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Information on EC 2.4.2.5 - nucleoside ribosyltransferase
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EC Tree
2.4.2.5 nucleoside ribosyltransferaseIUBMB Comments
Base1 and base2 represent various purines and pyrimidines.
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Word Map
- 2.4.2.5
- tachycardia
- nodal
-
atrioventricular
-
reentrant
- atrial
-
catheter
-
electrophysiological
-
radiofrequency
-
supraventricular
- ventricular
-
sinus
- arrhythmia
-
reentry
-
pace
-
retrograde
-
pacing
-
paroxysmal
-
cryoablation
-
slow-fast
-
fluoroscopy
- beat
- flutter
-
ostium
-
antegrade
-
triangle
-
wenckebach
-
posteroseptal
-
concealed
-
electrograms
-
palpitation
-
fast-slow
-
ventriculoatrial
-
electroanatomical
-
orthodromic
-
echo
-
msec
- tachyarrhythmias
-
ectopy
-
interatrial
- synthesis
-
electrophysiologists
-
perinodal
-
preexcitation
-
extrastimulus
-
overdrive
-
wolff-parkinson-white
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anteroseptal
-
12-lead
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postablation
-
tricuspid
-
flecainide
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
avnrt, n-ribosyltransferase, nucleoside n-ribosyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AvNRT
N-ribosyltransferase
NRT
nucleoside N-ribosyltransferase
-
-
-
-
ribosyltransferase, nucleoside
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-ribosyl-base1 + base2 = D-ribosyl-base2 + base1
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
nucleoside:purine(pyrimidine) D-ribosyltransferase
Base1 and base2 represent various purines and pyrimidines.
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CAS REGISTRY NUMBER
COMMENTARY
9030-31-3
-
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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
guanosine + 6-methoxyguanine
guanine + 6-methoxyguanosine
-
-
-
?
D-ribosyl-base1 + base2
D-ribosyl-base2 + base1
-
-
-
?
guanosine + 2,6-diaminopurine
guanine + 2,6-diaminopurine ribonucleoside
-
-
-
?
guanosine + 2,6-diaminopurine
guanine + 2,6-diaminopurine ribonucleoside
-
-
-
?
guanosine + 2,6-diaminopurine
guanine + 2,6-diaminopurine ribonucleoside
-
-
-
?
guanosine + 2-chloroadenine
guanine + 2-chloroadenosine
-
-
-
?
guanosine + 2-chloroadenine
guanine + 2-chloroadenosine
-
-
-
?
guanosine + 2-chloroadenine
guanine + 2-chloroadenosine
-
-
-
?
guanosine + 2-fluoroadenine
guanine + 2-fluoroadenosine
-
-
-
?
guanosine + 2-fluoroadenine
guanine + 2-fluoroadenosine
-
-
-
?
guanosine + 2-fluoroadenine
guanine + 2-fluoroadenosine
-
-
-
?
additional information
?
-
substrate specificity of recombinant enzyme, overview. Binding structure of guanosine to the active site of AvNRT
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-
-
additional information
?
-
-
substrate specificity of recombinant enzyme, overview. Binding structure of guanosine to the active site of AvNRT
-
-
-
additional information
?
-
substrate specificity of recombinant enzyme, overview. Binding structure of guanosine to the active site of AvNRT
-
-
-
additional information
?
-
substrate specificity of recombinant enzyme, overview. Binding structure of guanosine to the active site of AvNRT
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-
-
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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
D-ribosyl-base1 + base2
D-ribosyl-base2 + base1
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
the activity of AvNRT increases up to 2fold in 4 M NaCl aqueous solution
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
Pseudomonas trifolii
-
40°C: about 60% of maximal activity, 60°C: about 80% of maximal activity, formation of guanosine
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a chemolithoautotrophic hyperthermophilic sulfitereducing archaeal coccus
UniProt
brenda
a chemolithoautotrophic hyperthermophilic sulfitereducing archaeal coccus
UniProt
brenda
a chemolithoautotrophic hyperthermophilic sulfitereducing archaeal coccus
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme homology structure modeling and molecular dynamics simulations, overview. Nucleophilic attack on C1' by the carboxylate of the catalytic residue Glu85. Pro11 and Pro42 play a prominent role in making up the active site cavity where one of the Asp79 carboxylate oxygens and the carboxamide nitrogen of Asn113 recognize the O5' of the sugar moiety of the substrate while the backbone NH of Ala10 hydrogen bonds to O3'. The heteroaromatic ring of the nucleobase thus gets sandwiched between the phenyl rings of Phe12 and Phe13, on one side and the hydrophobic sidechains of Phe56 and Leu119 on the opposite side. The Met120 side chain sulfur appears close to the H1' atom, which suggests that it likely plays a role, together with the carboxylate of Asp62, in stabilization of the oxocarbenium reaction intermediate
additional information
-
enzyme homology structure modeling and molecular dynamics simulations, overview. Nucleophilic attack on C1' by the carboxylate of the catalytic residue Glu85. Pro11 and Pro42 play a prominent role in making up the active site cavity where one of the Asp79 carboxylate oxygens and the carboxamide nitrogen of Asn113 recognize the O5' of the sugar moiety of the substrate while the backbone NH of Ala10 hydrogen bonds to O3'. The heteroaromatic ring of the nucleobase thus gets sandwiched between the phenyl rings of Phe12 and Phe13, on one side and the hydrophobic sidechains of Phe56 and Leu119 on the opposite side. The Met120 side chain sulfur appears close to the H1' atom, which suggests that it likely plays a role, together with the carboxylate of Asp62, in stabilization of the oxocarbenium reaction intermediate
additional information
-
enzyme homology structure modeling and molecular dynamics simulations, overview. Nucleophilic attack on C1' by the carboxylate of the catalytic residue Glu85. Pro11 and Pro42 play a prominent role in making up the active site cavity where one of the Asp79 carboxylate oxygens and the carboxamide nitrogen of Asn113 recognize the O5' of the sugar moiety of the substrate while the backbone NH of Ala10 hydrogen bonds to O3'. The heteroaromatic ring of the nucleobase thus gets sandwiched between the phenyl rings of Phe12 and Phe13, on one side and the hydrophobic sidechains of Phe56 and Leu119 on the opposite side. The Met120 side chain sulfur appears close to the H1' atom, which suggests that it likely plays a role, together with the carboxylate of Asp62, in stabilization of the oxocarbenium reaction intermediate
-
additional information
-
enzyme homology structure modeling and molecular dynamics simulations, overview. Nucleophilic attack on C1' by the carboxylate of the catalytic residue Glu85. Pro11 and Pro42 play a prominent role in making up the active site cavity where one of the Asp79 carboxylate oxygens and the carboxamide nitrogen of Asn113 recognize the O5' of the sugar moiety of the substrate while the backbone NH of Ala10 hydrogen bonds to O3'. The heteroaromatic ring of the nucleobase thus gets sandwiched between the phenyl rings of Phe12 and Phe13, on one side and the hydrophobic sidechains of Phe56 and Leu119 on the opposite side. The Met120 side chain sulfur appears close to the H1' atom, which suggests that it likely plays a role, together with the carboxylate of Asp62, in stabilization of the oxocarbenium reaction intermediate
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). F2KPY9_ARCVS
Archaeoglobus veneficus (strain DSM 11195 / SNP6)
144
0
16086
TrEMBL
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
additional information
homotetramer
4 * 18000, recombinant enzyme, SDS-PAGE, 4* 19245, recombinant enzyme, analytical ultracentrifugation
homotetramer
-
4 * 18000, recombinant enzyme, SDS-PAGE, 4* 19245, recombinant enzyme, analytical ultracentrifugation
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homotetramer
-
4 * 18000, recombinant enzyme, SDS-PAGE, 4* 19245, recombinant enzyme, analytical ultracentrifugation
-
additional information
three-dimensional modeling of AvNRT, overview
additional information
-
three-dimensional modeling of AvNRT, overview
additional information
-
three-dimensional modeling of AvNRT, overview
-
additional information
-
three-dimensional modeling of AvNRT, overview
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme activity is retained in the presence of several water-miscible organic solvents
additional information
-
the enzyme activity is retained in the presence of several water-miscible organic solvents
additional information
-
the enzyme activity is retained in the presence of several water-miscible organic solvents
-
additional information
-
the enzyme activity is retained in the presence of several water-miscible organic solvents
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme AvNRT from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and preparative gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene nrt, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme AvNRT in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the enzyme is a thermophilic and halotolerant biocatalyst that is successfully employed in the synthesis of different purine ribonucleoside analogues, potential of AvNRT as an industrial biocatalyst for the synthesis of nucleoside analogues
synthesis
-
the enzyme is a thermophilic and halotolerant biocatalyst that is successfully employed in the synthesis of different purine ribonucleoside analogues, potential of AvNRT as an industrial biocatalyst for the synthesis of nucleoside analogues
-
synthesis
-
the enzyme is a thermophilic and halotolerant biocatalyst that is successfully employed in the synthesis of different purine ribonucleoside analogues, potential of AvNRT as an industrial biocatalyst for the synthesis of nucleoside analogues
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koch, A.L.
Some enzymes of nucleoside metabolism of Escherichia coli
J. Biol. Chem.
223
535-549
1956
Escherichia coli
brenda
Kamimura, A.; Mitsugi, K.; Okumura, S.
Bacterial synthesis of nucleosides by the pentosyl transfer reaction from nucleoside to base
Agric. Biol. Chem.
37
2063-2072
1973
Pseudomonas trifolii, Pseudomonas trifolii IAM-1555
-
brenda
Acosta, J.; Del Arco, J.; Pisabarro, V.; Gago, F.; Fernandez-Lucas, J.
N-Ribosyltransferase from Archaeoglobus veneficus a novel halotolerant and thermostable biocatalyst for the synthesis of purine ribonucleoside analogs
Front. Bioeng. Biotechnol.
8
593
2020
Archaeoglobus veneficus (F2KPY9), Archaeoglobus veneficus, Archaeoglobus veneficus DSM 11195 (F2KPY9), Archaeoglobus veneficus SNP6 (F2KPY9)
brenda
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Release 2023.1 (January 2023)
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