Information on EC 2.1.1.14 - 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase

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

EC NUMBER
COMMENTARY hide
2.1.1.14
-
RECOMMENDED NAME
GeneOntology No.
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
S-methylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
L-methionine biosynthesis I
-
-
L-methionine biosynthesis II
-
-
L-methionine biosynthesis III
-
-
Metabolic pathways
-
-
methionine metabolism
-
-
S-adenosyl-L-methionine cycle I
-
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S-adenosyl-L-methionine cycle II
-
-
seleno-amino acid biosynthesis
-
-
Selenocompound metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine S-methyltransferase
Requires phosphate and contains zinc. The enzyme from Escherichia coli also requires a reducing system. Unlike EC 2.1.1.13, methionine synthase, this enzyme does not contain cobalamin.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-29-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Candida albicans ATCC MYA-2876
-
UniProt
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
strain pJG816
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Orobanche ramosa
Hemp broomrape
UniProt
Manually annotated by BRENDA team
Phaseolus sp.
bean
-
-
Manually annotated by BRENDA team
green string bean
-
-
Manually annotated by BRENDA team
pea, 2 enzyme forms: a 5-methyltetrahydropteroylglutamate dependent enzyme and a S-methylmethionine dependent enzyme
-
-
Manually annotated by BRENDA team
potato
-
-
Manually annotated by BRENDA team
spinach
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
5-methyltetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate + L-homocysteine
tetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate + L-methionine
show the reaction diagram
5-methyltetrahydropteroyl-gamma-glutamylglutamate + L-homocysteine
tetrahydropteroyl-gamma-glutamylglutamate + L-methionine
show the reaction diagram
5-methyltetrahydropteroyl-tri-L-glutamate + L-homocysteine
tetrahydropteroyl-tri-L-glutamate + L-methionine
show the reaction diagram
-
-
-
-
?
5-methyltetrahydropteroylmonoglutamate + L-homocysteine
tetrahydropteroylmonoglutamate + L-methionine
show the reaction diagram
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine
tetrahydropteroyltri-L-glutamate + L-methionine
show the reaction diagram
N5-methyltetrahydropteroylmonoglutamate + L-homocysteine
tetrahydropteroylmonoglutamate + L-methionine
show the reaction diagram
S-adenosylmethionine + homocysteine
methionine + S-adenosylhomocysteine
show the reaction diagram
-
-
-
?
S-adenosylmethionine + L-selenohomocysteine
L-selenomethionine + S-adenosylhomocysteine
show the reaction diagram
-
-
reaction catalyzed both by vitamin B12 dependent and independent enzyme
?
S-methylmethionine + homocysteine
methionine
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
below 1 mM more effective than Mg2+, above 1 mM inhibitory
phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-methyltetrahydropteroyl-alpha-glutamate
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-
Chloromethyl ketones
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-
Diamide
-
-
GSSG
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inactivates by glutathionylation at Cys645
High ionic strength
-
-
-
iodoacetamide
-
-
methionine
Mn2+
-
above 1 mM
Pteroyl-alpha-glutamylglutamic acid
-
-
Pteroyl-gamma-glutamyl-gamma-glutamylglutamic acid
-
-
Zinc
-
His647, Cys649 and Cys733 are involved in zinc coordination. Addition of L-homocysteine leads to reorganization of the zinc binding site with a stronger coordination to Cys649, Cys733, and a water molecule
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.094 - 0.12
5-methyltetrahydropteroyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamate
0.028 - 0.129
5-methyltetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate
0.109 - 0.113
5-methyltetrahydropteroyl-gamma-glutamylglutamate
0.000026
5-methyltetrahydropteroylglutamate
-
-
0.35
5-methyltetrahydropteroylmonoglutamate
-
-
0.0044 - 0.4
5-methyltetrahydropteroyltriglutamate
0.041 - 0.6
homocysteine
0.01 - 0.025
L-homocysteine
0.004
S-adenosylmethionine
-
-
0.0022 - 0.055
S-methylmethionine
0.016
selenohomocysteine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.417 - 0.6
5-methyltetrahydropteroyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamate
0.12 - 0.533
5-methyltetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate
0.283 - 0.35
5-methyltetrahydropteroyl-gamma-glutamylglutamate
0.33 - 0.45
L-homocysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
999
-
specific activity after growth in different media
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
L-methionine
7.9
Phaseolus sp.
-
L-methionine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 9
at pH 4.6: 0.0096 micromol/min/mg, at pH 6.5: 0.155 micromol/min/mg, at pH 9.0: 0.119 micromol/min/mg
6 - 8.5
-
-
6 - 8.7
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pH 6.0: about 70% of maximum activity, pH 8.7: about 90% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
calculated from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Orobanche ramosa
-
Manually annotated by BRENDA team
Orobanche ramosa
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Shewanella sp. (strain W3-18-1)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
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
75000
-
gel filtration, sedimentation data
80000
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SDS-PAGE
84000
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equilibrium ultracentrifugation
85000
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gel filtration, recombinant enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cocrystallization with L-homocysteine or met and ternary complexes with folate substrates, sitting drop method
-
binding of L-homocysteine or methionine results in conformational rearrangements at the amino acid binding pocket, moving the catalytic zinc into position to activate the thiol group. Active-site residues Asn126 and Tyr660 play key roles in catalysis
hanging drop vapour diffusion method
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hanging-drop vapor diffusion method
an unusual-barrel structure in which the active site lies between the tops of the two (betaalpha)8 barrels
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vapor batch (microbatch) method using 25% poly(ethylene glycol) 4000, 0.2 M ammonium sulfate, and 0.1 M sodium acetate (pH 4.6)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48.5
-
melting temperature, mutant V39A/R46C/T106I/K713E/C645A
51.3
-
melting temperature, mutant V39A/R46C/T106I/K713E
54.7
-
melting temperature, wild-type
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidative stress inactivates the enzyme
-
660332
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography
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DEAE Sepharose column chromatography
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HiTrap heparin column chromatography
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immobilized metal ion affinity chromatography (Ni2+), gel fitration
Ni2+-chelating chromatography, and S200 gel filtration
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rapid one-step purification
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Zn(II)-NTA column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
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expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3)Star cells
expressed in Escherichia coli strain K-12
-
expressed in Escherichia coli strain MTD23
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expressed in Saccharomyces cerevisiae strain DAY4.1
homologous expression and heterologous expression in Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dramatically induced by GroE depletion
-
the MET1gene is downregulated 2.4fold referred to germinated seeds in response to sucrose
Orobanche ramosa
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N126A
13% of wild-type activity
Y660A
no residual activity
Y660F
93% of wild-type activity
Y660Q
14% of wild-type activity
N126A
Candida albicans ATCC MYA-2876
-
13% of wild-type activity
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Y660A
Candida albicans ATCC MYA-2876
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no residual activity
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Y660F
Candida albicans ATCC MYA-2876
-
93% of wild-type activity
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Y660Q
Candida albicans ATCC MYA-2876
-
14% of wild-type activity
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C645A
-
the mutation confers resistance to diamide when cells are grown in media lacking methionine, but not when cells are grown in the presence of methionine, cysteine 645 serves to modulate the activity of MetE in vivo in response to disulfide stress
C726S
-
mutant does not contain zinc, no activity, probably due to lack of zinc
V39A/R46C/T106I/K713E
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mutant confers accelerated growth in the Escherichia coli K-12 WE strain in the presence of acetate. Strains harboring acetate-tolerant MetE mutants are less inhibited by homocysteine in L-isoleucine-enriched medium. The acetate-tolerant MetE mutants stimulate the growth of the host strain at elevated temperatures of 44 and 45C. The mutant MetE enzymes display a reduced melting temperature but an enhanced in vivo stability
V39A/R46C/T106I/K713E/C645A
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C645A mutation additionally improves acetate tolerance. Strains harboring acetate-tolerant MetE mutants are less inhibited by homocysteine in L-isoleucine-enriched medium. The acetate-tolerant MetE mutants stimulate the growth of the host strain at elevated temperatures of 44 and 45C. The mutant MetE enzymes display a reduced melting temperature but an enhanced in vivo stability
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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