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Information on EC 1.5.3.24 - sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)
for references in articles please use BRENDA:EC1.5.3.24
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.3 With oxygen as acceptor
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).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
showSynonyms
heterotetrameric sarcosine oxidase, HSO, sarcosine oxidase, sarcosine oxidase P, sarcosine: oxygen oxidoreductase (demethylating), sarcosine:oxygen oxidoreductase (demethylating), TSOX, more
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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
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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PATHWAY SOURCE
PATHWAYS
MetaCyc
glycine betaine degradation I
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-proline + O2
?
-
Substrates: poor substrate, the reduction of the enzyme with L-proline at pH 8.0 is not significant under aerobic conditions
Products: -
Products: -
?
methylthioacetate + 5,6,7,8-tetrahydrofolate + O2
?
-
Substrates: -
Products: -
Products: -
?
N-ethyl-glycine + 5,6,7,8-tetrahydrofolate + O2
?
-
Substrates: -
Products: -
Products: -
?
N-methyl-L-alanine + 5,6,7,8-tetrahydrofolate + O2
?
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + 2,6-dichlorophenolindophenol
?
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + ferricyanide
?
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + phenazine methosulfate
?
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5-formyltetrahydrofolate + O2
?
-
Substrates: -
Products: -
Products: -
?
sarcosine + pteroyltetraglutamate + O2
?
-
Substrates: -
Products: -
Products: -
?
sarcosine + tetrahydropteroyltetraglutamate + O2
?
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Stenotrophomonas maltophilia DSM 2701
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with NAD+ or NADP+ as electron acceptor in the presence or absence of various thiols (glutathione, coenzyme A, dithioerythritol)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-proline
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
-
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
Substrates: -
Products: -
Products: -
?
sarcosine + 5,6,7,8-tetrahydrofolate + O2
glycine + 5,10-methylenetetrahydrofolate + H2O2
Stenotrophomonas maltophilia DSM 2701
Q3ZDQ8; Q3ZDR0; Q3ZDQ7; Q3ZDQ9
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the enzyme contains both 1 mol of non-covalently bound FAD and 1 mol of covalently bound FAD per mol of enzyme
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 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
-
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
-
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Show AA Sequence and Transmembrane Helices (4177 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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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 * 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
-
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
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.
Mechanism of reduction of Corynebacterium sarcosine oxidase by dithiothreitol
J. Biochem.
95
1201-1207
1984
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
Kvalnes-Krick, K.; Schuman Jorns, M.
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.; Schuman Jorns, M.
Interaction of tetrahydrofolate and other folate derivates with bacterial sarcosine oxidase
Biochemistry
26
7391-7395
1987
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
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. 1IN
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
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
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
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.; 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
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
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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