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Information on EC 1.7.1.13 - preQ1 synthase and Organism(s) Escherichia coli and UniProt Accession Q46920

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IUBMB Comments
The reaction occurs in the reverse direction. This enzyme catalyses one of the early steps in the synthesis of queuosine (Q-tRNA), and is followed by the action of EC 2.4.2.29, queuine tRNA-ribosyltransferase. Queuosine is found in the wobble position of tRNAGUN in Eukarya and Bacteria and is thought to be involved in translational modulation. The enzyme is not a GTP cyclohydrolase, as was thought previously based on sequence-homology studies.
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This record set is specific for:
Escherichia coli
UNIPROT: Q46920
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
nitrile reductase, 7-cyano-7-deazaguanine reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
queuine synthase
-
-
-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase
The reaction occurs in the reverse direction. This enzyme catalyses one of the early steps in the synthesis of queuosine (Q-tRNA), and is followed by the action of EC 2.4.2.29, queuine tRNA-ribosyltransferase. Queuosine is found in the wobble position of tRNAGUN in Eukarya and Bacteria [2] and is thought to be involved in translational modulation. The enzyme is not a GTP cyclohydrolase, as was thought previously based on sequence-homology studies.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one + 2 NADPH + 2 H+
2-amino-5-amino-methyl-pyrrolo[2,3-d]pyrimidin-4-one + 2 NADP+
show the reaction diagram
natural substrate
-
-
?
2-amino-5-cyanopyrrolo[2,3-d]pyrimidine + 2 NADPH + 2 H+
2-amino-5-amino-methyl-pyrrolo[2,3-d]pyrimidine + 2 NADP+
show the reaction diagram
analogue of natural substrate, poor substrate
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-
?
5-cyanopyrrolo[2,3-d]pyrimidin-4-one + 2 NADPH + 2 H+
5-amino-methyl-pyrrolo[2,3-d]pyrimidin-4-one + 2 NADP+
show the reaction diagram
analogue of natural substrate
-
-
?
7-cyano-7-carbaguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carbaguanine + 2 NADP+
show the reaction diagram
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-
-
-
?
7-cyano-7-deazaguanine + NADPH + H+
queuine + NADP+ + H+
show the reaction diagram
-
-
-
-
?
7-cyano-7-carba-2-deaminoguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carba-2-deaminoguanine + 2 NADP+
show the reaction diagram
-
-
-
-
?
7-cyano-7-carbaguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carbaguanine + 2 NADP+
show the reaction diagram
-
-
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
show the reaction diagram
additional information
?
-
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
2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one + 2 NADPH + 2 H+
2-amino-5-amino-methyl-pyrrolo[2,3-d]pyrimidin-4-one + 2 NADP+
show the reaction diagram
Q46920
natural substrate
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
show the reaction diagram
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late step in biosynthesis of the modified tRNA nucleoside queuosine
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7-formyl-7-deazaguanine
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carbonyl analogue of the imine intermediate, recognized by QueF as weak ligand for binding but not as substrate for reduction or oxidation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0061
2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
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wild-type, pH 7.5, 25°C
0.176
5-cyanopyrrolo[2,3-d]pyrimidin-4-one
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wild-type, pH 7.5, 25°C
0.0015
7-cyano-7-deazaguanine
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or below, pH 7.0, 37°C
0.0002 - 0.006
NADPH
0.05
7-cyano-7-carba-2-deaminoguanine
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pH 7.5, 25°C
0.001
7-cyano-7-carbaguanine
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below 1 microM, pH 7.5, 25°C
0.0078 - 0.036
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
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wild-type, pH 7.5, 25°C
0.05
5-cyanopyrrolo[2,3-d]pyrimidin-4-one
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wild-type, pH 7.5, 25°C
0.127
7-cyano-7-deazaguanine
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pH 7.0, 37°C
0.0033 - 0.142
NADPH
0.14
7-cyano-7-carba-2-deaminoguanine
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pH 7.5, 25°C
0.12
7-cyano-7-carbaguanine
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pH 7.5, 25°C
0.01
NADPH
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
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substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant E230Q, pH 7.5, 25°C
3.8
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substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant S90A, pH 7.5, 25°C
4.4
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substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant E230Q, pH 7.5, 25°C
8.7
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substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant F228W, pH 7.5, 25°C
10.8
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substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant F228W, pH 7.5, 25°C
12.9
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substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant S90A, pH 7.5, 25°C
14.3
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substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant H229A, pH 7.5, 25°C
17.9
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substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant H229A, pH 7.5, 25°C
90
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substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, wild-type, pH 7.5, 25°C
117
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substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, wild-type, pH 7.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
Tris-buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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mass spectroscopy
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
construction of homology model and docking studies of natural and non-natural substrates. Residues C190 and D197 play an essential role in the catalytic mechanism
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C190A
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complete loss of activity
D197N
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complete loss of activity
E230Q
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about 4% of wild-type activity for natural substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
F228W
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about 8% of wild-type activity for natural substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
H229A
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about 15% of wild-type activity for natural substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
Q89A
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poor activity
Q89L
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poor activity
S90A
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about 10% of wild-type activity for natural substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
C190A
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mutation in catalytic residue, no evidence of covalent binding of substrate preQ0. Mutant displays proton uptake
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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4 h, no loss of activity
724879
9
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4 h, 80% residual activity
724879
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
half-life 28.2
40
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half-life 12.8
45
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half-life 2.8
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 1 year, 1% residual activity
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
overproduction in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okada, N.; Noguchi, S.; Nishimura, S.; Ohgi, T.; Goto, T.; Crain, P.F.; McCloskey, J.A.
Structure determination of a nucleoside Q precursor isolated from E. coli tRNA: 7-(aminomethyl)-7-deazaguanosine
Nucleic Acids Res.
5
2289-2296
1978
Escherichia coli
Manually annotated by BRENDA team
Noguchi, S.; Yamaizumi, Z.; Ohgi, T.; Goto, T.; Nishimura, Y.; Hirota, Y.; Nishimura, S.
Isolation of Q nucleoside precursor present in tRNA of an E. coli mutant and its characterization as 7-(cyano)-7-deazaguanosine
Nucleic Acids Res.
5
4215-4223
1978
Escherichia coli
Manually annotated by BRENDA team
van Lanen, S.G.; Reader, J.S.; Swairjo, M.A.; de Crecy-Lagard, V.; Lee, B.; Iwata-Reuyl, D.
From cyclohydrolase to oxidoreductase: discovery of nitrile reductase activity in a common fold
Proc. Natl. Acad. Sci. USA
102
4264-4269
2005
Bacillus subtilis, Escherichia coli
Manually annotated by BRENDA team
Wilding, B.; Winkler, M.; Petschacher, B.; Kratzer, R.; Egger, S.; Steinkellner, G.; Lyskowski, A.; Nidetzky, B.; Gruber, K.; Klempier, N.
Targeting the substrate binding site of E. coli nitrile reductase QueF by modeling, substrate and enzyme engineering
Chemistry
19
7007-7012
2013
Escherichia coli, Escherichia coli (Q46920)
Manually annotated by BRENDA team
Moeller, K.; Nguyen, G.S.; Hollmann, F.; Hanefeld, U.
Expression and characterization of the nitrile reductase queF from E. coli
Enzyme Microb. Technol.
52
129-133
2013
Escherichia coli (Q46920)
Manually annotated by BRENDA team
Gjonaj, L.; Pinkse, M.; Fernandez-Fueyo, E.; Hollmann, F.; Hanefeld, U.
Substrate and cofactor binding to nitrile reductase A mass spectrometry based study
Catal. Sci. Technol.
6
7391-7397
2016
Escherichia coli (Q46920)
-
Manually annotated by BRENDA team
Jung, J.; Czabany, T.; Wilding, B.; Klempier, N.; Nidetzky, B.
Kinetic analysis and probing with substrate analogues of the reaction pathway of the nitrile reductase QueF from Escherichia coli
J. Biol. Chem.
291
25411-25426
2016
Escherichia coli
Manually annotated by BRENDA team
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