Information on EC 2.1.1.13 - methionine synthase

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

EC NUMBER
COMMENTARY hide
2.1.1.13
-
RECOMMENDED NAME
GeneOntology No.
methionine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
folate transformations I
-
-
folate transformations II
-
-
L-methionine biosynthesis I
-
-
L-methionine biosynthesis III
-
-
L-methionine salvage from L-homocysteine
-
-
Metabolic pathways
-
-
methionine metabolism
-
-
N10-formyl-tetrahydrofolate biosynthesis
-
-
One carbon pool by folate
-
-
Selenocompound metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
5-methyltetrahydrofolate:L-homocysteine S-methyltransferase
Contains zinc and cobamide. The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II). Reactivation by reductive methylation is catalysed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system. For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8, [methionine synthase] reductase. In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2, ferredoxin---NADP+ reductase). Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, 5-methyltetrahydropteroyltriglutamate---homocysteine S-methyltransferase, which acts only on the triglutamate.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-23-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
African Green monkey, Cos-7, i.e. SV40-transformed kidney cells
-
-
Manually annotated by BRENDA team
Chromatium sp.
D
-
-
Manually annotated by BRENDA team
Chromatium sp. D
D
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
L. cv. Harunanijo
-
-
Manually annotated by BRENDA team
yellowtail
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Ochromonas malhamensis
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the interaction of methionine synthase with cytosolic cobalamin trafficking chaperone MMACHC may play a role in the regulation of the cellular processing of cobalamins that is required for cobalamin cofactor synthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-methyl-5,6,7,8-tetrahydropteroylheptaglutamate + homocysteine
?
show the reaction diagram
-
-
-
-
?
5-methyl-5,6,7,8-tetrahydropteroylpentaglutamate + L-homocysteine
?
show the reaction diagram
5-methyltetrahydrofolate + 2-mercaptoethanol
S-methylmercaptoethanol + tetrahydrofolate
show the reaction diagram
-
-
-
?
5-methyltetrahydrofolate + L-homocysteine
tetrahydrofolate + L-methionine
show the reaction diagram
N5-methyltetrahydrofolate + L-homocysteine
tetrahydrofolate + L-methionine
show the reaction diagram
N5-methyltetrahydropteroylheptaglutamate + L-homocysteine
tetrahydropteroylheptaglutamate + L-methionine
show the reaction diagram
-
-
-
-
?
N5-methyltetrahydropteroylmonoglutamate + L-homocysteine
tetrahydropteroylmonoglutamate + L-methionine
show the reaction diagram
N5-methyltetrahydropteroylpentaglutamate + L-homocysteine
tetrahydropteroylpentaglutamate + L-methionine
show the reaction diagram
N5-methyltetrahydropteroyltriglutamate + L-homocysteine
tetrahydropteroyltriglutamate + L-methionine
show the reaction diagram
S-adenosyl-L-methionine + L-homocysteine
methionine + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + L-selenohomocysteine
selenomethionine + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + tetrahydrofolate
5-methyltetrahydrofolate + S-adenosyl-L-homocysteine
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
5-methyltetrahydrofolate + L-homocysteine
tetrahydrofolate + L-methionine
show the reaction diagram
N5-methyltetrahydrofolate + L-homocysteine
tetrahydrofolate + L-methionine
show the reaction diagram
-
transcription is not regulated by Met, but is enhanced by homocysteine and repressed by choline and betaine. Synthesis of the enzyme is also regulated posttranscriptionally
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
required
Cobalamin
cobinamide
FAD
-
enzyme requires reduced FAD and S-adenosyl-L-methionine
S-adenosyl-L-methionine
vitamin B12
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
-
Cu
-
1:1 stoichiometry with Co
additional information
-
no other metals except for Co
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-methyl-5-amino-benzimidazole
-
IC50: more than 0.15 mM
1-methyl-5-nitro-7-methoxybenzimidazole
-
IC50: 0.15 mM
1-methyl-5-nitro-benzimidazole
-
IC50: more than 0.15 mM
1-methylbenzimidazole
-
IC50: more than 0.15 mM
2,1,3-benzothiadiazole
-
IC50: more than 0.15 mM
2-nitro-1H-benzimidazole
-
IC50: 0.12 mM
4-(7-nitroquinoxalin-2-yl)benzoic acid
mixed inhibition type
-
4-amino-2,1,3-benzothiadiazole
-
IC50: more than 0.15 mM
4-nitro-2,1,3-benzothiadiazole
-
IC50: 0.08 mM
4-nitro-N-[2-(5-nitro-1H-benzimidazol-2-yl)ethyl]benzamide
competitive inhibition
-
5-amino-7-methoxy-N1-methylbenzimidazole
-
IC50: 0.095 mM
5-amino-7-methoxybenzimidazole
-
IC50: more than 0.15 mM
5-aminobenzimidazole
-
IC50: more than 0.15 mM
5-methoxybenzimidazole
-
IC50: more than 0.15 mM
5-nitro-7-methoxybenzimidazole
-
IC50: 0.1 mM
benzimidazole
-
IC50: more than 0.15 mM
N-(3-bromo-4-[[(1-[2-[(2,2-dimethylpropanoyl)amino]-4-methyl-6-oxo-1,6-dihydropyrimidin-5-yl]aziridin-2-yl)methyl](methyl)amino]benzoyl)-L-glutamic acid
-
-
N-[(5-nitro-1H-benzimidazol-2-yl)methyl]benzamide
mixed inhibition type
-
ZL-031
-
i.e. diethyl N-[4-[(2-[2,4-diamino-5-(2,3-dibromopropane)-5,6,7,8-tetrahydropyrido(3,2-d)pyrimidin-6-yl]methyl)amino]3-bromo-benzoyl]L-glutamate
ZL-033
-
i.e. N-[4-[(2-[2,4-diamino-5-(2,3-dibromopropane)-5,6,7,8-tetrahydropyrido(3,2-d)pyrimidin-6-yl]methyl)amino]3-bromo-benzoyl]L-glutamic acid
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aquacob(III)alamin
-
the addition of 0.05 mM aquacob(III)alamin to the crude extract results in an about 13fold increase in activity which is not greatly affected by the addition of cytochrome P450 reductase or reductase domain of neuronal nitric oxide synthase
cadaverine
-
up to 40% stimulation at 1 mm
cyanocobalamin
K+
-
at 67 mM 1.4 fold activity
Li+
-
at 67 mM, 1.3fold activity
methionine synthase reductase
-
restores the activity of human methionine synthase through reductive methylation of methionine synthase-bound cob(II)alamin. Oxidized methionine synthase reductase does not reactivate methionine synthase, the presence of methionine synthase reductase along with AqCbl or MeCbl causes a dramatic increase in methionine synthase activity (7fold for AqCbl and 20fold for MeCbl) as compared to the cofactor alone
-
methylcob(III)alamin
-
the addition of 0.05 mM methylcob(III)alamin to the crude extract results in an about 6fold increase in activity which is not greatly affected by the addition of cytochrome P450 reductase or reductase domain of neuronal nitric oxide synthase
Na+
-
at 67 mM 1.5 fold activity
NADPH
-
reactivation of methionine synthase is dependent on NADPH concentration in a hyperbolic manner with maximum activity at about 0.2 mM
NH4+
-
at 67 mM 1.5 fold activity
putrescine
-
up to 50% stimulation at 1 mm
S-adenosyl-L-methionine
-
required
S-adenosylmethionine
-
at about 0.0001 mM
spermidine
-
up to 2.5 fold stimulation at 1 mm
spermine
-
up to 4 fold stimulation at 1 mm
TrisHCl
-
at 67 mM 1.2 fold activity
vitamin B12
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0223
5-Methyl-5,6,7,8-tetrahydropteroylheptaglutamate
-
-
0.013 - 0.0731
5-methyl-5,6,7,8-tetrahydropteroylmonoglutamate
0.004 - 0.0277
5-Methyl-5,6,7,8-tetrahydropteroylpentaglutamate
0.0244
5-methyl-5,6,7,8-tetrahydropteroyltriglutamate
-
-
2.4
5-methyltetrahydropteroylglutamate
-
-
0.0026 - 0.43
L-homocysteine
0.017
L-Selenohomocysteine
-
-
0.03 - 0.06
methyltetrahydrofolate
0.089
N5-methyltetrahydrofolate
-
-
0.025 - 0.165
N5-methyltetrahydropteroylmonoglutamate
0.00065 - 0.0016
S-adenosyl-L-methionine
0.035
S-methyltetrahydrofolate
-
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.33 - 13
5-methyltetrahydrofolate
Escherichia coli
-
-
0.0217 - 0.0367
S-adenosyl-L-methionine
additional information
additional information
Homo sapiens
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
2-nitro-1H-benzimidazole
-
in 50 mM phosphate buffer, pH 7.4, at 37C
0.017
4-nitro-2,1,3-benzothiadiazole
-
in 50 mM phosphate buffer, pH 7.4, at 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
1-methyl-5-amino-benzimidazole
0.12
2-nitro-1H-benzimidazole
Rattus norvegicus
-
IC50: 0.12 mM
0.009
4-(7-nitroquinoxalin-2-yl)benzoic acid
Rattus norvegicus
Q9Z2Q4
pH 7.4, 37C
-
0.15
4-amino-2,1,3-benzothiadiazole
Rattus norvegicus
-
IC50: more than 0.15 mM
0.08
4-nitro-2,1,3-benzothiadiazole
Rattus norvegicus
-
IC50: 0.08 mM
0.018
4-nitro-N-[2-(5-nitro-1H-benzimidazol-2-yl)ethyl]benzamide
Rattus norvegicus
Q9Z2Q4
pH 7.4, 37C
-
0.095
5-amino-7-methoxy-N1-methylbenzimidazole
Rattus norvegicus
-
IC50: 0.095 mM
0.15
5-amino-7-methoxybenzimidazole
0.1
5-nitro-7-methoxybenzimidazole
Rattus norvegicus
-
IC50: 0.1 mM
0.15
benzimidazole
Rattus norvegicus
-
IC50: more than 0.15 mM
0.00415
N-(3-bromo-4-[[(1-[2-[(2,2-dimethylpropanoyl)amino]-4-methyl-6-oxo-1,6-dihydropyrimidin-5-yl]aziridin-2-yl)methyl](methyl)amino]benzoyl)-L-glutamic acid
Homo sapiens
-
pH 7.2, 37C
0.02
N-[(5-nitro-1H-benzimidazol-2-yl)methyl]benzamide
Rattus norvegicus
Q9Z2Q4
pH 7.4, 37C
-
0.01
ZL-031
Homo sapiens
-
at 37C
0.0014
ZL-033
Homo sapiens
-
at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00017
-
muscle
0.00043
-
intestine
0.0005
-
recombinant enzyme from crude extract, in 0.2 M potassium phosphate buffer (pH 7.2), at 37C
0.0023
-
pancreas
0.003
-
brain
0.0073
-
kidney
0.0327
-
liver
1.54
-
recombinant enzyme after 3669fold purification, in 0.2 M potassium phosphate buffer (pH 7.2), at 37C
1.94
-
after 279fold purification at 37C
2.53
-
crude cell extract at 37C
9.3 - 11.7
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.2
-
-
7.5 - 7.8
Chromatium sp.
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
pH 6.0: about 75% of maximum activity, pH 7.5: about 35% of activity maximum
6.2 - 8.2
-
pH about 50% of maximum activity at pH 6.2 and 8.2
6.5 - 8.3
Chromatium sp.
-
pH 6.5: about 30% of maximum activity, pH 8.3: about 85% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 39
-
10C: about 10% of maximum activity, 39C: maximum activity
15 - 31
-
15C: about 10% of maximum activity, 31C: maximum activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
adenocyrcinoma cell line
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
S180 cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
-
distribution in tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
18% of total activity
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)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36200
-
sedimentation in high salt buffer
40000
-
gel filtration
86000
-
SDS-PAGE
112000
-
GST fusion protein, SDS-PAGE
140000 - 150000
-
gel filtration, sedimentation coefficient in sucrose density gradients
140000
-
sucrose density gradient centrifugation
150000
-
gel filtration
151000 - 155000
-
gel filtration
153000
-
gel filtration
160000
-
gel filtration
186000
-
gel filtration
200000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 40000, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3.0 A structure of a 65000 Da C-terminal fragment of methionine synthase that spans the cobalamin- and the S-adenosylmethionine-binding domains, arranged in a conformation suitable for the methyl transfer from S-adenosylmethionine to cobalamin that occurs during activation
-
cobalamin-binding domain
-
hanging drop vapor diffusion method using 0.2 M potassium nitrate, 18% (w/v) PEG3350, or microbatch vapor diffusion method using 0.2 M potassium nitrate, 20% (w/v) PEG3350, 50 mM HEPES pH 7.5
-
the 65-kDa I690C/G743C MetH fragment is crystallized by the microbatch method, using 0.2 M potassium nitrate and 20% (w/v) PEG3350
-
sitting drop vapour diffusion method in reservoir solution of 0.1 M Tris/HCl pH 7.5 containing 0.1-0.4 M sodium acetate, 10-12% poly(ethylene glycol) 8000 and 10-12% poly(ethyleneglycol) 1000
-
docking studies for inhibitors 4-(7-nitroquinoxalin-2-yl)benzoic acid, N-[(5-nitro-1H-benzimidazol-2-yl)methyl]benzamide, and 4-nitro-N-[2-(5-nitro-1H-benzimidazol-2-yl)ethyl]benzamide. Polar residues within the binding site of 5-methyltetrahydrofolate, namely, Asn404, Asn458, Asp525, Asn567, and Arg579, are critical for the interaction with substrate
design and preparation of myoglobin reconstituted with the cobalt corrinoid complex, Co(TDHC) as a simple model for the active site. In the heme pocket of myoglobin, CoII(TDHC) is tightly bound and provides a model of the baseoff/His-on state of the cobalamin binding domain of methionine synthase, and the intermediate, the tetra-coordinated Co(I) species, is detectable in the protein matrix
synthetic construct
-
hanging drop vapor diffusion method, using 25% 1,2-propanediol, 10% (v/v) glycerol, 5% (w/v) PEG 3000, 100 mM potassium citrate, pH 4.8, 15% (v/v) 1,2,3-heptanetriol, and 100 mM YCl3 (final pH, 5.2), at 4C
-
hybrid quantum mechanics/molecular mechanics computations reveal the traditionally assumed SN2 mechanism for formation the CH3-cob(III)alamin resting state. The activation energy barrier for the SN2 reaction is 8-9 kcal/mol, which is comparable with respect to the determined experimental rate constant. Alternatively, an electron transfer based radical mechanism is possible, where first an electron transfer from His-on cob(I)alamin to the pterin ring of the protonated CH3-H4-folate takes place, forming the CoII(d7)-pterin radical diradical state, followed by a methyl radical transfer. The major advantage of electron transfer is that a methyl radical can be transferred at a longer distance, which does not require the close proximity of two binding modules of MetH as does the SN2 type. The protonation event must take place either prior to or during the methyl transfer reaction in a ternary complex
sitting drop vapour diffusion method, crystal structures of the N-terminal substrate-binding module of the enzyme and their complexes with the substrates L-homocysteine and 5-methyltetrahydrofolate
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
stability optimum, 0C, t1/2: 6 days
441185
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetone inactivates
-
apoenzyme is very unstable, may be stabilized by forming a complex with methylcobalamin
-
freezing and thawing, 40% loss of activity
-
homocysteine, 0.01 M, stabilizes
-
mercaptoethanol, 0.2 M, inactivation after 2 h at 24C or during freezing and thawing, no effect at 0C
-
precipitation at pH 5 inactivates
-
rapid loss of activity in frozen state
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 15-20 mg/ml protein, stable for at least 1 month
-
-20C, ammonium sulfate paste containing homocysteine
-
-80C, methylated enzyme
-
0C, glutathione, N2-atmosphere, stable for at least a week
-
0C, pH 7, half-life 6 days
-
4C, 20% loss of activity after 2 weeks
-
freeze-dried, 20% loss of activity after 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
cobalamin affinity chromatography
-
DEAE cellulose batch chromatography and Q-sepharose column chromatography
-
glutathione agarose column chromatography
-
Hi-Trap column chromatography and MonoQ column chromatography
-
Ni-charged HiTrap chelating column chromatography and Mono Q column chromatography
-
Ni-NTA resin HisTrap column chromatography, HiPrep Q Sepharose column chromatography, and Resource Q column chromatography
-
nickel affinity chromatography using a Hi-Trap and a MonoQ column
-
partial
preparation of different cobalamin forms
-
Q-Sepharose column chromatography and cobalamin affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a GST fusion protein in Saccharomyces cerevisiae strain SDYalpha
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli Hms174(DE3) cells
-
expressed in Pichia pastoris cells
-
expressed in Sf9 insect cells
-
mutant enzymes I690C/G743C and I690C/G743C/Y1139 are expressed in Escherichia coli Hms174(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Glycine N-methyltransferase disruption significantly reduces hepatic expression
-
high expression in tumor cells
-
maximum mRNA accumulations of methionine synthase MS1 is attained in the evening
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D504A
-
the mutant exhibits 4% of wild type activity
D504N
-
the mutant exhibits 11% of wild type activity
D504S
-
the mutant exhibits 7% of wild type activity
D614A
-
the mutant exhibits less than 2% of wild type activity
D614N
-
the mutant exhibits less than 2% of wild type activity
D614S
-
the mutant exhibits 11% of wild type activity
E620Q
-
the mutation has no effect on enzyme activity
E620S
-
the mutation has no effect on enzyme activity
H128N
-
the mutant is 5fold less active compared to the wild type GST fusion protein
R530A
-
the mutant exhibits 33% of wild type activity
S448A
-
the mutant exhibits 67% of wild type activity
W576F
-
the mutant is 3fold less active compared to the wild type GST fusion protein
W576Y
-
the mutant is 8fold less active compared to the wild type GST fusion protein
Y527F
-
the mutant exhibits 67% of wild type activity
Cys310Ser
-
contains less than 0.05 equiv. of zinc, no proton release upon incubation with L-homocysteine, no enzymativc activity of holoenzyme
Cys311Ser
-
contains less than 0.05 equiv. of zinc, no proton release upon incubation with L-homocysteine, no enzymativc activity of holoenzyme
I690C/G743C
I690C/G743C/Y1139F
-
the I690C/G743C MetH variant is trapped in the activation conformation
Y1139F
-
the mutation lowers the cobalamine reduction potential from -490 mV to -540 mV
D963E /K1071N
-
reduced activity
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
incubation of resolved apoenzyme with methyl-B12 results in spontaneous formation of holoenzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
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