Information on EC 2.8.4.3 - tRNA-2-methylthio-N6-dimethylallyladenosine synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.8.4.3
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RECOMMENDED NAME
GeneOntology No.
tRNA-2-methylthio-N6-dimethylallyladenosine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylsulfanyl-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
show the reaction diagram
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced electron acceptor = 2-sulfanyl-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
show the reaction diagram
S-adenosyl-L-methionine + 2-sulfanyl-N6-dimethylallyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-methylsulfanyl-N6-dimethylallyladenine37 in tRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
tRNA (N6-dimethylallyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-methylthiotransferase
This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur [3]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. The identity of the electron donor is not known.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
N6-dimethylallyladenine in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine
2-thio-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
S-adenosyl-L-methionine + 2-thio-N6-dimethylallyladenine37 in tRNA
S-adenosyl-L-homocysteine + 2-methylthio-N6-dimethylallyladenine37 in tRNA
show the reaction diagram
additional information
?
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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
N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine
2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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the enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes
[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[4Fe-4S]-center
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the sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. Presence of a [4Fe-4S]+2/+1 cluster under reducing and anaerobic conditions, whereas [3Fe-4S]+1 and [2Fe-2S]+2 forms are generated under aerobic conditions
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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x * 50000, SDS-PAGE
50710
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x * 50710, calculated from sequence
53600
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1 * 60000 SDS-PAGE, 1 * 53600, calculated, His-tagged recombinant protein
60000
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gel filtration, His-tagged recombinan protein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 60000 SDS-PAGE, 1 * 53600, calculated, His-tagged recombinant protein
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C150/154/157A
Show AA Sequence (17028 entries)
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