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Information on EC 1.5.3.24 - sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)
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1.5.3.24 sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)IUBMB Comments
The enzyme, found in some bacterial species, is composed of four different subunits and two active sites connected by a large "reaction chamber". An imine intermediate is transferred between the sites, eliminating the production of toxic formaldehyde. The enzyme contains three cofactors: noncovalently bound FAD and NAD+, and FMN that is covalently bound to a histidine residue. In the absence of folate the enzyme catalyses the reaction of EC 1.5.3.1, sarcosine oxidase (formaldehyde-forming).
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
heterotetrameric sarcosine oxidase, HSO, sarcosine oxidase, sarcosine oxidase P, sarcosine: oxygen oxidoreductase (demethylating), sarcosine:oxygen oxidoreductase (demethylating), TSOX, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
heterotetrameric sarcosine oxidase
sarcosine oxidase
sarcosine: oxygen oxidoreductase (demethylating)
-
-
TSOX
heterotetrameric sarcosine oxidase
-
-
-
-
heterotetrameric sarcosine oxidase
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
-
heterotetrameric sarcosine oxidase
Stenotrophomonas maltophilia DSM 2701
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
-
-
sarcosine oxidase
-
-
ambiguous
-
TSOX
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sarcosine + 5,6,7,8-tetrahydrofolate + O2 = glycine + 5,10-methylenetetrahydrofolate + H2O2
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
sarcosine, 5,6,7,8-tetrahydrofolate:O2 oxidoreductase (demethylating, 5,10-methylenetetrahydrofolate-forming)
The enzyme, found in some bacterial species, is composed of four different subunits and two active sites connected by a large "reaction chamber". An imine intermediate is transferred between the sites, eliminating the production of toxic formaldehyde. The enzyme contains three cofactors: noncovalently bound FAD and NAD+, and FMN that is covalently bound to a histidine residue. In the absence of folate the enzyme catalyses the reaction of EC 1.5.3.1, sarcosine oxidase (formaldehyde-forming).
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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
L-proline + O2
?
-
poor substrate, the reduction of the enzyme with L-proline at pH 8.0 is not significant under aerobic conditions
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + phenazine methosulfate
?
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Arthrobacter sp. 1-IN
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Stenotrophomonas maltophilia DSM 2701
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
-
-
-
?
additional information
?
-
-
no activity with NAD+ or NADP+ as electron acceptor in the presence or absence of various thiols (glutathione, coenzyme A, dithioerythritol)
-
-
-
additional information
?
-
-
oxygen cannot be replaced by methylene blue or cytochrome c. The enzyme shows no activity with N,N-dimethylglycine, glycine, betaine, choline, 1,3-dimethylurea, 1-methylguanidine, 1-methylhydantoin, sarcosyl-glycine, and sarcosyl-sarcosine
-
-
-
additional information
?
-
-
the reduction of the oxidized enzyme with dithiothreitol or its reoxidation with air shows slow kinetics. Moreover, the oxidized enzyme in an about 40% reduced state with dithiothreitol contains a flavin semiquinone comprising approximately 35% of the total flavin
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-
-
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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
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Arthrobacter sp. 1-IN
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
-
-
-
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Stenotrophomonas maltophilia DSM 2701
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
contains 1 mol of noncovalently bound Flavin (FAD) plus 1 mol of covalently bound flavin [8alpha-(N3-histidyl)-FAD] per mole of enzyme
FAD
-
the enzyme contains both 1 mol of non-covalently bound FAD and 1 mol of covalently bound FAD per mol of enzyme
FAD
-
the enzyme contains both covalently bound FAD [8a-(7V3-histidyl)FAD] and noncovalently bound FAD
FMN
-
the wild type enzyme contains 1 mol of covalently bound FMN attached to subunit beta
NAD+
-
the wild type enzyme contains 1 mol of noncovalently bound NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyldicarbonate
-
the enzyme rapidly loses its activity on incubation with 0.5 mM diethyldicarbonate
pyrrole 2-carboxylate
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competitive inhibition with respect to sarcosine
-
additional information
-
there is no inhibitory effect with metal ions and chemicals such as Ca2+, Mg2+, Fe3+, alpha,alpha'-dipyridyl, EDTA, 2-mercaptoethanol, glutathione (reduced form), dithiothreitol, NaN3, NaF, and NaAsO2
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acetate
-
competitive inhibitor, protects the enzyme approximately 50% from inactivation by iodoacetamide or completely from inactivation by diethyldicarbonate
iodoacetamide
-
the inhibition by iodoacetamide is prevented by the substrate analog sodium acetate
methylthioacetate
-
competitive inhibition with respect to sarcosine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
2-Furoic acid
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
-
mutant enzyme H175A, pH and temperature not specified in the publication
8.6
-
wild type enzyme, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Stenotrophomonas maltophilia DSM 2701
subunits alpha, beta, gamma and delta; renamed as Stenotrophomomas maltophilia
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
UniProt
brenda
subunits alpha, beta, gamma and delta; renamed as Stenotrophomomas maltophilia
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
5,6,7,8-tetrahydrofolate may serve primarily to trap formaldehyde as it is formed at the active site of the enzyme during sarcosine oxidation
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
heterotetramer
-
1 * 100000 + 1 * 42000 + 1 * 20000 + 1 * 6000, SDS-PAGE
heterotetramer
-
1 * 100000 + 1 * 44000 + 1 * 21000 + 1 *10000, SDS-PAGE
heterotetramer
-
1 * 110000 + 1 * 44000 + 1 * 21000 + 1 * 10000, SDS-PAGE
heterotetramer
-
1 * 110000 + 1 *44000 + 1 * 21000 + 1 * 10000, SDS-PAGE
heterotetramer
-
1 * 103000 + 1 * 44000 + 1 * 21000 + 1 * 10000, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with methylthioacetate, pyrrole 2-carboxylate and sulfite or sarcosine-reduced enzyme, using 0.1 M HEPES (pH 7.5) and 1.7 M ammonium sulfate
-
hanging drop vapor diffusion method, using 17-20% (w/v) PEG 20 K, 100 mM Tris, pH 8.5, 40 mM sodium furoate and 10 mM Na2SO3
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
native protein and the selenomethionine substituted protein, hanging drop vapor diffusion method, using about 17% (w/v) PEG 20000 with 100 mM Tris buffer (pH 8.5)
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C141S
-
the mutant exhibits specific activity values reduced to those of the wild type recombinant enzyme or the natural enzyme
C195S
-
the mutant exhibits specific activity values similar to those of the wild type recombinant enzyme or the natural enzyme
C351S
-
the mutant exhibits specific activity values similar to those of the wild type recombinant enzyme or the natural enzyme
G139A
-
the mutant of the alpha subunit is expressed only at low temperature (15°C), but the purified enzyme exhibits properties indistinguishable from the wild type enzyme
G30A
-
the mutant of the beta subunit exhibits subunit expression levels similar to those of the wild type enzyme, but the mutation blocks subunit assembly and covalent attachment of FMN
H175A
-
the mutant contains 1 mol of covalently bound flavin (FMN) and exhibits catalytic activity similar to the wild type enzyme
K358R
-
the mutant shows 0.07% activity and higher apparent Km for sarcosine than the wild type enzyme
Y269A
-
the mutant shows 10% activity compared to the wild type enzyme
Y271A
-
the mutant shows 0.0076% activity compared to the wild type enzyme
Y271F
-
the mutant shows 0.78% activity compared to the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
the enzyme activity is completely lost on heating at 45°C for 10 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no activity loss is detected after 3 cycles of freezing and thawing within 1 week
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, purified enzyme in 10 mM potassium phosphate, pH 8.0, at least 1 year, no loss of activity
-
0°C, purified enzyme in 10 mM potassium phosphate, pH 8.0, 2 weeks, no loss of activity
-
25°C, purified enzyme in 10 mM potassium phosphate, pH 8.0, 24 h, no loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DE-52 column chromatography, phenyl Sepharose column chromatography, and Q-Sepharose column chromatography
Arthrobacter sp. 1-IN
-
ammonium sulfate precipitation, Ultrogel AC A 34 Sepharose column chromatography, phenyl-Sepharose column chromatography, and DEAE-Sephacel column chromatography
-
ammonium sulfate precipitation, Ultrogel ACA 34 chromatography, DEAE-cellulose column chromatography, and Phenyl-Sepharose column chromatography
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
ammonium sulfate precipitation, Ultrogel AcA gel filtration, DEAE-cellulose column chromatography, hydroxyapatite column chromatography, and DEAE Sephacel column chromatography
-
DEAE-cellulose colum chromatography, QAE-Sephadex A-50 gel filtration, DEAE Sephadex A-50 gel filtration, Ultrogel AcA34 gel filtration, and creatine-AH-Sepharose 4B colum chromatography
-
phenyl-Sepharose column chromatography and Talon affinity resin column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli XL-1 Blue or BL21 (DE3) cells
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kvalnes-Krick, K.; Jorns, M.S.
Bacterial sarcosine oxidase comparison of two multisubunit enzymes containing both covalent and noncovalent flavin
Biochemistry
25
6061-6069
1986
Corynebacterium sp. P-1
brenda
Kvalnes-Krick, K.; Jorns, M.S.
Interaction of tetrahydrofolate and other folate derivatives with bacterial sarcosine oxidase
Biochemistry
26
7391-7395
1987
Corynebacterium sp. P-1
brenda
Zeller, H.D.; Hille, R.; Jorns, M.S.
Bacterial sarcosine oxidase identification of novel substrates and a biradical reaction intermediate
Biochemistry
28
5145-5154
1989
Corynebacterium sp. P-1
brenda
Chlumsky, L.J.; Zhang, L.; Ramsey, A.J.; Jorns, M.S.
Preparation and properties of recombinant corynebacterial sarcosine oxidase evidence for posttranslational modification during turnover with sarcosine
Biochemistry
32
11132-11142
1993
Corynebacterium sp. P-1
brenda
Chlumsky, L.J.; Sturgess, A.W.; Nieves, E.; Jorns, M.S.
Identification of the covalent flavin attachment site in sarcosine oxidase
Biochemistry
37
2089-2095
1998
Corynebacterium sp. P-1
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
1189-1198
2000
Arthrobacter sp. 1-IN
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
40
5352-5367
2001
Corynebacterium sp. P-1
brenda
Suzuki, H.; Kawamura-Konishi, Y.
Cysteine residues in the active site of Corynebacterium sarcosine oxidase
J. Biochem.
109
909-917
1991
Corynebacterium sp. U-96
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
799-815
2007
Corynebacterium sp. U-96
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
491-505
2010
Corynebacterium sp. U-96
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. U-96
brenda
Suzuki, M.
Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96
J. Biochem.
89
599-607
1981
Corynebacterium sp. U-96
brenda
Hayashi, S.; Suzuki, M.; Nakamura, S.
Chemical modification of Corynebacterium sarcosine oxidase role of sulfhydryl and histidyl groups
J. Biochem.
94
551-558
1983
Corynebacterium sp. U-96
brenda
Hayashi, S.
Mechanism of reduction of Corynebacterium sarcosine oxidase by dithiothreitol
J. Biochem.
95
1201-1207
1984
Corynebacterium sp. U-96
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
1000-1018
2006
Stenotrophomonas maltophilia
brenda
Hassan-Abdallah, A.; Zhao, G.; Eschenbrenner, M.; Chen, Z.W.; Mathews, F.S.; Jorns, M.S.
Cloning, expression and crystallization of heterotetrameric sarcosine oxidase from Pseudomonas maltophilia
Protein Expr. Purif.
43
33-43
2005
Stenotrophomonas maltophilia (Q3ZDQ8 and Q3ZDR0 and Q3ZDQ7 and Q3ZDQ9), Stenotrophomonas maltophilia DSM 2701 (Q3ZDQ8 and Q3ZDR0 and Q3ZDQ7 and Q3ZDQ9)
brenda
Yoneda, S.; Saito, T.; Nakajima, D.; Watanabe, G.
Potential of mean force and umbrella sampling simulation for the transport of 5-oxazolidinone in heterotetrameric sarcosine oxidase
Proteins
89
811-818
2021
Corynebacterium sp. U-96
brenda
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