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Information on EC 2.4.2.6 - nucleoside deoxyribosyltransferase and Organism(s) Limosilactobacillus fermentum and UniProt Accession Q6YNI5
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2.4.2.6 nucleoside deoxyribosyltransferaseIUBMB Comments
Base1 and base2 represent various purines and pyrimidines.
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Word Map
The taxonomic range for the selected organisms is: Limosilactobacillus fermentum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
ndrt, nucleoside 2'-deoxyribosyltransferase, trans-n-deoxyribosylase, ctndt, drtase i, nucleoside 2-deoxyribosyltransferase, 2'-deoxyribosyltransferase, nucleoside deoxyribosyltransferase, drtase ii, landt, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deoxyribose transferase
-
-
-
-
deoxyribosyltransferase, nucleoside
-
-
-
-
NdRT-II
-
-
-
-
nucleoside trans-N-deoxyribosylase
-
-
-
-
purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl transferase
-
-
-
-
trans-deoxyribosylase
-
-
-
-
trans-N-deoxyribosylase
-
-
-
-
trans-N-glycosidase
-
-
-
-
transdeoxyribosylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
nucleoside:purine(pyrimidine) deoxy-D-ribosyltransferase
Base1 and base2 represent various purines and pyrimidines.
CAS REGISTRY NUMBER
COMMENTARY
9026-86-2
-
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',3'-dideoxyadenosine + cytosine
2',3'-dideoxycytidine + adenine
-
-
-
?
2',3'-dideoxyadenosine + thymine
2',3'-dideoxythymidine + adenine
-
-
-
?
2',3'-dideoxycytidine + adenine
2',3'-dideoxyadenosine + cytosine
-
-
-
?
2',3'-dideoxycytidine + hypoxanthine
2',3'-dideoxyinosine + cytosine
-
-
-
?
2',3'-dideoxycytidine + thymine
2',3'-dideoxythymidine + cytosine
-
-
-
?
2',3'-dideoxyguanosine + thymine
2',3'-dideoxythymidine + guanine
-
-
-
?
2',3'-dideoxyinosine + adenine
2',3'-dideoxyadenosine + hypoxanthine
-
-
-
?
2',3'-dideoxythymidine + adenine
2',3'-dideoxyadenosine + thymine
-
-
-
?
2',3'-dideoxyuridine + cytosine
2',3'-dideoxycytidine + uracil
-
-
-
?
2',3'didehydro-2',3'-dideoxythymidine + adenine
2',3'didehydro-2',3'-dideoxyadenosine + thymine
-
-
-
?
2'-deoxyadenosine + cytosine
2'-deoxycytidine + adenine
-
-
-
?
2'-deoxyadenosine + thymine
2'-deoxythymidine + adenine
-
-
-
?
2'-deoxycytidine + adenine
2'-deoxyadenosine + cytosine
-
-
-
?
2'-deoxycytidine + hypoxanthine
2'-deoxyinosine + cytosine
-
-
-
?
2'-deoxycytidine + thymine
2'-deoxythymidine + cytosine
-
-
-
?
2'-deoxyguanosine + thymine
2'-deoxythymidine + guanine
-
-
-
?
2'-deoxyinosine + adenine
2'-deoxyadenosine + hypoxanthine
-
-
-
?
2'-deoxythymidine + adenine
2'-deoxyadenosine + thymine
-
-
-
?
2'-deoxyuridine + cytosine
2'-deoxycytidine + uracil
-
-
-
?
2'-deoxycytidine + adenosine
2'-deoxyadenosine + cytosine
-
-
-
-
?
additional information
?
-
-
the enzyme glycosylates N2,3-ethenoguanine (8,9-dihydro-9-oxoimidazo[2,1-b]purine) at N7 and N1 with somewhat less selectivity for N7
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
0.02
mutant G9S, with 2'-deoxyinosine and adenine as substrates
0.03
0.036
0.05
0.06
0.19
wild-type, with 2',3'-dideoxyuridine and cytosine as substrates
0.42
mutant A15T, 2',3'-dideoxyadenosine and thymine as substrates
0.46
mutant A15T, 2'-deoxyadenosine and thymine as substrates
0.5
0.6
mutant G9S, with 2',3'-dideoxyguanosine and thymine as substrates
1.08
wild-type, with 2'-deoxyinosine and adenine as substrates
1.1
mutant A15T, 2'-deoxyadenosine and cytosine as substrates
1.29
1.35
mutant A15T, 2',3'-dideoxyadenosine and cytosine as substrates
1.47
mutant A15T, 2',3'-dideoxycytidine and thymine as substrates
1.6
mutant G9S, with 2',3'-dideoxyuridine and cytosine as substrates
1.9
12.7
mutant G9S, with 2'-deoxyuridine and cytosine as substrates
20.1
32
wild-type, 2'-deoxycytidine and thymine as substrates
33.2
wild-type, 2'-deoxyadenosine and cytosine as substrates
40.2
wild-type, with 2'-deoxyuridine and cytosine as substrates
6.8
6.9
7.1
7.11
mutant A15T, 2'-deoxycytidine and thymine as substrates
8.4
wild-type, 2'-deoxyadenosine and thymine as substrates
83.7
9.28
9.3
0.01
wild-type, 2',3'-dideoxyadenosine and thymine as substrates
0.01
wild-type, 2',3'-dideoxycytidine and thymine as substrates
0.01
wild-type, with 2',3'-dideoxyguanosine and thymine as substrates
0.01
wild-type, with 2',3'-dideoxyinosine and adenine as substrates
0.03
wild-type, 2',3'-dideoxyadenosine and cytosine as substrates
0.03
wild-type, 2,3'-dideoxythymidine and adenine as substrates
0.03
wild-type, with 2',3'-dideoxythymidine and adenine as substrates
0.036
wild-type, 2',3'didehydro-2',3'-dideoxythymidine and adenine as substrates
0.036
wild-type, with 2',3'didehydro-2',3'-dideoxythymidine and adenine as substrates
0.05
wild-type, 2',3'-dideoxycytidine and hypoxanthine as substrates
0.05
wild-type, with 2',3'-dideoxycytidine and hypoxanthine as substrates
0.06
mutant G9S, with 2',3'-dideoxyinosine and adenine as substrates
0.06
wild-type, 2',3'-dideoxycytidine and adenine as substrates
0.06
wild-type, with 2'-deoxycytidine and hypoxanthine as substrates
0.5
mutant A15T, 2,3'-dideoxythymidine and adenine as substrates
0.5
mutant G9S, with 3'-dideoxythymidine and adenine as substrates
1.29
mutant A15T, 2'-deoxycytidine and hypoxanthine as substrates
1.29
mutant G9S, with 2',3'-dideoxycytidine and adenine as substrates
1.9
mutant A15T, 2'-deoxythymidine and adenine as substrates
1.9
mutant G9S, with 2'-deoxythymidine and adenine as substrates
20.1
wild-type, 2'-deoxythymidine and adenine as substrates
20.1
wild-type, with 2'-deoxythymidine and adenine as substrates
6.8
mutant A15T, 2',3'-dideoxycytidine and hypoxanthine as substrates
6.8
mutant G9S, with 2',3'-dideoxycytidine and hypoxanthine as substrates
6.9
wild-type, 2'-deoxycytidine and hypoxanthine as substrates
6.9
wild-type, with 2',3'-dideoxycytidine and adenine as substrates
7.1
mutant A15T, 2',3'-dideoxycytidine and adenine as substrates
7.1
mutant G9S, with 2'-deoxycytidine and hypoxanthine as substrates
83.7
wild-type, 2'-deoxycytidine and adenine as substrates
83.7
wild-type, with 2'-deoxycytidine and adenine as substrates
9.28
mutant A15T, 2',3'didehydro-2',3'-dideoxythymidine and adenine as substrates
9.28
mutant G9S, with 2',3'didehydro-2',3'-dideoxythymidine and adenine as substrates
9.3
mutant A15T, 2'-deoxycytidine and adenine as substrates
9.3
mutant G9S, with 2'-deoxycytidine and adenine as substrates
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
attached to cell wall surface, enzyme can be released into the culture broth
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A15C
A15S
A15T
A15V
can not improve 2',3'-dideoxyribose transfer reaction, kcat is diminished as compared to wild-type
A15C
is not capable of improving 2',3'-dideoxyribose transfer reaction
A15S
activity with 2'-deoxycytidine and adenine as substrates is closer to that of the wild-type enzyme than that of the A15T mutant, kcat is diminished as compared to wild-type
A15S
Ser appears a good alternative for Thr, rate of 2',3'-dideoxyribosyl transfer from 2',3'-dideoxycytidine to adenine of the two mutants is almost identical
A15T
a single amino-acid substitution allows the conversion of the nucleoside 2'-deoxyribosyltransferase activity to a nucleoside 2',3'-dideoxy- or 2'3'-didehydro, 2',3'-dideoxyribosyltransferase activity. Specificity for the base is unchanged compared to the wild-type. The mutant displays an improved activity to the transfer of 2',3'-dideoxyribose, which is enhanced by 250fold (depending on the donors and acceptors) while the deoxyribosyl group transfer remains acceptable (30% of the wild-type)
A15T
mutation allows conversion of the nucleoside 2'deoxyribosyltransferase activity to a nucleoside 2',3'-dideoxy- or 2',3'-didehydro,2',3'-dideoxyribosyltransferase activity, kcat is diminished as compared to wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Sephacryl S-200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaminski, P.A.; Dacher, P.; Dugue, L.; Pochet, S.
In vivo reshaping the catalytic site of nucleoside 2-deoxyribosyltransferase for dideoxy- and didehydronucleosides via a single amino acid substitution
J. Biol. Chem.
283
20053-20059
2008
Lactobacillus leichmannii (Q9RSV5), Lactobacillus leichmannii, Limosilactobacillus fermentum (Q6YNI5), Limosilactobacillus fermentum, Limosilactobacillus fermentum PAK9 (Q6YNI5)
Kaminski, P.A.; Dugue, L.; Pochet, S.
Expanding substrate specificity of nucleoside 2-deoxyribosyltransferase
Nucleic Acids Symp. Ser.
52
495-496
2008
Lactobacillus leichmannii, Limosilactobacillus fermentum (Q6YNI5)
Lin, Y.; Zhang, W.; Zhu, F.; Su, J.; Fang, D.; Yang, Y.; Zhang, G.; Xie, L.; Zhang, R.; Wang, H.
Subcellular localization of N-deoxyribosyltransferase in Lactobacillus fermentum: cell surface association of an intracellular nucleotide metabolic enzyme
FEMS Microbiol. Lett.
323
132-141
2011
Limosilactobacillus fermentum, Limosilactobacillus fermentum CGMCC 1.2133
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