pipecolic acid oxidase in primates.
Brain Neoplasms
Expression of sarcosine metabolism-related proteins according to metastatic site in breast cancer.
Breast Neoplasms
Expression of sarcosine metabolism-related proteins according to metastatic site in breast cancer.
Breast Neoplasms
Implications of differences in expression of sarcosine metabolism-related proteins according to the molecular subtype of breast cancer.
Folic Acid Deficiency
Sarcosine oxidase activity of rat liver tissue: effect of folic acid deficiency and induced hyperthyroidism.
Genetic Diseases, Inborn
Identification of L-pipecolate oxidase in human liver and its deficiency in the Zellweger syndrome.
Hyperthyroidism
Sarcosine oxidase activity of rat liver tissue: effect of folic acid deficiency and induced hyperthyroidism.
Neoplasm Metastasis
Expression of sarcosine metabolism-related proteins according to metastatic site in breast cancer.
Peroxisomal Disorders
Adrenoleukodystrophy and other peroxisomal disorders that affect the nervous system, including new observations on L-pipecolic acid oxidase in primates.
Prostatic Neoplasms
The Urinary Sarcosine/Creatinine Ratio is a Potential Diagnostic and Prognostic Marker in Prostate Cancer.
Starvation
Global gene expression analysis of the response of physic nut (Jatropha curcas L.) to medium- and long-term nitrogen deficiency.
Zellweger Syndrome
Identification of L-pipecolate oxidase in human liver and its deficiency in the Zellweger syndrome.
Zellweger Syndrome
The human L-pipecolic acid oxidase is similar to bacterial monomeric sarcosine oxidases rather than D-amino acid oxidases.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
154.3
2-isopropyl-4-(methylaminomethyl)thiazole
wild-type, 37°C, pH not specified in the publication
-
258.4
4-(ethylaminomethyl)pyridine
wild-type, 37°C, pH not specified in the publication
-
98
L-proline
wild-type, 37°C, pH not specified in the publication
324.5
N-methyl-D-proline
wild-type, 37°C, pH not specified in the publication
-
0.25
N-Methyl-L-alanine
wild-type, 37°C, pH not specified in the publication
244.7
N-methyl-L-aspartate
wild-type, 37°C, pH not specified in the publication
177.8
N-methyl-L-phenylalanine
wild-type, 37°C, pH not specified in the publication
136.5
N-methyl-L-tryptophan
wild-type, 37°C, pH not specified in the publication
168.5
N-Methyl-L-leucine
wild-type, 37°C, pH not specified in the publication
0.285
sarcosine
-
immobilized enzyme on alkylamine glass beads, pH 7.8, 37°C
19.7
sarcosine
wild-type, reconstituted in presence of 7-chloro-8-ethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
47.2
sarcosine
wild-type, reconstituted in presence of 3-methyl-7,8-dimethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
61.2
sarcosine
wild-type, 37°C, pH not specified in the publication
81.9
sarcosine
wild-type, reconstituted in presence of FMN, pH not specified in the publication, 37°C
85.9
sarcosine
wild-type, reconstituted in presence of 7-methyl-8-bromo-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
112.5
sarcosine
wild-type, reconstituted in presence of 7-methyl-8-chloro-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
128.9
sarcosine
mutant F235V/F339L, pH not specified in the publication, 37°C
134.7
sarcosine
wild-type, reconstituted in presence of 7,8-diethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
137.2
sarcosine
wild-type, reconstituted in presence of FAD, pH not specified in the publication, 37°C
141.6
sarcosine
-
native enzyme, reconstructed in aqueous, pH 8.0, 37°C
142.3
sarcosine
-
native enzyme, reconstructed with 20% dimethyl sulfoxide, pH 8.0, 37°C
153.6
sarcosine
wild-type, reconstituted in presence of isoalloxazine, pH not specified in the publication, 37°C
183.1
sarcosine
wild-type, reconstituted in presence of 7-bromo-8-methyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
additional information
additional information
kinetic parameters for formation of charge transfer complexes with enzyme and substrate or an inhibitor
-
additional information
additional information
-
steady-state kinetics relative to pH, stopped-flow spectroscopy
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0458
2-isopropyl-4-(methylaminomethyl)thiazole
wild-type, 37°C, pH not specified in the publication
-
0.00004
4-(ethylaminomethyl)pyridine
wild-type, 37°C, pH not specified in the publication
-
0.0003
L-proline
wild-type, 37°C, pH not specified in the publication
0.0048
N-methyl-D-proline
wild-type, 37°C, pH not specified in the publication
-
0.0295
N-methyl-L-aspartate
wild-type, 37°C, pH not specified in the publication
0.0537
N-Methyl-L-leucine
wild-type, 37°C, pH not specified in the publication
0.009
N-methyl-L-phenylalanine
wild-type, 37°C, pH not specified in the publication
0.0045
N-methyl-L-tryptophan
wild-type, 37°C, pH not specified in the publication
0.004
N-Methyl-L-alanine
wild-type, 37°C, pH not specified in the publication
0.001
sarcosine
mutant F235V/F339L, pH not specified in the publication, 37°C
0.001
sarcosine
wild-type, reconstituted in presence of 7,8-diethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.001
sarcosine
wild-type, reconstituted in presence of 7-methyl-8-bromo-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.001
sarcosine
wild-type, reconstituted in presence of FAD, pH not specified in the publication, 37°C
0.0011
sarcosine
wild-type, reconstituted in presence of 7-methyl-8-chloro-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.0011
sarcosine
wild-type, reconstituted in presence of isoalloxazine, pH not specified in the publication, 37°C
0.0013
sarcosine
wild-type, reconstituted in presence of 7-bromo-8-methyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.0013
sarcosine
wild-type, reconstituted in presence of 7-chloro-8-ethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.0013
sarcosine
wild-type, reconstituted in presence of FMN, pH not specified in the publication, 37°C
0.0015
sarcosine
wild-type, reconstituted in presence of 3-methyl-7,8-dimethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.053
sarcosine
wild-type, 37°C, pH not specified in the publication
0.115
sarcosine
-
native enzyme, reconstructed with 20% dimethyl sulfoxide, pH 8.0, 37°C
0.204
sarcosine
-
native enzyme, reconstructed in aqueous, pH 8.0, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00033
2-isopropyl-4-(methylaminomethyl)thiazole
wild-type, 37°C, pH not specified in the publication
-
0.00004
4-(ethylaminomethyl)pyridine
wild-type, 37°C, pH not specified in the publication
-
0.0003
L-proline
wild-type, 37°C, pH not specified in the publication
0.000015
N-methyl-D-proline
wild-type, 37°C, pH not specified in the publication
-
0.016
N-Methyl-L-alanine
wild-type, 37°C, pH not specified in the publication
0.00012
N-methyl-L-aspartate
wild-type, 37°C, pH not specified in the publication
0.00021
N-Methyl-L-leucine
wild-type, 37°C, pH not specified in the publication
0.000051
N-methyl-L-phenylalanine
wild-type, 37°C, pH not specified in the publication
0.000033
N-methyl-L-tryptophan
wild-type, 37°C, pH not specified in the publication
0.000007
sarcosine
wild-type, reconstituted in presence of 7-bromo-8-methyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.0000073
sarcosine
wild-type, reconstituted in presence of FAD, pH not specified in the publication, 37°C
0.0000073
sarcosine
wild-type, reconstituted in presence of isoalloxazine, pH not specified in the publication, 37°C
0.0000075
sarcosine
wild-type, reconstituted in presence of 7,8-diethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.0000078
sarcosine
mutant F235V/F339L, pH not specified in the publication, 37°C
0.0000097
sarcosine
wild-type, reconstituted in presence of 7-methyl-8-chloro-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.0000112
sarcosine
wild-type, reconstituted in presence of 7-methyl-8-bromo-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.0000157
sarcosine
wild-type, reconstituted in presence of FMN, pH not specified in the publication, 37°C
0.0000307
sarcosine
wild-type, reconstituted in presence of 3-methyl-7,8-dimethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.0000683
sarcosine
wild-type, reconstituted in presence of 7-chloro-8-ethyl-10-(1'-D-ribityl) isoalloxazine, pH not specified in the publication, 37°C
0.000808
sarcosine
-
native enzyme, reconstructed with 20% dimethyl sulfoxide, pH 8.0, 37°C
0.00087
sarcosine
wild-type, 37°C, pH not specified in the publication
0.00144
sarcosine
-
native enzyme, reconstructed in aqueous, pH 8.0, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23.2
-
pH 8.0, 25°C, mutant C315A, presence of 8-nor-8-chloro-FAD
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q50LF0: subunit alpha, Q50LF2: subunit beta, Q50LF1: subunit delta, Q50LE9: subunit gamma
UniProt
brenda
subunits alpha, beta, gamma, and delta
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
hydride-transfer is the most energetically favorable mechanism. Hydrogen is not transferred in the hydride state (H-) but in a hydrogen atom state. A single electron is simultaneously transferred from sarcosine to flavin through their overlapping orbitals, the reaction mechanism can be labeled the hydrogen-atom coupled electron-transfer (HACET) mechanism. Sarcosine is moved close to the flavin ring because of a small charge transfer and the positively charged residues (Arg49, Arg52, and Lys348) near the active site play a prominent role in stabilizing the sarcosine-flavin complex
physiological function
-
sarcosine oxidase catalyzes the oxidation of the methyl group in sarcosine and transfer of the oxidized methyl group into the one-carbon metabolic pool, yielding equimolar glycine, hydrogen peroxide, and formaldehyde or 5,10-methylenetetrahydrofolate
additional information
-
the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the hetero-octameric (alphabeta)4 form and shows NADH dehydrogenase activity, structure of isolated subunit tetramers, overview
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
-
1 * 110000 (A) + 1 * 44000 (B) + 1 * 21000 (C) + 1 * 10000 (D), SDS-PAGE
110000
-
1 * 110000 (A) + 1 * 44000 (B) + 1 * 21000 (C) + 1 * 10000 (D), SDS-PAGE
174000
21000
-
1 * 110000 (A) + 1 * 44000 (B) + 1 * 21000 (C) + 1 * 10000 (D), SDS-PAGE
42000
43000
44000
45000
48000
and 51700, modified enzyme covalently bound with about two or three poly-Lys, mass spectrum analysis
51000
51700
and 48000, modified enzyme covalently bound with about two or three poly-Lys, mass spectrum analysis
54000
-
4 * 54000, recombinant alpha-subunnit, + 4 * 43000, recombinant beta-subunit, SDS-PAGE, (alphabeta)4 , the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the heterooctameric (alphabeta)4 form and shows NADH dehydrogenase activity, transmission electron microscopy and gel filtration
43000
-
4 * 54000, recombinant alpha-subunnit, + 4 * 43000, recombinant beta-subunit, SDS-PAGE, (alphabeta)4 , the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the heterooctameric (alphabeta)4 form and shows NADH dehydrogenase activity, transmission electron microscopy and gel filtration
44000
-
1 * 110000 (A) + 1 * 44000 (B) + 1 * 21000 (C) + 1 * 10000 (D), SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
or trimer, alpha,beta or alpha,beta2, 100000 (alpha), 55000 (beta), SDS-PAGE
heterooctamer
-
4 * 54000, recombinant alpha-subunnit, + 4 * 43000, recombinant beta-subunit, SDS-PAGE, (alphabeta)4 , the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the heterooctameric (alphabeta)4 form and shows NADH dehydrogenase activity, transmission electron microscopy and gel filtration
heterotetramer
monomer
tetramer
additional information
heterotetramer
1 * 103000 + 1 * 44000 + 1 * 21000 + 1 * 11000, SDS-PAGE
heterotetramer
-
1 * 110000 + 1 * 44000 + 1 * 21000 + 1 * 10000, calculated from amino acid sequence
tetramer
-
1 * 110000 (A) + 1 * 44000 (B) + 1 * 21000 (C) + 1 * 10000 (D), SDS-PAGE
tetramer
-
1 * 96000 + 1 * 45000 + 1 * 23000 + 1 * 14000, SDS-PAGE
additional information
-
structure of isolated subunit tetramers, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme inhibitor complexes, discussion of active site bindung determinants
mutants K265M, K265Q, K265A, K265R, to 1.6-2.1 A resolution. The overall structure of MSOX and residue conformation in the sarcosine binding cavity are unaffected by replacement of K265 with Met or Arg. The side chain of K265M exhibits the same configuration in each molecule of K265M crystals and is nearly congruent with K265 in wild-type MSOX. The side chain of K265R is dramatically shifted compared with K265, points in the opposite direction, and exhibits significant conformational variability between molecules of the same crystal. The major species in solutions of K265R is likely to contain a flipped-out R265 and exhibit negligible oxygen activation, similar to K265M. The 400fold higher oxygen reactivity observed with K265R is attributed to a minor flipped-in R265 conformer whose oxygen reactivity is similar to that of wild-type MSOX. Structural water molecule 1 is strikingly absent in K265M and K265R
R49K mutant after reconstitution with FAD, sitting drop vapor diffusion method, high salt or high PEG conditions
unliganded enzyme, high flexibility of the active site loop is important for enzyme activity
-
complexed with methylthioacetate, pyrrole 2-carboxylate and sulfite, and sarcosine-reduced enzyme. Sarcosine oxidase comprises alpha-, beta-, gamma- and delta-subunits, FAD and FMN cofactors, and a large internal cavity. Methylthioacetate and pyrrole 2-carboxylate are sandwiched between the re-face of the FAD isoalloxazine ring and the beta-subunit C-terminal residues. Reduction of flavin cofactors shifts the beta-subunit A1 residue towards the alpha-subunit M55, forming a surface cavity at the oxygen-channel vestibule and rendering the beta-subunit C-terminal residues mobile. Three channels connect the cavity and the enzyme surface. Two of them exist in the inter-subunit space between alpha- and beta-subunits, and the substrate sarcosine seems to enter the active site through either of these channels and reaches the reside of the FAD isoalloxazine ring by traversing the mobile beta-subunit C-terminal residues. The third channel goes through the alpha-subunit and has a folinic acid-binding site
-
in complex with dimethylglycine and folinic acid. The alpha subunit consists of two domains, contains NAD+ and binds folinic acid. The beta subunit contains dimethylglycine, FAD and FMN. The gamma subunit is in contact with two domains of alpha subunit and has possibly a folate-binding structure. The delta subunit contains a single atom of and has a Cys3His zinc finger structure
-
enzyme in complex with dimethylglycine and folinic acid, vapor diffusion method, using 0.1 M Tris-HCl (pH 8.5), 1.9 M ammonium sulfate, and 10 mM CuSO4
-
alpha subunit contains NAD+ and putative folate binding site. The FAD binding site is in the beta subunit, FMN is bound at the interface of the alpha and beta subunit. A zinc ion, coordinated by three cysteine and one histidine side-chains, is bound to the delta subunit
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C265A
-
almost wild type activity but much more stable against thiol modifying inhibitors
C265D
-
almost wild type activity but much more stable against thiol modifying inhibitors
C265R
-
almost wild type activity but much more stable against thiol modifying inhibitors
C265S
-
almost wild type activity but much more stable against thiol modifying inhibitors
C318S
C314A
-
mutation of the covalent attachment site of FAD, mutant forms unstable complexes with FAD. In situ reconstitution of activity by assaying mutant in presence of FAD or 8-nor-8-chloro-FAD, giving a specific activity of 14% or 80% of wild-type, resp. Mutant exhibits high affinity for reduced flavin
C315A
-
inactive, no bound FAD, forms stable non-covalent complex with 5-deazaFAD
H269N
His269 is probably not the active-site base but involved in interaction with substrate
H45A
-
contains covalently bound FAD, 4fold less FAD than in wild type enzyme, catalytic properties similar than wild type enzyme, 50% of wild type activity
H45N
-
contains covalently bound FAD, 4fold less FAD than in wild type enzyme, catalytic properties similar than wild type enzyme, 50% of wild type activity
K265A
K265M
K265Q
K265R
R49A
-
inactive, no bound FAD, forms stable non-covalent complex with 5-deazaFAD
R49K
Y317F
-
20fold decrease in the maxumim rate of the reductive half-reaction. Unlike wild-type, Kd-values of mutant are pH-dependent
K265A
Bacillus sp. (in: Bacteria) B-0618
-
at least 250fold decrease in reaction rate. Crystallization analysis
-
K265M
Bacillus sp. (in: Bacteria) B-0618
-
at least 250fold decrease in reaction rate. Crystallization analysis
-
K265Q
Bacillus sp. (in: Bacteria) B-0618
-
at least 250fold decrease in reaction rate. Crystallization analysis
-
K265R
Bacillus sp. (in: Bacteria) B-0618
-
at least 250fold decrease in reaction rate. Crystallization analysis
-
H173N
-
leads to catalytically inactive beta subunit, study on organization of subunits and coenzymes
K171A
K171D
K171R
K358A
K358D
Y358R
the variant displays 0.07% activity and a higher apparent KM for sarcosine as compared to wild type enzyme
F235V/F339L
additional information
C318S
-
modification of covalent flavin attachment site, mutant with extremely weak activity
K265A
at least 250fold decrease in reaction rate. Crystallization analysis
K265M
at least 250fold decrease in reaction rate. Crystallization analysis
K265Q
at least 250fold decrease in reaction rate. Crystallization analysis
K265R
-
less than 30% of covalently bound FAD, strongly reduced turnover
K265R
at least 250fold decrease in reaction rate. Crystallization analysis
R49K
40fold decrease of turnover, 150fold decrease of catalytic efficiency, structure very similar to wild type enzyme
R49K
-
contains covalently bound FAD, 4fold less FAD than in wild type enzyme, 4% of wild type activity
K171A
-
39% activity of the wild-type enzyme, strongly increased Km for oxygen
K171A
the mutant shows 39% activity of the wild type enzyme
K171D
-
32% activity of the wild-type enzyme, strongly increased Km for oxygen
K171D
the mutant shows 32% activity of the wild type enzyme
K171R
the mutant shows 58% activity of the wild type enzyme
additional information
-
immobilization of the enzyme onto alkylamine and arylamine glass by crosslinking with glutaraldehyde for determination of serum sarcosine, method, overview. The enzyme shows a decrease in optimum pH and KM, and an increase in optimum temperature and time for linearity after immobilization
additional information
-
production of soluble apoenzyme lacking covalently bound FAD by controlled expression in Escherichia coli. Reconstitution of enzyme by incubation with FAD
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
37°C, 2.5 h, more than 90% of initial activity of poly-lysine modified enzyme is maintained
742678
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pH 8.0, 7 days, residual activity of soluble enzyme is 7.9%, residual activity poly-lysine modified enzyme is 95.6%
60
60
10 min, residual activity of soluble enzyme is 2.3%, residual activity poly-lysine modified enzymeis 74.7%
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
modified technique is successfully established for efficiently improving the stability of sarcosine oxidase via poly-Lys covalent binding onto enzymatic surface. Compared to the free enzyme, higher pH stability and thermostability of modified sarcosine oxidase is achieved with a series of characterization analysis. It is owing to that the loosening of three-dimensional configuration can be restricted by the enzymatic surface protection with poly-Lys and subsequently maintained a more stable enzyme structure. The changed microenvironment around the enzyme in themodification process can also contribute to the better stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
37°C, pH 8.0, 7 days, residual activity of soluble enzyme is 7.9%, residual activity poly-lysine modified enzyme is 95.6%
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity-purification, 4-aminopyrrole-2-carboxylic acid as the affinity ligand, which is coupled with Sepharose CL 4B via spacers composed of epichlorohydrin and ethylenediamine. With the affinity medium, the purification process consists of only one affinity chromatography step to capture monomeric enzyme. The purified enzyme iss 94% and 96% pure when analyzed on an HPLC and reducing SDS-PAGE
HiTrap DEAE column chromatography, HisTrap column chromatography, HiTrap phenyl column chromatography, Resources Q column chromatography, and Superdex 200 gel filtration
-
native enzyme by ammoniumm sulfate fractionation, hydrophobic interaction and anion exchange chromatography, and gel filtration
-
recombinant His-tagged alpha and beta subunits from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
-
recombinant protein, purified by one step of affinity purification on a Ni-Sepharose column, and another step of ion-exchange purification on a DEAE column
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enhancement of soluble expression of codon-optimized enzyme in Escherichia coli via chaperone co-expression
-
expressed in Escherichia coli BL21 (DE3) in the form of inclusion bodies. Unfolded Bacillus sp. SOX was extracted from an inclusion body and reconstructed with FAD and a group of coenzyme-like compounds. The interactions between the enzyme and various ligands are simulated using molecular docking in the SwissDock service and DS 2.5 program. When the length of the ligand is reduced, the number of H bonds is also reduced. Furthermore, new bonds are formed between the enzyme and the ligands, owing to replacements at the position 7- or 8-sites. Based on the results of structural analysis, phosphoric acid and adenine groups in the natural coenzyme likely play vital roles in maintenance of the enzyme structure. The 7-and 8-site modifications in ligands could facilitate the formation of novel interactions that stabilize the complex. The activities of natural enzyme and refolded FAD-enzyme aree significantly reduced in the presence of organic solvents. However, when the enzyme is refolded with coenzyme-like ligands containing halogen atoms at the position 7- or 8-site, the trend towards reduction is effectively inhibited, and the enzymes exhibit considerably higher relative specificities
-
expression in Escherichia coli
genes TK0116 and TK0117, separate cloning and expression in Eschericia coli strain BL21(DE3) of His-tagged alpha and beta subunits of SOX
-
integration strategy coupling codon and fermentation optimization is used for efficiently enhancing sarcosine oxidase production in recombinant Escherichia coli
mutant proteins expressed as His-tag fusion proteins in Escherichia coli BL21(DE3)
-
native and mutant enzyme in Escherichia coli BL21(DE3), R49 mutants contain His-tag
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
-
reconstitution of holoprotein from inclusion bodies, suitable conditions for binding of flavoprotein to apoprotein are 0.3 g/l protein concentration, pH 8.5, 4°C, ratio of GSH/GSSH 2
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
medicine
analysis
-
sarcosine oxidases can be applied in enzymatic measuring of creatinine
analysis
-
improved amperometric biosensor for detection of creatinine based on immobilization of nanoparticles of creatininase, creatinase, and sarcosine oxidase onto glassy carbon electrode. The biosensor shows optimum response within 2 s at pH 6.0 in 0.1 M sodium phosphate buffer and 25°C, when operated at 1.0 V against Ag/AgCl. Recoveries of added creatinine in sera are 97.97% for 0.1 mM and 98.76% for 0.15 mM
analysis
-
sarcosine oxidases can be applied in enzymatic measuring of creatinine
-
diagnostics
a photobioelectrochemical sensor based on CdSe/ZnS quantum dot and sarcosine oxidase is developed to determine sarcosine concentrations. The linear range is from 0.1 mM to 1 mM and the sensitivity depends on the number of immobilised enzyme layers.It is demonstrated that the [SOD/PAH]6-layer system is well suited for sensitive sarcosine detection. Sarcosine is an intermediate in the enzymatic analysis of creatinine, and thus, a sarcosine sensor can be beneficial for the diagnosis of kidney diseases
diagnostics
developement of a simple and low cost electrochemical enzymatic biosensor for the determination of sarcosine in urine, based on the covalent immobilization of sarcosine oxidase, using N-ethyl-N-(3-dimethylaminopropyl) carbodiimide and N-hydroxysuccinimide, on the surface of the screen-printed carbon electrode.The biosensor presents high analytical performance features, such as large concentration linear range (10-100 nM), low detection limit (16 nM) and large storage stability (60 days). The biosensor is successfully applied to the analysis of sarcosine in synthetic urine samples
diagnostics
sarcosine oxidase is an important diagnostic enzyme in the renal function examination
diagnostics
-
sarcosine oxidase is an important diagnostic enzyme in the renal function examination
-
medicine
a photobioelectrochemical sensor based on CdSe/ZnS quantum dot and sarcosine oxidase is developed to determine sarcosine concentrations. The linear range is from 0.1 mM to 1 mM and the sensitivity depends on the number of immobilised enzyme layers.It is demonstrated that the [SOD/PAH]6-layer system is well suited for sensitive sarcosine detection. Sarcosine is an intermediate in the enzymatic analysis of creatinine, and thus, a sarcosine sensor can be beneficial for the diagnosis of kidney diseases
medicine
developement of a simple and low cost electrochemical enzymatic biosensor for the determination of sarcosine in urine, based on the covalent immobilization of sarcosine oxidase, using N-ethyl-N-(3-dimethylaminopropyl) carbodiimide and N-hydroxysuccinimide, on the surface of the screen-printed carbon electrode.The biosensor presents high analytical performance features, such as large concentration linear range (10-100 nM), low detection limit (16 nM) and large storage stability (60 days). The biosensor is successfully applied to the analysis of sarcosine in synthetic urine samples
medicine
-
the enzyme can be used as biosensor for the analysis of sarcosine in urine samples
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Inouye, Y.; Nishimura, M.; Matsuda, Y.; Hoshika, H.; Iwasaki, H.; Hujimura, K.; Asano, K.; Nakamura, S.
Purification and characterization of sarcosine oxidase of Streptomyces origin
Chem. Pharm. Bull.
35
4194-4202
1987
Streptomyces sp., Streptomyces sp. KB210-8SY
brenda
Ogushi, S.; Nagao, K.; Emi, S.; Ando, M.; Tsuru, D.
Sarcosine oxidase from Arthrobacter urefaciens: Purification and some properties
Chem. Pharm. Bull.
36
1445-1450
1988
Paenarthrobacter ureafaciens
-
brenda
Matsuda, Y.; Hoshika, H.; Inouye, Y.; Ikuta, S.; Matsuura, K.; Nakamura, S.
Purification and characterization of sarcosine oxidase of Bacillus origin
Chem. Pharm. Bull.
35
711-717
1987
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) B-0618
brenda
Kim, J.M.; Shimizu, S.; Yamada, H.
Crystallization and characterization of sarcosine oxidase from Alcaligenes denitrificans subsp. denitrificans
Agric. Biol. Chem.
51
1167-1168
1987
Achromobacter denitrificans
-
brenda
Kim, J.M.; Shimizu, S.; Yamada, H.
Sarcosine oxidase involved in creatinine degradation in Alcaligenes denitrificans subsp. denitrificans J9 and Arthrobacter spp. J5 and J11
Agric. Biol. Chem.
50
2811-2816
1986
Achromobacter denitrificans, Arthrobacter sp., Arthrobacter sp. J5 J11
-
brenda
Schuman Jorns, M.
Properties and catalytic function of the two nonequivalent flavins in sarcosine oxidase
Biochemistry
24
3189-3194
1985
Corynebacterium sp.
brenda
Suzuki, M.
Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96
J. Biochem.
89
599-607
1981
Corynebacterium sp.
brenda
Hayashi, S.; Nakamura, S.; Suzuki, M.
Corynebacterium sarcosine oxidase: a unique enzyme having covalently-bound and noncovalently-bound flavins
Biochem. Biophys. Res. Commun.
96
924-930
1980
Corynebacterium sp.
brenda
Mori, N.; Sano, M.; Tani, Y.; Yamada, H.
Purification and properties of sarcosine oxidase from Cylindrocarpum didymum M-1
Agric. Biol. Chem.
44
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brenda
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brenda
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One-carbon metabolism in microorganisms. I. Oxidative demethylation in a sarcosine-utilizing bacterium
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brenda
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Biochemistry
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brenda
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brenda
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Interaction of tetrahydrofolate and other folate derivates with bacterial sarcosine oxidase
Biochemistry
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Corynebacterium sp.
brenda
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Structure of the flavocoenzyme of two homologous amine oxidases: monomeric sarcosine oxidase and N-methyltryptophan oxidase
Biochemistry
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Bacillus sp. (in: Bacteria)
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Bacillus sp. (in: Bacteria)
brenda
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Bacillus sp. (in: Bacteria)
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Cricetulus griseus, Mus musculus
brenda
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Arthrobacter sp.
brenda
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Monomeric sarcosine oxidase: evidence for an ionizable group in the E.S complex
Biochemistry
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Bacillus sp. (in: Bacteria)
brenda
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Monomeric sarcosine oxidase: role of histidine 269 in catalysis
Biochemistry
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Bacillus sp. (in: Bacteria) (P40859)
brenda
Nishiya, Y.; Imanaka, T.
Analysis of interaction between the Arthrobacter sarcosine oxidase and the coenzyme flavin adenine dinucleotide by site-directed mutagenesis
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brenda
Nishiya, Y.; Zuihara, S.; Imanaka, T.
Active site analysis and stabilization of sarcosine oxidase by the substitution of cysteine residues
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Arthrobacter sp.
brenda
Harris, R.J.; Meskys, R.; Sutcliffe, M.J.; Scrutton, N.S.
Kinetic studies of the mechanism of carbon-hydrogen bond breakage by the heterotetrameric sarcosine oxidase of Arthrobacter sp. 1-IN
Biochemistry
39
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Arthrobacter sp.
brenda
Zhao, G.; Qu, J.; Davis, F.A.; Jorns, M.S.
Inactivation of monomeric sarcosine oxidase by reaction with N-(cyclopropyl)glycine
Biochemistry
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Bacillus sp. (in: Bacteria)
brenda
Wagner, M.A.; Trickey, P.; Chen, Z.W.; Mathews, F.S.; Jorns, M.S.
Monomeric sarcosine oxidase: 1. Flavin reactivity and active site binding determinants
Biochemistry
39
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2000
Bacillus sp. (in: Bacteria) (P40859)
brenda
Wagner, M.A.; Jorns, M.S.
Monomeric sarcosine oxidase: 2. Kinetic studies with sarcosine, alternate substrates, and a substrate analogue
Biochemistry
39
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2000
Bacillus sp. (in: Bacteria)
brenda
Eschenbrenner, M.; Chlumsky, L.J.; Khanna, P.; Strasser, F.; Jorns, M.S.
Organization of the multiple coenzymes and subunits and role of the covalent flavin link in the complex heterotetrameric sarcosine oxidase
Biochemistry
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Corynebacterium sp.
brenda
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Cofactors in sarcosine oxidase from Corynebacterium sp. U-96
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Corynebacterium sp.
brenda
Mukouyama, E.B.; Oguchi, M.; Kodera, Y.; Maeda, T.; Suzuki, H.
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Biochem. Biophys. Res. Commun.
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Corynebacterium sp.
brenda
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Expression and characterization of a thermostable sarcosine oxidase (SOX) from Bacillus sp. in Escherichia coli
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Bacillus sp. (in: Bacteria) (Q6ITC6), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) BSD-8 (Q6ITC6)
brenda
Ida, K.; Moriguchi, T.; Suzuki, H.
Crystal structure of heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96
Biochem. Biophys. Res. Commun.
333
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2005
Corynebacterium sp.
brenda
Zhao, G.; Jorns, M.S.
Ionization of zwitterionic amine substrates bound to monomeric sarcosine oxidase
Biochemistry
44
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2005
Bacillus sp. (in: Bacteria)
brenda
Hassan-Abdallah, A.; Bruckner, R.C.; Zhao, G.; Jorns, M.S.
Biosynthesis of covalently bound flavin: isolation and in vitro flavinylation of the monomeric sarcosine oxidase apoprotein
Biochemistry
44
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2005
Bacillus sp. (in: Bacteria)
brenda
Zhao, G.; Jorns, M.S.
Spectral and kinetic characterization of the michaelis charge transfer complex in monomeric sarcosine oxidase
Biochemistry
45
5985-5992
2006
Bacillus sp. (in: Bacteria) (P40859)
brenda
Hassan-Abdallah, A.; Zhao, G.; Jorns, M.S.
Role of the covalent flavin linkage in monomeric sarcosine oxidase
Biochemistry
45
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2006
Bacillus sp. (in: Bacteria)
brenda
Chen, Z.W.; Hassan-Abdulah, A.; Zhao, G.; Jorns, M.S.; Mathews, F.S.
Heterotetrameric sarcosine oxidase: structure of a diflavin metalloenzyme at 1.85 A resolution
J. Mol. Biol.
360
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2006
Stenotrophomonas maltophilia
brenda
Hynson, R.M.; Mathews, F.S.; Schuman Jorns, M.
Identification of a stable flavin-thiolate adduct in heterotetrameric sarcosine oxidase
J. Mol. Biol.
362
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2006
Stenotrophomonas maltophilia
brenda
Nagata, K.; Sasaki, H.; Ohtsuka, J.; Hua, M.; Okai, M.; Kubota, K.; Kamo, M.; Ito, K.; Ichikawa, T.; Koyama, Y.; Tanokura, M.
Crystal structure of monomeric sarcosine oxidase from Bacillus sp. NS-129 reveals multiple conformations at the active-site loop
Proc. Jpn. Acad. Ser. B Phys. Biol. Sci.
81
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2005
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) NS-129
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brenda
Hassan-Abdallah, A.; Zhao, G.; Jorns, M.S.
Covalent flavinylation of monomeric sarcosine oxidase: identification of a residue essential for holoenzyme biosynthesis
Biochemistry
47
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2008
Bacillus sp. (in: Bacteria)
brenda
Hassan-Abdallah, A.; Zhao, G.; Chen, Z.W.; Mathews, F.S.; Schuman Jorns, M.
Arginine 49 is a bifunctional residue important in catalysis and biosynthesis of monomeric sarcosine oxidase: a context-sensitive model for the electrostatic impact of arginine to lysine mutations
Biochemistry
47
2913-2922
2008
Bacillus sp. (in: Bacteria) (P40859)
brenda
Zhao, G.; Bruckner, R.C.; Jorns, M.S.
Identification of the oxygen activation site in monomeric sarcosine oxidase: role of lys265 in catalysis
Biochemistry
47
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2008
Bacillus sp. (in: Bacteria)
brenda
Saito, M.; Kanno, M.; Iizuka, H.; Suzuki, H.
Kinetic studies on the role of Lys-171 and Lys-358 in the beta subunit of sarcosine oxidase from Corynebacterium sp. U-96
J. Biochem.
141
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Corynebacterium sp. U-96
brenda
Jorns, M.S.; Chen, Z.W.; Mathews, F.S.
Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase
Biochemistry
49
3631-3639
2010
Bacillus sp. (in: Bacteria) (P40859), Bacillus sp. (in: Bacteria) B-0618 (P40859)
brenda
Moriguchi, T.; Ida, K.; Hikima, T.; Ueno, G.; Yamamoto, M.; Suzuki, H.
Channeling and conformational changes in the heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96
J. Biochem.
148
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2010
Corynebacterium sp.
brenda
Liu, H.; Sun, G.; Ma, X.; Sun, L.; Lu, X.; Zhang, P.
Purification and characterization of a sarcosine oxidase from Bacillus sp. BSD-8
Chin. J. Biotechnol.
26
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2010
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) BSD-8
brenda
Lee, S.; Jia, B.; Pham, B.P.; Shao, Y.; Kwak, J.M.; Cheong, G.W.
Architecture and characterization of sarcosine oxidase from Thermococcus kodakarensis KOD1
Extremophiles
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87-93
2012
Thermococcus kodakarensis
brenda
Pundir, C.; Chauhan, N.; Kumari, G.; Vandana, C.
Immobilization of Arthrobacter sarcosine oxidase onto alkylamine and arylamine glass and its application in serum sarcosine determination
Indian J. Biotechnol.
10
219-223
2011
Arthrobacter sp.
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brenda
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
J. Biochem.
151
633-642
2012
Corynebacterium sp.
brenda
Rebelo, T.S.; Pereira, C.M.; Sales, M.G.; Noronha, J.P.; Costa-Rodrigues, J.; Silva, F.; Fernandes, M.H.
Sarcosine oxidase composite screen-printed electrode for sarcosine determination in biological samples
Anal. Chim. Acta
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2014
Bacillus sp. (in: Bacteria), Bacillus sp. BSD-8 (Q6ITC6)
brenda
Watanabe, G.; Nakajima, D.; Hiroshima, A.; Suzuki, H.; Yoneda, S.
Analysis of water channels by molecular dynamics simulation of heterotetrameric sarcosine oxidase
Biophys. Physicobiol.
12
131-137
2015
Corynebacterium sp. U-96 (Q50LF0 and Q50LF2 and Q50LF1 and Q50LE9)
brenda
Pietra, F.
On the quest of dioxygen by monomeric sarcosine oxidase. A molecular dynamics investigation
Chem. Biodivers.
12
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2015
Bacillus sp. BSD-8 (Q6ITC6)
brenda
Riedel, M.; Goebel, G.; Abdelmonem, A.M.; Parak, W.J.; Lisdat, F.
Photoelectrochemical sensor based on quantum dots and sarcosine oxidase
Chemphyschem
14
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2013
Bacillus sp. BSD-8 (Q6ITC6)
brenda
Tong, Y.; Xin, Y.; Yang, H.; Zhang, L.; Wang, W.
Efficient improvement on stability of sarcosine oxidase via poly-lysine modification on enzyme surface
Int. J. Biol. Macromol.
67
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2014
Bacillus sp. BSD-8 (Q6ITC6)
brenda
Tong, Y.; Feng, S.; Xin, Y.; Yang, H.; Zhang, L.; Wang, W.; Chen, W.
Enhancement of soluble expression of codon-optimized Thermomicrobium roseum sarcosine oxidase in Escherichia coli via chaperone co-expression
J. Biotechnol.
218
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2016
Thermomicrobium roseum, Thermomicrobium roseum DSM 5159
brenda
Bucci, A.; Yu, T.Q.; Vanden-Eijnden, E.; Abrams, C.F.
Kinetics of O2 entry and exit in monomeric sarcosine oxidase via Markovian Milestoning Molecular Dynamics
J. Chem. Theory Comput.
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2016
Bacillus sp. (in: Bacteria)
brenda
Xin, Y.; Zheng, M.; Wang, Q.; Lu, L.; Zhang, L.; Tong, Y.; Wang, W.
Structural and catalytic alteration of sarcosine oxidase through reconstruction with coenzyme-like ligands
J. Mol. Catal. B
133
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2016
Bacillus sp. (in: Bacteria)
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brenda
Tong, Y.; Xin, Y.; Yang, H.; Zhang, L.; Tao, X.; Xu, H.; Wang, W.
Novel affinity purification of monomeric sarcosine oxidase expressed in Escherichia coli
J. Sep. Sci.
36
3086-3092
2013
Bacillus sp. BSD-8 (Q6ITC6)
brenda
Tong, Y.; Yang, H.; Xin, Y.; Zhang, L.; Wang, W.
Novel integration strategy coupling codon and fermentation optimization for efficiently enhancing sarcosine oxidase (SOX) production in recombinant Escherichia coli
World J. Microbiol. Biotechnol.
31
707-716
2015
Bacillus sp. (in: Bacteria) (Q6ITC6), Bacillus sp. (in: Bacteria) BSD-8 (Q6ITC6)
brenda
Kumar, P.; Jaiwal, R.; Pundir, C.S.
An improved amperometric creatinine biosensor based on nanoparticles of creatininase, creatinase and sarcosine oxidase
Anal. Biochem.
537
41-49
2017
Bacillus sp. (in: Bacteria)
brenda
Lahham, M.; Jha, S.; Goj, D.; Macheroux, P.; Wallner, S.
The family of sarcosine oxidases Same reaction, different products
Arch. Biochem. Biophys.
704
108868
2021
Corynebacterium sp. U-96 (Q50LF0 and Q50LF2 and Q50LE9 and Q50LF1)
brenda
Ida, K.; Moriguchi, T.; Suzuki, H.
Crystal structure of heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96
Biochem. Biophys. Res. Commun.
333
359-366
2005
Corynebacterium sp. U-96
brenda
Hayashi, S.; Nakamura, S.; Suzuki, M.
Corynebacterium sarcosine oxidase A unique enzyme having covalently-bound and noncovalently-bound flavins
Biochem. Biophys. Res. Commun.
96
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1980
Corynebacterium sp. U-96
brenda
Jorns, M.S.
Properties and catalytic function of the two nonequivalent flavins in sarcosine oxidase
Biochemistry
24
3189-3194
1985
Corynebacterium sp. U-96
brenda
Hayashi, S.; Suzuki, M.; Nakamura, S.
Steady-state kinetics and spectral properties of Corynebacterium sarcosine oxidase
Biochim. Biophys. Acta
742
630-646
1983
Corynebacterium sp. U-96
brenda
Wang, Q.; Xin, Y.; Yang, H.; Tong, Y.; Wang, W.
Deflavination of Bacillus sp. sarcosine oxidase and reconstitution of flavoproteins
J. Food Sci. Biotechnol.
37
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2018
Bacillus sp. (in: Bacteria)
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brenda
Zheng, M.; Hao, M.; Fan, G.; Zhang, Y.; Xin, Y.; Zhang, L.
Preparation, reconstruction, and characterization of a predicted Thermomicrobium roseum sarcosine oxidase
Mol. Catal.
455
132-142
2018
Thermomicrobium roseum (B9L163), Thermomicrobium roseum DSM 5159 (B9L163)
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brenda
Xin, Y.; Hao, M.; Fan, G.; Zhang, Y.; Zhang, L.
Soluble expression of Thermomicrobium roseum sarcosine oxidase and characterization of N-demethylation activity
Mol. Catal.
464
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2019
Thermomicrobium roseum (B9L163), Thermomicrobium roseum DSM 5159 (B9L163)
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brenda
Abe, Y.; Shoji, M.; Nishiya, Y.; Aiba, H.; Kishimoto, T.; Kitaura, K.
The reaction mechanism of sarcosine oxidase elucidated using FMO and QM/MM methods
Phys. Chem. Chem. Phys.
19
9811-9822
2017
Bacillus sp. B-0618 (P40859)
brenda
Shoji, M.; Abe, Y.; Boero, M.; Shigeta, Y.; Nishiya, Y.
Reaction mechanism of N-cyclopropylglycine oxidation by monomeric sarcosine oxidase
Phys. Chem. Chem. Phys.
22
16552-16561
2020
Bacillus sp. B-0618 (P40859)
brenda
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