Information on EC 1.5.1.20 - methylenetetrahydrofolate reductase [NAD(P)H]

New: Word Map on EC 1.5.1.20
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.5.1.20
-
RECOMMENDED NAME
GeneOntology No.
methylenetetrahydrofolate reductase [NAD(P)H]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Carbon fixation pathways in prokaryotes
-
-
folate transformations I
-
-
folate transformations II
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
N10-formyl-tetrahydrofolate biosynthesis
-
-
One carbon pool by folate
-
-
reductive acetyl coenzyme A pathway I (homoacetogenic bacteria)
-
-
sulfopterin metabolism
-
-
tetrahydrofolate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
5-methyltetrahydrofolate:NAD(P)+ oxidoreductase
A flavoprotein (FAD). Menadione can also serve as an electron acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
71822-25-8
-
9028-69-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
ecotype Columbia, expression in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
Q7WQX3
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
USDA110
-
-
Manually annotated by BRENDA team
-
Q8FZN0
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
Cercocebus sp.
monkey
-
-
Manually annotated by BRENDA team
strain ATCC 23439
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain 113-3
-
-
Manually annotated by BRENDA team
expression in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
formerly Mesorhizobium loti
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain DAY4, two isoenzymes, encoded by the genes MET12 and MET13
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
synonym Sinorhizobium meliloti
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
mutations in the enzyme lead to hyperhomocysteinemia. A C677T polymorphism is associated with an increased risk for the development of cardiovascular disease, Alzheimer's disease, and depression in adults and of neural tube defects in the fetus
metabolism
-
the enzyme plays a key role in folate metabolism and in the homeostasis of homocysteine
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6R)-5,10-methylenetetrahydrofolate + NAD(P)H + H+
(6S)-5-methyltetrahydrofolate + NAD(P)+
show the reaction diagram
-
-
-
r
(6R,S)-5,10-methylenetetrahydrofolate + ?
?
show the reaction diagram
5,10-methylene-5,6,7,8-tetrahydropteroylpentaglutamate + reduced acceptor
(+)-5-methyl-5,6,7,8-tetrahydropteroylpentaglutamate + oxidized acceptor
show the reaction diagram
-
equilibrium lies far in favor of 5-methyl-5,6,7,8-tetrahydropteroylpentaglutamate formation, pentaglutamate form binds to the same enzyme site as monoglutamate form
menadione as acceptor for 5,10-methylene-5,6,7,8-tetrahydropteroylpentaglutamate formation
?
5,10-methylenetetrahydrofolate + acceptor
5-methyltetrahydrofolate + reduced acceptor
show the reaction diagram
5,10-methylenetetrahydrofolate + FADH2
5-methyltetrahydrofolate + FAD
show the reaction diagram
5,10-methylenetetrahydrofolate + NAD(P)H
5-methyltetrahydrofolate + NAD(P)+
show the reaction diagram
-
NADH is the preferred cofactor of the plant enzyme
-
-
r
5,10-methylenetetrahydrofolate + NAD(P)H + H+
5-methyltetrahydrofolate + NAD(P)+
show the reaction diagram
5,10-methylenetetrahydrofolate + NADH
5-methyltetrahydrofolate + NAD+
show the reaction diagram
5,10-methylenetetrahydrofolate + NADPH
5-methyltetrahydrofolate + NADP+
show the reaction diagram
5,10-methylenetetrahydrofolate + NADPH
?
show the reaction diagram
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
show the reaction diagram
5,10-methylenetetrahydrofolate + reduced ferredoxin
5-methyltetrahydrofolate + oxidized ferredoxin
show the reaction diagram
5-methyltetrahydrofolate + NAD+
5,10-methylenetetrahydrofolate + NADH
show the reaction diagram
5-methyltetrahydrofolate + NADP+
5,10-methylenetetrahydrofolate + NADPH
show the reaction diagram
5-methyltetrahydrofolate + oxidized menadione
5,10-methylenetetrahydrofolate + reduced menadione
show the reaction diagram
5-methyltetrahydropteroylmonoglutamate + 5,10-methylenetetrahydropteroylhexaglutamate
5,10-methylenetetrahydropteroylmonoglutamate + 5-methyltetrahydropteroylhexaglutamate
show the reaction diagram
-
-
-
r
NADH + menadione
NAD+ + reduced menadione
show the reaction diagram
-
-
-
-
-
NADPH + H+ + menadione
NADP+ + menadiol
show the reaction diagram
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
nitrate + reduced benzyl viologen
nitrite + benzyl viologen
show the reaction diagram
nitrate + reduced methyl viologen
nitrite + methyl viologen
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(6R)-5,10-methylenetetrahydrofolate + NAD(P)H + H+
(6S)-5-methyltetrahydrofolate + NAD(P)+
show the reaction diagram
Q5SLG6
-
-
-
r
5,10-methylenetetrahydrofolate + FADH2
5-methyltetrahydrofolate + FAD
show the reaction diagram
5,10-methylenetetrahydrofolate + NAD(P)H + H+
5-methyltetrahydrofolate + NAD(P)+
show the reaction diagram
5,10-methylenetetrahydrofolate + NADH
5-methyltetrahydrofolate + NAD+
show the reaction diagram
5,10-methylenetetrahydrofolate + NADPH
5-methyltetrahydrofolate + NADP+
show the reaction diagram
5,10-methylenetetrahydrofolate + NADPH
?
show the reaction diagram
5,10-methylenetetrahydrofolate + NADPH + H+
5-methyltetrahydrofolate + NADP+
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + reduced acceptor
5-methyltetrahydrofolate + oxidized acceptor
show the reaction diagram
5,10-methylenetetrahydrofolate + reduced ferredoxin
5-methyltetrahydrofolate + oxidized ferredoxin
show the reaction diagram
5-methyltetrahydrofolate + NAD+
5,10-methylenetetrahydrofolate + NADH
show the reaction diagram
-
-
-
-
r
5-methyltetrahydrofolate + NADP+
5,10-methylenetetrahydrofolate + NADPH
show the reaction diagram
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
-
flavin-dependent enzyme
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
iron-sulfur centre
-
enzyme contains 15.2 molecules iron and 19.5 molecules acid-labile sulfur as iron-sulfur clusters
Molybdenum
Zinc
-
2.3 molecules zinc per enzyme molecule
additional information
-
no evidence for participation of heavy metals ions in catalytic process
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-5-methyl-5,6,7,8-tetrahydropteroylpentaglutamate
-
inhibits at high concentrations
2,4-dihydroxyphenylacetic acid
-
at 0.01 M
5,10-methylenetetrahydrofolate
dicoumarol
-
inhibits menadione reductase activity only
diethyldicarbonate
-
20 mM NADP+ and 20 mM NAD+ partially protected the enzyme against inactivation whereas 20 mM nicotinamide gives complete protection
dihydrofolate
dihydropteroylhexaglutamate
-
-
dihydropteroylpolyglutamate
folylpolyglutamate
-
overview
-
LY309887
-
i.e. 6R-2,5-thienyl-5,10-dideazatetrahydrofolate monoglutamate
menadione
-
inhibits enzyme activity in yeast extracts
Mersalyl
-
80% inhibition at 1 mM
methylenetetrahydrofolate
-
-
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
-
-
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamylglutamic acid
-
-
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)glutamic acid
-
-
N-([5-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2,3-dihydrothiophen-2-yl]carbonyl)-4-methylideneglutamic acid
-
-
N-bromosuccinimide
-
inactivates the enzyme by modification of tryptophan
N-[4-[2-(2,4-diamino-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminopyrido[3,2-d]pyrimidin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2-fluorobenzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2-amino-4-methylquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
NADPH
-
100 mM
p-chloromercuribenzoate
-
60% inhibition of the methylenetetrahydrofolate reductase activity at 0.04 mM, 83% inhibition of the menadione reductase activity at 0.04 mM
Phenylglyoxal
-
-
Polyglutamate analogues
-
-
-
S-adenosyl-L-methionine
S-adenosylmethionine
tetrahydrofolate
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
A23187
-
treatment of cells results in increase in enzyme mRNA and protein
homocysteine
-
treatment of cells results in increase in enzyme mRNA and protein
inositol-requiring enzyme-1
-
the induction of MTHFR was also observed after overexpression of inositol-requiring enzyme-1
-
S-adenosylmethionine
-
stimulates
thapsigargin
-
treatment of cells results in increase in enzyme mRNA and protein
tunicamycin
-
treatment of cells results in increase in enzyme mRNA and protein
Valproic acid
-
300 mg/kg treatment increases MTHFR promoter activity 2.5fold and MTHFR mRNA and protein 3.7fold
additional information
-
induction of MTHFR is observed after overexpression of inositol-requiring enzyme IRE1 and is inhibited by a dominant-negative mutant of IRE1. Tranfection of c-Jun and its activators LiCl and sodium valproate increase MTHFR expression, whereas inhibitor of c-Jun SP600125 reduces activation; transfection of c-Jun and two activators of c-Jun (LiCl and sodium valproate) increase MTHFR expression, MTHFR mRNA is up-regulated by endoplasmic reticulum stress
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
(+)-5-methyl-5,6,7,8-tetrahydropteroylpentaglutamate
-
-
0.023
(+)-5-methyltetrahydrofolate
-
-
0.18
(6R)-5,10-methylenetetrahydrofolate
at pH 7.0 and 50C
0.0005 - 0.287
5,10-methylenetetrahydrofolate
0.019 - 0.16
5-methyltetrahydrofolate
0.0019
5-methyltetrahydropteroylhexaglutamate
-
-
0.033
5-methyltetrahydropteroylmonoglutamate
-
-
11.1
benzyl viologen
-
-
0.12
DL-5-methyltetrahydrofolate
-
-
0.0004 - 0.187
methylenetetrahydrofolate
0.0027 - 0.585
NADH
0.0073 - 0.049
NADPH
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 50
methylenetetrahydrofolate
10.4 - 160
NADH
26.7 - 160
NADPH
additional information
additional information
Escherichia coli
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 0.051
(+)-5-methyl-5,6,7,8-tetrahydropteroylpentaglutamate
-
-
0.16 - 0.873
5,10-methylenetetrahydrofolate
0.0065
dihydrofolate
-
-
0.000013
dihydropteroylhexaglutamate
-
-
0.061
methylenetetrahydrofolate
-
recombinant wild-type enzyme, pH 7.2, 4C
0.014
NADH
-
recombinant wild-type enzyme, pH 7.2, 4C, the mutant enzymes all show a Km below 0.0035 mM
0.2
S-adenosylmethionine
-
-
additional information
additional information
-
dihydropteroylpolyglutamate inhibitors with different numbers of glutamyl residues
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
Homo sapiens
-
-
0.0022
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamylglutamic acid
Homo sapiens
-
-
0.033
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)glutamic acid
Homo sapiens
-
-
0.0018
N-([5-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2,3-dihydrothiophen-2-yl]carbonyl)-4-methylideneglutamic acid
Homo sapiens
-
-
0.0035
N-[4-[2-(2,4-diaminopyrido[3,2-d]pyrimidin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
Homo sapiens
-
-
0.0012
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2-fluorobenzoyl]-4-methylideneglutamic acid
Homo sapiens
-
-
0.0016
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
Homo sapiens
-
-
additional information
N-[4-[2-(2,4-diamino-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]benzoyl]-4-methylideneglutamic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000424
-
liver homogenate
0.000094
-
wild-type, cell extract
0.00022
Cercocebus sp.
-
reverse reaction
0.000231
-
brain homogenate
0.00029
Cercocebus sp.
-
forward reaction
0.00071
-
forward reaction
0.001
-
reverse reaction
0.0017
-
muscle
0.0045
-
brain
0.0048
-
intestine
0.0082
-
kidney
0.0089
-
pancreas
0.0106
-
liver
0.1
-
-
0.367
-
-
0.413
-
-
1.2
-
-
6.92
-
recombinant enzyme
12.4
-
recombinant enzyme
153
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 6.4
-
formation of 5-methyltetrahydrofolate
6.3 - 6.9
-
-
6.5
-
NADPH-tetrahydrofolate oxidoreductase activity
6.6
-
methyltetrahydrofolate-menadione oxidoreductase activity
6.6 - 6.7
-
methylenetetrahydrofolate reductase reaction
6.8
-
-
7
-
assay at
7.1
-
menadione reductase reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 8.6
-
about 60% of activity maximum at pH 5.8, about 50% of activity maximum at pH 8.6, menadione reductase activity
6 - 8
-
pH 6: about 70% of activity maximum, pH 8: about 35% of activity maximum with 5-methyl-5,6,7,8-tetrahydropteroylmonoglutamate, about 65% of activity maximum with 5-methyl-5,6,7,8-tetrahydropteroylpentaglutamate
6.2 - 7.3
-
half-maximal activity at pH 6.2 and pH 7.3, methylenetetrahydrofolate reductase reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
-
methylenetetrahydrofolate reductase reaction, slow increase of activity between 25C and 45C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
-
dimeric enzyme, gel filtration
74500
-
calculated from amino acid sequence
75000
-
SDS-PAGE
77300
-
SDS-PAGE
108000
-
A177V mutant enzyme, gel filtration
124000
-
determination at pH 9, alpha2,beta2 enzyme form, PAGE
133000
-
tetrameric enzyme, gel filtration
136000
-
scanning transmission electron microscopy
141000
-
gel filtration
150000
-
gel filtration
170000 - 190000
-
gel filtration, single enzyme with methylenetetrahydrofolate reductase and dopamine methyltransferase activity
190000
-
wild type enzyme, gel filtration
210000
-
gel filtration
237000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
x-ray crystallography
homotetramer
-
4 * 33000
octamer
tetramer
additional information
-
alterations in the hydrophobic interactions by 1 M urea lead to dissociation of the native tetramer, resulting in stabilization of enzymatically active holoenzyme dimers, at 3 M urea followed by unfolding of the dimers to denatured monomers along with dissociation of FAD from the enzyme subunits, alterations of the electrostatic interactions by 1.2 M NaCl lead to dissociation of the enzyme into inactive, partially denatured dimers
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
treatment by alkaline phosphatase removes seven phosphoryl groups from enzyme. Treated enzyme is more active than native enzyme and less sensitive to inhibition by S-adenosylmethionie
additional information
-
protein sequence shows no obvious intracellular targeting sequences
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged wild-type and mutant E28Q
-
ligand-free mutant F223L and mutant F223L/E28Q in complex with methylenetetrahydrofolate, to 1.65 and 1.7 A resolution, respectively. folate is bound in a catalytically competent conformation, and L223 undergoes a conformational change similar to that observed for F223 in the E28Q-methylenetetrahydrofolate structure
-
mutant A177V, free and in complex with 5,10-dideazafolate analogue LY309887
-
hanging-drop vapor diffusion method. Structure of proteolyzed form of recombinant NapB at 1.25 A resolution
-
crystal structure determined at a resolution of 3.2 A
-
hanging drop vapor diffusion method, using 0.1 M sodium acetate buffer (NaOAc, pH 4.3,4.5), 1 M lithium chloride, 10% (w/v) polyethylene glycol 6000, 10-20% (v/v) glycerol, and 2-5% (v/v) dioxane, at 20C
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 7.6
-
at this pH-range enzyme is more stable in Tris-HCl than in triethanolamine-HCl or phosphate buffers
437714
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
5 min, 17% loss of activity
45
-
inactivation above
46
-
5 min, 53% loss of activity
49
-
5 min, 70% loss of activity
51
-
dimeric enzyme, 50% inactivatin at pH 7.2
58
-
tetrameric enzyme, 50% inactivatin at pH 7.2
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.005 mM FAD stabilizes enzyme during purification procedure
-
extremely sensitive to proteolysis
FAD stabilizes
-
folate and FAD stabilize the polymorphic mutant enzyme
-
inclusion of 10% glycerol during purification is essential for stability
-
methyltetrahydrofolate and S-adenosylmethionine protects enzyme from the loss of FAD after dilution
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen labile, half-life: less than 1 h in aerobic buffer, sodium dithionite prevents inactivation by oxygen
-
437713, 437714
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, several months, stable
-