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Information on EC 2.1.1.265 - tellurite methyltransferase and Organism(s) Escherichia coli and UniProt Accession P25397

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.265 tellurite methyltransferase
IUBMB Comments
The enzyme is involved in the detoxification of tellurite. It can also methylate selenite and selenium dioxide.
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This record set is specific for:
Escherichia coli
UNIPROT: P25397
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
TehB, tellurite-resistance S-adenosyl-L-methionine transferase protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tellurite-resistance S-adenosyl-L-methionine transferase protein
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tellurite methyltransferase
The enzyme is involved in the detoxification of tellurite. It can also methylate selenite and selenium dioxide.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + tellurite
S-adenosyl-L-homocysteine + methanetelluronate
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + tellurite
S-adenosyl-L-homocysteine + methanetelluronate
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
dependent on, the conserved motifs I and II in TehB are involved in S-adenosyl-L-methionine binding
S-adenosyl-L-methionine
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TehB is a SAM-dependent methyltransferase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sinefungin
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a cofactor analogue of S-adenosyl-L-methionine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene tehB
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
replacement of the conserved aspartate residue in motif I by asparagine or alanine, or of the conserved phenylalanine in motif II by tyrosine or alanine, decreases resistance to background levels
metabolism
the Escherichia coli chromosomal determinant for tellurite resistance consists of two genes tehA and tehB, which, when expressed on a multicopy plasmid, confer resistance to K2TeO3 at 0.128 mg/ml
physiological function
TehB utilizes a methyltransferase activity in the detoxification of tellurite
physiological function
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TehB is an S-adenosyl-l-methionine-dependent methyltransferase that detoxifies tellurite in bacteria, the cytoplasmic TehB is a tellurite-resistance protein
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26256
x * 26256, His6-tagged TehB, sequence caculation, x * 27000-28000, recombinant His6-tagged TehB, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer or dimer
x * 26256, His6-tagged TehB, sequence caculation, x * 27000-28000, recombinant His6-tagged TehB, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TehB complexed with S-adenosyl-L-methionine or sinefungin, hanging drop vapour diffusion method, mixing of 0.001 ml of protein and 0.001 ml of reservoir solution, the latter containing 0.1 M NaF and 16-18% PEG 3350, at 20°C, formation of sinefungin complex crystals by microseeding of crystals in reservoir solution containing 5 mM sinefungin, method optimization, X-ray diffraction structure determination and analysis at 1.9 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D36A
site-directed mutagenesis of a motif I residue, the tellurite resistance of the mutant is abolished
D36N
site-directed mutagenesis of a motif I residue, the tellurite resistance of the mutant is abolished
D59A
site-directed mutagenesis of a motif I residue, the tellurite resistance of the mutant is abolished
D97E
site-directed mutagenesis of a motif II residue, the tellurite resistance of the mutant is unaltered
D97N
site-directed mutagenesis of a motif II residue, the tellurite resistance of the mutant is partially reduced
F98A
site-directed mutagenesis of a motif II residue, the tellurite resistance of the mutant is abolished
F98Y
site-directed mutagenesis of a motif II residue, the tellurite resistance of the mutant is abolished
Y96A
site-directed mutagenesis of a motif II residue, the tellurite resistance of the mutant is partially reduced
additional information
mutagenesis by the two-stage PCR-based overlapping extension method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type TehB from Escherichia coli strains C41(DE3) and BL21(DE3), respectively, by nickel affinity chromatographhy
recombinant His-tagged enzyme with a TEV protease cleavage site from Escherichia coli strain BL21(DE3) PlysS by nickel affinity chromatography, cleavage of the His-tag, followed by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tehB, expression of His6-tagged wild-type enzyme in Escherichia coli strain coli C41(DE3), expression of the mutant TehB enzymes in tehAB operon from pTWT101, a pTZ19R clone, in Escherichia coli strain JM109, expression of His6-tagged mutant enzymes in Escherichia coli strain BL21(DE3)
gene tehB, expression as His-tagged enzyme with a TEV protease cleavage site in Escherichia coi strain BL21 (DE3) PlysS
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Choudhury, H.G.; Beis, K.
Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-L-methionine transferase protein TehB from Escherichia coli
Acta Crystallogr. Sect. F
66
1496-1499
2010
Escherichia coli, Escherichia coli MG1655
Manually annotated by BRENDA team
Liu, M.; Turner, R.J.; Winstone, T.L.; Saetre, A.; Dyllick-Brenzinger, M.; Jickling, G.; Tari, L.W.; Weiner, J.H.; Taylor, D.E.
Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance
J. Bacteriol.
182
6509-6513
2000
Escherichia coli (P25397)
Manually annotated by BRENDA team