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Information on EC 2.1.1.14 - 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P25665
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2.1.1.14 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferaseIUBMB Comments
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.
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Word Map
- 2.1.1.14
- methyltetrahydrofolate
-
cobalamin-dependent
- tetrahydrofolate
-
n5-methyl
-
overoxidation
-
s-bacillithiolation
- bacillithiol
- analysis
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
met-8, cobalamin-independent methionine synthase, cobalamin-independent methionine synthase (mete), methionine synthase mete, 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase, ppmete, atmete, 5-methyltetrahydropteroyltriglutamate-homocysteine s-methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase
-
homocysteine methylase
-
-
-
-
methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase
-
-
-
-
methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase
-
-
-
-
tetrahydropteroyltriglutamate methyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
mechanism
-
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
final step in methionine synthesis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
S-methylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -
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
9068-29-5
-
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
5-methyltetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate + L-homocysteine
tetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate + L-methionine
-
-
-
?
5-methyltetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate + L-homocysteine
tetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate + L-methionine
-
-
-
-
?
5-methyltetrahydropteroyl-tri-L-glutamate + L-homocysteine
tetrahydropteroyl-tri-L-glutamate + L-methionine
-
-
-
-
?
S-adenosylmethionine + L-selenohomocysteine
L-selenomethionine + S-adenosylhomocysteine
-
-
reaction catalyzed both by vitamin B12 dependent and independent enzyme
?
additional information
?
-
-
5-methyltetrahydropteroyl-alpha-glutamate or 5-methyl-tetrahydropteroyl-alpha-glutamylglutamate cannot replace the triglutamate folate derivative as methyl donor
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Zn2+
Mg2+
-
at low phosphate concentration, 0.1 mM, the Mg2+-stimulation is 4.5fold, smaller stimulation at higher concentrations of phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
5-methyltetrahydropteroyl-gamma-glutamyl-gamma-glutamylglutamate
-
at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.7
-
pH 6.0: about 70% of maximum activity, pH 8.7: about 90% of maximum activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50800
-
x * 50800, equilibrium sedimentation of carboxymethylated enzyme in 5 M guanidine-HCl
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 50800, equilibrium sedimentation of carboxymethylated enzyme in 5 M guanidine-HCl
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V39A/R46C/T106I/K713E
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 45°C. The mutant MetE enzymes display a reduced melting temperature but an enhanced in vivo stability
V39A/R46C/T106I/K713E/C645A
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 45°C. The mutant MetE enzymes display a reduced melting temperature but an enhanced in vivo stability
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guest, J.R.; Friedman, S.; Foster, M.A.; Tejerina, G.; Woods, D.D.
Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli
Biochem. J.
92
497-504
1964
Escherichia coli
Gonzalez, J.C.; Banerjee, R.V.; Huang, S.; Sumner, J.S.; Matthews, R.G.
Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problem
Biochemistry
31
6045-6056
1992
Escherichia coli
Zhou, Z.S.; Smith, A.E.; Matthews, R.G.
L-Selenohomocysteine: One-step synthesis from L-selenomethionine and kinetic analysis as substrate for methionine synthases
Bioorg. Med. Chem. Lett.
10
2471-2475
2000
Escherichia coli
Peariso, K.; Zhou, Z.S.; Smith, A.E.; Matthews, R.G.; Penner-Hahn, J.E.
characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy
Biochemistry
40
987-993
2001
Escherichia coli
Whitefield, C.D.; Steers, E.J.; Weissbach, H.
Purification and properties of 5-methyltetrahydropteroyltriglutamate-homocysteine transmethylase
J. Biol. Chem.
245
390-401
1970
Escherichia coli
Taylor, R.T.; Weissbach, H.
N5-Methyltetrahydrofolate-homocysteine methyltransferases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
9
121-165
1973
Auxenochlorella pyrenoidosa, Escherichia coli, Klebsiella aerogenes, Neurospora crassa, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium
-
Chu, J.; Shoeman, R.; Hart, J.; Coleman, T.; Mazaitis, A.; Kelker, N.; Brot, N.; Weissbach, H.
Cloning and expression of the metE gene in Escherichia coli
Arch. Biochem. Biophys.
239
467-474
1985
Escherichia coli
Gonzalez, J.C.; Peariso, K.; Penner-Hahn, J.E.; Matthews, R.G.
Cobalamin-independent methionine synthase from Escherichia coli: A zinc metalloenzyme
Biochemistry
35
12228-12234
1996
Escherichia coli
Hondorp, E.R.; Matthews, R.G.
Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli
PLoS Biol.
2
1738-1753
2004
Escherichia coli
Taurog, R.E.; Jakubowski, H.; Matthews, R.G.
Synergistic, random sequential binding of substrates in cobalamin-independent methionine synthase
Biochemistry
45
5083-5091
2006
Escherichia coli, Escherichia coli pJG816
Taurog, R.E.; Matthews, R.G.
Activation of methyltetrahydrofolate by cobalamin-independent methionine synthase
Biochemistry
45
5092-5102
2006
Escherichia coli
Pejchal, R.; Ludwig, M.L.
Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication
PLoS Biol.
3
e31
2005
Arabidopsis thaliana (O50008), Escherichia coli (P25665), Saccharomyces cerevisiae (P05694), Thermotoga maritima (Q9X112), Thermotoga maritima
Hondorp, E.R.; Matthews, R.G.
Oxidation of cysteine 645 of cobalamin-independent methionine synthase causes a methionine limitation in Escherichia coli
J. Bacteriol.
191
3407-3410
2009
Escherichia coli
Fujiwara, K.; Taguchi, H.
Mechanism of methionine synthase overexpression in chaperonin-depleted Escherichia coli
Microbiology
158
917-924
2012
Escherichia coli
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