Any feedback?
Information on EC 2.4.99.17 - S-adenosylmethionine:tRNA ribosyltransferase-isomerase
for references in articles please use BRENDA:EC2.4.99.17Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.99.17 S-adenosylmethionine:tRNA ribosyltransferase-isomeraseIUBMB Comments
The reaction is a combined transfer and isomerization of the ribose moiety of S-adenosyl-L-methionine to the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn. It is part of the queuosine biosynthesis pathway.
Specify your search results
Word Map
- 2.4.99.17
- nucleoside
-
hypermodified
-
penultimate
- 7-aminomethyl-7-deazaguanine
-
thermotoga
-
anticodon
- maritima
-
compelling
-
isomerization
-
trna-modifying
- trnatyr
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
+
+
7-aminomethyl-7-carbaguanosine34 in tRNA
=
+
+
epoxyqueuosine34 in tRNA
Synonyms
s-adenosylmethionine:trna ribosyltransferase-isomerase, quea enzyme, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
QueA
QueA enzyme
-
-
-
-
queuosine biosynthesis protein QueA
-
-
-
-
S-adenosylmethionine:tRNA ribosyltransferase-isomerase
S-adenosylmethionine:tRNA ribosyltransferase-isomerase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine34 in tRNA = L-methionine + adenine + epoxyqueuosine34 in tRNA
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing; L-methionine, adenine releasing)
The reaction is a combined transfer and isomerization of the ribose moiety of S-adenosyl-L-methionine to the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn. It is part of the queuosine biosynthesis pathway.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
149719-25-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
S-adenosyl-L-methionine + 7-(aminomethyl)-7-deazaguanine-tRNATyr
L-methionine + adenine + epoxyqueuosine-tRNATyr
-
-
-
-
?
S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine in tRNA
L-methionine + adenine + epoxyqueuosine in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine in tRNA(Asp)
L-methionine + adenine + epoxyqueuosine in tRNA(Asp)
-
-
-
-
ir
S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine34 in tRNA
L-methionine + adenine + epoxyqueuosine34 in tRNA
S-adenosyl-L-methionine + 7-aminomethyl-7-deazaguanine in minihelix RNA
L-methionine + adenine + epoxyqueuosine in minihelix RNA
-
efficient substrate
-
-
ir
S-adenosyl-L-methionine + 7-aminomethyl-7-deazaguanine in tRNA(Tyr)
L-methionine + adenine + epoxyqueuosine in tRNA(Tyr)
-
-
-
-
ir
S-adenosyl-L-methionine + 7-aminomethyl-7-deazaguanine34 in tRNA
L-methionine + adenine + epoxyqueuosine34 in tRNA
the enzyme catalyzes the formation of the 2,3-epoxy-4,5-dihydroxycyclopentane ring of the queuosine precursor epoxyqueuosine
-
-
?
S-adenosyl-L-methionine + 7-aminomethyl-7-deazaguanosine in tRNA
L-methionine + adenine + epoxyqueuosine in tRNA
-
-
-
-
ir
S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine34 in tRNA
L-methionine + adenine + epoxyqueuosine34 in tRNA
-
-
-
?
S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine34 in tRNA
L-methionine + adenine + epoxyqueuosine34 in tRNA
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
S-adenosyl-L-methionine + 7-aminomethyl-7-deazaguanine in tRNA(Tyr)
L-methionine + adenine + epoxyqueuosine in tRNA(Tyr)
-
-
-
-
ir
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenine
-
noncompetitive inhibition against S-adenosyl-L-methionine and 7-(aminomethyl)-7-deazaguanine-tRNATyr
epoxyqueuosine-tRNATyr
-
competitive inhibition against 7-(aminomethyl)-7-deazaguanine-tRNATyr and noncompetitive inhibition against S-adenosyl-L-methionine
L-methionine
-
uncompetitive inhibition versus 7-(aminomethyl)-7-deazaguanine-tRNATyr and noncompetitive inhibition against S-adenosyl-L-methionine
S-adenosylhomocysteine
-
competitive inhibition against S-adenosyl-L-methionine and noncompetitive inhibition against 7-(aminomethyl)-7-deazaguanine-tRNATyr
sinefungin
-
competitive inhibition against S-adenosyl-L-methionine and noncompetitive inhibition against 7-(aminomethyl)-7-deazaguanine-tRNATyr
Mg2+
-
Mg2+ in millimolar concentrations inhibits enzyme activity but has little or no effect in the submillimolar range
Mn2+
-
Mn2+ in millimolar concentrations inhibits enzyme activity but has little or no effect in the submillimolar range
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
7-(aminomethyl)-7-deazaguanine-tRNATyr
-
in 100 mM glycylglycine (pH 8.7), 100 mM KCl, 0.5 mM dithiothreitol, 100 mM EDTA, at 37°C
-
0.0377
7-aminomethyl-7-deazaguanine in minihelix RNA
-
in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C
-
0.0015
7-aminomethyl-7-deazaguanine in tRNA(Tyr)
-
in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C
-
0.098
S-adenosyl-L-methionine
-
in 100 mM glycylglycine (pH 8.7), 100 mM KCl, 0.5 mM dithiothreitol, 100 mM EDTA, at 37°C
0.1014
S-adenosyl-L-methionine
-
in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.245
7-aminomethyl-7-deazaguanine in minihelix RNA
-
in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C
-
0.042
7-aminomethyl-7-deazaguanine in tRNA(Tyr)
-
in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C
-
0.042
S-adenosyl-L-methionine
-
in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.67
7-aminomethyl-7-deazaguanine in minihelix RNA
-
in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C
-
28.3
7-aminomethyl-7-deazaguanine in tRNA(Tyr)
-
in 100 mM glycylglycine (pH 8.7), 100 mM EDTA, 100 mM KCl, 0.5 mM dithiothreitol, at 37°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
S-adenosylhomocysteine
-
competitive inhibition against 7-(aminomethyl)-7-deazaguanine-tRNATyr, in 100 mM glycylglycine (pH 8.7), 100 mM KCl, 0.5 mM dithiothreitol, 100 mM EDTA, at 37°C
0.133
S-adenosylhomocysteine
-
competitive inhibition against S-adenosyl-L-methionine, in 100 mM glycylglycine (pH 8.7), 100 mM KCl, 0.5 mM dithiothreitol, 100 mM EDTA, at 37°C
0.0046
sinefungin
-
competitive inhibition against S-adenosyl-L-methionine, in 100 mM glycylglycine (pH 8.7), 100 mM KCl, 0.5 mM dithiothreitol, 100 mM EDTA, at 37°C
0.0055
sinefungin
-
competitive inhibition against 7-(aminomethyl)-7-deazaguanine-tRNATyr, in 100 mM glycylglycine (pH 8.7), 100 mM KCl, 0.5 mM dithiothreitol, 100 mM EDTA, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.7
8.7
-
optimal activity at pH 8.7 in buffers containing various oxyanions, including acetate, carbonate, EDTA, and phosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
the enzyme catalyzes the penultimate step in the de novo biosynthesis of queuosine
metabolism
the enzyme is involved in the biosynthesis of the hypermodified tRNA nucleoside queuosine
Show AA Sequence and Transmembrane Helices (32087 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 100 mM Tris/HCl (pH 8.0), 200 mM (NH4)2SO4, 3 mM dithiothreitol, and 25-29% (w/v) PEG 4000
nanodroplet vapor diffusion method, using 12% (w/v) polyethylene glycol 4000, 0.1 M citric acid at pH 5.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, glutathione-Sepharose column chromatography, and MonoQ anion-exchange column chromatography
-
glutathione-Sepharose column chromatography and POROS HQ column chromatography
-
nickel-resin column chromatography, RESOURCE Q column chromatography, and Superdex 200 gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme is overexpressed as a fusion protein with the glutathione S-transferase from Schistosoma japonicum in Escherichia coli strain DH5alpha
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grimm, C.; Ficner, R.; Sgraja, T.; Haebel, P.; Klebe, G.; Reuter, K.
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase
Biochem. Biophys. Res. Commun.
351
695-701
2006
Bacillus subtilis (O32054), Bacillus subtilis
brenda
Slany, R.K.; Boesl, M.; Crain, P.F.; Kersten, H.
A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine
Biochemistry
32
7811-7817
1993
Escherichia coli
brenda
Van Lanen, S.G.; Iwata-Reuyl, D.
Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA)
Biochemistry
42
5312-5320
2003
Escherichia coli
brenda
Slany, R.K.; Boesl, M.; Kersten, H.
Transfer and isomerization of the ribose moiety of AdoMet during the biosynthesis of queuosine tRNAs, a new unique reaction catalyzed by the QueA protein from Escherichia coli
Biochimie
76
389-393
1994
Escherichia coli
brenda
Mueller, S.O.; Slany, R.K.
Structural analysis of the interaction of the tRNA modifying enzymes Tgt and QueA with a substrate tRNA
FEBS Lett.
361
259-264
1995
Escherichia coli
brenda
Van Lanen, S.G.; Kinzie, S.D.; Matthieu, S.; Link, T.; Culp, J.; Iwata-Reuyl, D.
tRNA modification by S-adenosylmethionine:tRNA ribosyltransferase-isomerase. Assay development and characterization of the recombinant enzyme
J. Biol. Chem.
278
10491-10499
2003
Escherichia coli
brenda
Kinzie, S.D.; Thern, B.; Iwata-Reuyl, D.
Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a ribosyl donor
Org. Lett.
2
1307-1310
2000
Escherichia coli
brenda
Mathews, I.; Schwarzenbacher, R.; McMullan, D.; Abdubek, P.; Ambing, E.; Axelrod, H.; Biorac, T.; Canaves, J.; Chiu, H.; Deacon, A.; DiDonato, M.; Elsliger, M.; Godzik, A.; Grittini, C.; Grzechnik, S.; Hale, J.; Hampton, E.; Han, G.; Haugen, J.; Hornsby,
Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold
Proteins
59
869-874
2005
Thermotoga maritima (Q9WZ44), Thermotoga maritima
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.4.99.17)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
Server: brenda6