Information on EC 1.7.1.13 - preQ1 synthase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.7.1.13
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RECOMMENDED NAME
GeneOntology No.
preQ1 synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7-aminomethyl-7-carbaguanine + 2 NADP+ = 7-cyano-7-carbaguanine + 2 NADPH + 2 H+
show the reaction diagram
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.
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Folate biosynthesis
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Metabolic pathways
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queuosine biosynthesis
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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.
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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
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-
?
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
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-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
show the reaction diagram
7-cyano-7-deazaguanine + NADPH + H+
queuine + NADP+ + H+
show the reaction diagram
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?
additional information
?
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no substrates: acetonitrile, benzonitrile and benzylcyanide
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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
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
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-
?
7-cyano-7-deazaguanine + 2 NADPH + 2 H+
queuine + 2 NADP+
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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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 - 0.036
NADPH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one
Escherichia coli
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wild-type, pH 7.5, 25°C
0.05
5-cyanopyrrolo[2,3-d]pyrimidin-4-one
Escherichia coli
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wild-type, pH 7.5, 25°C
0.127
7-cyano-7-deazaguanine
Escherichia coli
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pH 7.0, 37°C
0.0033 - 0.142
NADPH
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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Tris-buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
2 * 33000, gel filtration
67900
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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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
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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hanging drop vapor diffusion method, using 0.04 M sodium dihydrogen phosphate, 0.96 M dipotassium hydrogen phosphate, and 10 mM GTP
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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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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half-life 28.2
40
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half-life 12.8
45
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half-life 2.8
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 1 year, 1% residual activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overproduction in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
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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
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Show AA Sequence (8150 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.7.1.13)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)