Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
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.
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.
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-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
7-cyano-7-deazaguanine + NADPH + H+
queuine + NADP+ + H+
-
-
-
-
?
additional information
?
-
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-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-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+
-
-
-
-
?
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
?
-
enzyme is highly specific for substrate preQ0
-
-
-
additional information
?
-
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
D197N
-
complete loss of activity
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

-
complete loss of activity
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.
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