HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.7.1.13 - preQ1 synthase
for references in articles please use BRENDA:EC1.7.1.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.7.1.13 preQ1 synthaseIUBMB 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, tRNA-guanosine34 transglycosylase. 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.
Specify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
7-aminomethyl-7-carbaguanine:NADP+ oxidoreductase, 7-cyano-7-deazaguanine reductase, NADPH-dependent 7-cyano-7-deazaguanine reductase, nitrile reductase, NRed, preQ0 reductase, preQ0oxidoreductase, QueF, queuine synthase, YkvM, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
7-cyano-7-deazaguanine reductase
NADPH-dependent 7-cyano-7-deazaguanine reductase
nitrile reductase
NRed
QueF
queuine synthase
-
-
-
-
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
7-aminomethyl-7-carbaguanine + 2 NADP+ = 7-cyano-7-carbaguanine + 2 NADPH + 2 H+
This enzyme catalyses one of the early steps in the synthesis of queosine (Q-tRNA), and is followed by the action of EC 2.4.2.29, queuine tRNA-ribosyltransferase. Queosine 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.
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, tRNA-guanosine34 transglycosylase. 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.
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
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+
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+
analogue of natural substrate, poor substrate
-
-
?
5-cyanopyrrolo[2,3-d]pyrimidin-4-one + 2 NADPH + 2 H+
5-amino-methyl-pyrrolo[2,3-d]pyrimidin-4-one + 2 NADP+
analogue of natural substrate
-
-
?
7-cyano-7-carba-2-deaminoguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carba-2-deaminoguanine + 2 NADP+
-
-
-
-
?
7-cyano-7-carbaguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carbaguanine + 2 NADP+
-
-
-
-
?
7-cyano-7-carbaguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carbaguanine + 2 NADP+
J7KT48
-
-
-
?
7-cyano-7-carbaguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carbaguanine + 2 NADP+
J7KT48
-
-
-
?
7-cyano-7-carbaguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carbaguanine + 2 NADP+
-
-
-
?
7-cyano-7-carbaguanine + 2 NADPH + 2 H+
7-aminomethyl-7-carbaguanine + 2 NADP+
-
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
-
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
-
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
-
queuine is 7-aminomethyl-7-deazaguanine
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
-
queuine is 7-aminomethyl-7-deazaguanine
-
?
additional information
?
-
-
no substrates: acetonitrile, benzonitrile and benzylcyanide
-
-
-
additional information
?
-
-
during catalysis each active site of the dimeric enzyme binds one substrate molecule. NADPH binds independent of the substrate. The PreQ0 binding pocket of the active site is not involved in the binding of NADPH
-
-
-
additional information
?
-
-
QueF binds substrate preQ0 in a strongly exothermic process (DeltaH 80.3 kJ/mol) whereby the thioimide adduct is formed with half-of-the-sites reactivity in the homodimeric enzyme. Both steps of preQ0 reduction involve transfer of the 4-pro-R-hydrogen from NADPH. They proceed about 4-7fold more slowly than trapping of the enzyme-bound preQ0 as covalent thioimide and are mainly rate-limiting for the enzyme's kcat
-
-
-
additional information
?
-
J7KT48
enzyme is highly specific for substrate preQ0
-
-
-
additional information
?
-
J7KT48
enzyme is highly specific for substrate preQ0
-
-
-
additional information
?
-
the nitrile to amine conversion proceeds through four major stages: formation of a C-S covalent bond between the substrate and the catalytic cysteine residue to form the thioimidate intermediate, hydride transfer from NADPH to the substrate to generate the thiohemiaminal intermediate, cleavage of the C-S covalent bond to generate the imine intermediate, and second hydride transfer from NADPH to the imine intermediate to generate the final amine product. The free energy barrier for the rate-limiting step, i.e. the second hydride transfer, is20.8 kcal/mol
-
-
-
additional information
?
-
the nitrile to amine conversion proceeds through four major stages: formation of a C-S covalent bond between the substrate and the catalytic cysteine residue to form the thioimidate intermediate, hydride transfer from NADPH to the substrate to generate the thiohemiaminal intermediate, cleavage of the C-S covalent bond to generate the imine intermediate, and second hydride transfer from NADPH to the imine intermediate to generate the final amine product. The free energy barrier for the rate-limiting step, i.e. the second hydride transfer, is20.8 kcal/mol
-
-
-
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
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+
Q46920
natural substrate
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
-
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
O31678
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
-
late step in biosynthesis of the modified tRNA nucleoside queuosine
-
-
?
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.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-formyl-7-deazaguanine
-
carbonyl analogue of the imine intermediate, recognized by QueF as weak ligand for binding but not as substrate for reduction or oxidation
peroxide
-
peroxide-induced inactivation of the wild-type enzyme is reversible with thioredoxin
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
0.0061
2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
-
wild-type, pH 7.5, 25°C
0.00025
7-cyano-7-carbaguanine
J7KT48
below 0.25 microM, pH 7.4, 30°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
0.024
7-cyano-7-carbaguanine
J7KT48
pH 7.4, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3
-
substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant E230Q, pH 7.5, 25°C
3.8
-
substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant S90A, pH 7.5, 25°C
4.4
-
substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant E230Q, pH 7.5, 25°C
8.7
-
substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant F228W, pH 7.5, 25°C
10.8
-
substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant F228W, pH 7.5, 25°C
12.9
-
substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant S90A, pH 7.5, 25°C
14.3
-
substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant H229A, pH 7.5, 25°C
17.9
-
substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, mutant H229A, pH 7.5, 25°C
90
-
substrate 5-cyanopyrrolo[2,3-d]pyrimidin-4-one, wild-type, pH 7.5, 25°C
117
-
substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one, wild-type, pH 7.5, 25°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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
J7KT48
more than 60% of maximum activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
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
Show AA Sequence and Transmembrane Helices (15621 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.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus subtilis (strain 168)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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
dimer
homodimer
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, space group: P3(1)21. Unit-cell parameters: a = b = 93.52 A, c = 193.76 A
-
structure of mutant E97Q, displays an intramolecular disulfide formed between the catalytic Cys55 and a conserved Cys99 located near the active site. This structure exhibits major rearrangement of the loops responsible for substrate binding
-
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
-
homology model based on the crystal structure of nitrile reductase from Vibrio cholerae, PDB ID 3uxv. The side chain of residue Glu89 and the main chain of Ser90 form hydrogen bonds with the ring nitrogen atoms of the substrate. The carboxylate group of Glu230 also forms hydrogen bonds with the substrate preQ0. The aromatic ring of Phe228 may form a pi-pi-stacking interaction with the aromatic ring of preQ0, while the main chain of His229coordinates the keto-functionality of the substrate
J7KT48
hanging drop vapor diffusion method, using 0.04 M sodium dihydrogen phosphate, 0.96 M dipotassium hydrogen phosphate, and 10 mM GTP
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C99A
-
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
C99S
-
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
C99A
-
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
-
C99S
-
mutant does not compromise enzyme activity. Contrary to wild-type, peroxide-induced inactivation is irreversible
-
C190A
E230Q
-
about 4% of wild-type activity for natural substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
F228W
-
about 8% of wild-type activity for natural substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
H229A
-
about 15% of wild-type activity for natural substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
S90A
-
about 10% of wild-type activity for natural substrate 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
C190A
-
mutation in catalytic residue, no evidence of covalent binding of substrate preQ0. Mutant displays proton uptake
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
overproduction in Escherichia coli
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
Swairjo, M.A.; Reddy, R.R.; Lee, B.; Van Lanen, S.G.; Brown, S.; de Crecy-Lagard, V.; Iwata-Reuyl, D.; Schimmel, P.
Crystallization and preliminary x-ray characterization of the nitrile reductase QueF: a queuosine-biosynthesis enzyme
Acta Crystallogr. Sect. F
F61
945-948
2005
Bacillus subtilis, Bacillus subtilis (O31678)
brenda
Kuchino, Y.; Kasai, H.; Nihei, K.; Nishimura, S.
Biosynthesis of the modified nucleoside Q in transfer RNA
Nucleic Acids Res.
3
393-398
1976
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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
brenda
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
brenda
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
brenda
Kim, Y.; Zhou, M.; Moy, S.; Morales, J.; Cunningham, M.A.; Joachimiak, A.
High-resolution structure of the nitrile reductase QueF combined with molecular simulations provide insight into enzyme mechanism
J. Mol. Biol.
404
127-137
2010
Vibrio cholerae (Q9KTK0), Vibrio cholerae, Vibrio cholerae ATCC 39315 (Q9KTK0)
brenda
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)
brenda
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)
brenda
Ribeiro, A.; Yang, L.; Ramos, M.; Fernandes, P.; Liang, Z.; Hirao, H.
Insight into enzymatic nitrile reduction QM/MM study of the catalytic mechanism of QueF nitrile reductase
ACS Catal.
5
3740-3751
2015
Vibrio cholerae O1 (Q9KTK0), Vibrio cholerae O1 ATCC 39315 (Q9KTK0)
-
brenda
Mohammad, A.; Bon Ramos, A.; Lee, B.W.; Cohen, S.W.; Kiani, M.K.; Iwata-Reuyl, D.; Stec, B.; Swairjo, M.A.
Protection of the queuosine biosynthesis enzyme QueF from irreversible oxidation by a conserved intramolecular disulfide
Biomolecules
7
E30
2017
Bacillus subtilis 168 (O31678), Bacillus subtilis (O31678)
brenda
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)
-
brenda
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
brenda
Li, M.; Zhou, Z.; Zhang, Z.; Yu, H.; Xu, J.
Biochemical properties of a new nitrile reductase cloned from Pectobacterium carotovorum
J. Mol. Catal. B
131
47-54
2016
Pectobacterium carotovorum subsp. carotovorum (J7KT48), Pectobacterium carotovorum subsp. carotovorum PCC21 (J7KT48)
-
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.7.1.13)
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.
Information
