2.4.2.6: nucleoside deoxyribosyltransferase
This is an abbreviated version!
For detailed information about nucleoside deoxyribosyltransferase, go to the full flat file.
Word Map on EC 2.4.2.6
Reaction
Synonyms
2'-deoxyribosyltransferase, 2'-N-deoxyribosyltransferase, Chro_1188, CtNDT, deoxynucleoside 5-monophosphate N-glycosidase, deoxyribose transferase, deoxyribosyltransferase, nucleoside, DRTase I, DRTase II, GQR93_14380, LaNDT, LhNDT, LlNDT, LmPDT, LrNDT, N-deoxyribosyltransferase, N-deoxyribosyltransferase II, NDRT, NdRT-II, NDT, NDT-II, NDT4, NTD, nucleoside 2'-deoxyribosyltransferase, nucleoside 2'-deoxyribosyltransferase type II, nucleoside 2-deoxyribosyltransferase, nucleoside deoxyribosyltransferase I, nucleoside deoxyribosyltransferase II, nucleoside N-deoxyribosyltransferase, nucleoside trans-N-deoxyribosylase, PDT, purine nucleoside 2'-deoxyribosyltransferase, purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl transferase, RCL, Tb927.5.1360, TbPDT, trans-deoxyribosylase, trans-N-deoxyribosylase, trans-N-glycosidase, transdeoxyribosylase, type I NDT, YejD
ECTree
2.4.2.6 nucleoside deoxyribosyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.4.2.6 - nucleoside deoxyribosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G10S
site-directed mutagenesis, the NDT mutant displays improved activity for dideoxynucleoside
G9C
can not improve 2',3'-dideoxyribose transfer reaction, kcat is diminished as compared to wild-type
G9S
G9T
Ser remains a better substituent for Gly-9 than Thr, kcat is diminished as compared to wild-type
G9W
can not improve 2',3'-dideoxyribose transfer reaction, kcat is diminished as compared to wild-type
A15C
A15S
A15T
A15V
can not improve 2',3'-dideoxyribose transfer reaction, kcat is diminished as compared to wild-type
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
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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
-
A15V
-
can not improve 2',3'-dideoxyribose transfer reaction, kcat is diminished as compared to wild-type
-
E105A
-
site-directed mutagenesis, the mutant shows about 200fold reduced activity and a 170fold increased Km compared to the wild-type enzyme
N53D
site-directed mutagenesis, the mutant shows no ribosyltransferase activity and reduced activity compared to the wild-type enzyme
V11A
site-directed mutagenesis, the mutant shows increased activity with 2'-deoxyinosine and adenine compared to wild-type enzyme
V11S
site-directed mutagenesis, the mutant shows increased activity with 2'-deoxyinosine and adenine compared to wild-type enzyme
Y5F
site-directed mutagenesis, the deoxyribose/ribose selectivity ratio improves about tenfold compared to wild-type if Tyr5 is replaced with a phenylalanine, the mutant shows reduced activity compared to the wild-type enzyme
Y5F/N53D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N53D
-
site-directed mutagenesis, the mutant shows no ribosyltransferase activity and reduced activity compared to the wild-type enzyme
-
V11A
-
site-directed mutagenesis, the mutant shows increased activity with 2'-deoxyinosine and adenine compared to wild-type enzyme
-
V11S
-
site-directed mutagenesis, the mutant shows increased activity with 2'-deoxyinosine and adenine compared to wild-type enzyme
-
Y5F
-
site-directed mutagenesis, the deoxyribose/ribose selectivity ratio improves about tenfold compared to wild-type if Tyr5 is replaced with a phenylalanine, the mutant shows reduced activity compared to the wild-type enzyme
-
Y5F/N53D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
additional information
G9S
-
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
G9S
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
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
additional information
establishment of a site-saturation mutagenesis (SSM) library for LhNDT, analysis of enzyme-substrate interactions and amino acids near the NDT substrate-binding sites. Site-directed mutagenesis of resdieues Gly10, Ala11 and Leu96, high-throughput screening
additional information
-
establishment of a site-saturation mutagenesis (SSM) library for LhNDT, analysis of enzyme-substrate interactions and amino acids near the NDT substrate-binding sites. Site-directed mutagenesis of resdieues Gly10, Ala11 and Leu96, high-throughput screening
additional information
-
immobilization on calcium alginate or calcium pectate of the enzyme increases the 2'-deoxynucleoside synthesis effiency of the organism, method optimization, overview
additional information
-
immobilization on calcium alginate or calcium pectate of the enzyme increases the 2'-deoxynucleoside synthesis effiency of the organism, method optimization, overview
-
additional information
-
immobilization of the purified recombinant enzyme for use as a biocatalyst. The biocatalyst stability is significantly enhanced by multipoint covalent immobilization using a hetero-functional support activated with nickel-chelates and glyoxyl groups to promote the irreversible multivalent attachment (Ni2+-Gx) through three reaction steps 1. affinity binding between the his-tag of the enzyme and the metals on the support, 2. covalent multi-valent attachment at alkaline pH by lysine residues attachment to the glyoxyl groups of the carrier and 3. mild reduction in order to turn the reversible Schiff's base formed into irreversible (secondary amino) bonds and transform the remaining aldehyde groups into inert hydroxyl moieties. The immobilized enzyme can be reused for more than 300 h and stored during almost 3 months without activity loss. The derivative (Ni2+-30 Gx-LaNDT) is able to biosynthesize 88 mg floxuridine/g biocatalyst after 1h of reaction. The floxuridine yield is not affected significantly when the biocatalyst obtained by affinity immobilization (Ni2+-LaNDT) is assayed, but a decrease of around 50% of enzymatic activity is observed when Ni2+-Gx-LaNDT derivative is used. Structure modeling of LaNDT is used to analyze the effect of immobilization on some of the physicochemical properties of the immobilized NDT, overview
additional information
-
immobilization of the purified recombinant enzyme for use as a biocatalyst. The biocatalyst stability is significantly enhanced by multipoint covalent immobilization using a hetero-functional support activated with nickel-chelates and glyoxyl groups to promote the irreversible multivalent attachment (Ni2+-Gx) through three reaction steps 1. affinity binding between the his-tag of the enzyme and the metals on the support, 2. covalent multi-valent attachment at alkaline pH by lysine residues attachment to the glyoxyl groups of the carrier and 3. mild reduction in order to turn the reversible Schiff's base formed into irreversible (secondary amino) bonds and transform the remaining aldehyde groups into inert hydroxyl moieties. The immobilized enzyme can be reused for more than 300 h and stored during almost 3 months without activity loss. The derivative (Ni2+-30 Gx-LaNDT) is able to biosynthesize 88 mg floxuridine/g biocatalyst after 1h of reaction. The floxuridine yield is not affected significantly when the biocatalyst obtained by affinity immobilization (Ni2+-LaNDT) is assayed, but a decrease of around 50% of enzymatic activity is observed when Ni2+-Gx-LaNDT derivative is used. Structure modeling of LaNDT is used to analyze the effect of immobilization on some of the physicochemical properties of the immobilized NDT, overview
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additional information
development of mono- and a bi-enzymatic analytical immobilized enzyme reactors (IMERs) for biosynthetic purposes, evaluation of performances in the in-flow synthesis of nucleoside analogues of pharmaceutical interest. Two biocatalytic routes based on nucleoside 2'-deoxyribosyltransferase from Lactobacillus reuteri (LrNDT) and on uridine phosphorylase from Clostridium perfrigens (CpUP)/purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP) are investigated in the synthesis of 2'-deoxy, 2',3'-dideoxy and arabinonucleoside derivatives. LrNDT-IMER catalyzes the synthesis of 5-fluoro-2'-deoxyuridine and 5-iodo-2'-deoxyuridine in 65-59% conversion yield, while CpUP/AhPNP-IMER provides the best results for the preparation of arabinosyladenine with 60% conversion yield. Enzyme LrNDT is immobilized on an epoxy silica monolithic resin by an in situ procedure (30% for LrNDT immobilization rate)
additional information
-
development of mono- and a bi-enzymatic analytical immobilized enzyme reactors (IMERs) for biosynthetic purposes, evaluation of performances in the in-flow synthesis of nucleoside analogues of pharmaceutical interest. Two biocatalytic routes based on nucleoside 2'-deoxyribosyltransferase from Lactobacillus reuteri (LrNDT) and on uridine phosphorylase from Clostridium perfrigens (CpUP)/purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP) are investigated in the synthesis of 2'-deoxy, 2',3'-dideoxy and arabinonucleoside derivatives. LrNDT-IMER catalyzes the synthesis of 5-fluoro-2'-deoxyuridine and 5-iodo-2'-deoxyuridine in 65-59% conversion yield, while CpUP/AhPNP-IMER provides the best results for the preparation of arabinosyladenine with 60% conversion yield. Enzyme LrNDT is immobilized on an epoxy silica monolithic resin by an in situ procedure (30% for LrNDT immobilization rate)
additional information
Limosilactobacillus reuteri ATCC 55730
-
development of mono- and a bi-enzymatic analytical immobilized enzyme reactors (IMERs) for biosynthetic purposes, evaluation of performances in the in-flow synthesis of nucleoside analogues of pharmaceutical interest. Two biocatalytic routes based on nucleoside 2'-deoxyribosyltransferase from Lactobacillus reuteri (LrNDT) and on uridine phosphorylase from Clostridium perfrigens (CpUP)/purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP) are investigated in the synthesis of 2'-deoxy, 2',3'-dideoxy and arabinonucleoside derivatives. LrNDT-IMER catalyzes the synthesis of 5-fluoro-2'-deoxyuridine and 5-iodo-2'-deoxyuridine in 65-59% conversion yield, while CpUP/AhPNP-IMER provides the best results for the preparation of arabinosyladenine with 60% conversion yield. Enzyme LrNDT is immobilized on an epoxy silica monolithic resin by an in situ procedure (30% for LrNDT immobilization rate)
-
additional information
-
development of mono- and a bi-enzymatic analytical immobilized enzyme reactors (IMERs) for biosynthetic purposes, evaluation of performances in the in-flow synthesis of nucleoside analogues of pharmaceutical interest. Two biocatalytic routes based on nucleoside 2'-deoxyribosyltransferase from Lactobacillus reuteri (LrNDT) and on uridine phosphorylase from Clostridium perfrigens (CpUP)/purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP) are investigated in the synthesis of 2'-deoxy, 2',3'-dideoxy and arabinonucleoside derivatives. LrNDT-IMER catalyzes the synthesis of 5-fluoro-2'-deoxyuridine and 5-iodo-2'-deoxyuridine in 65-59% conversion yield, while CpUP/AhPNP-IMER provides the best results for the preparation of arabinosyladenine with 60% conversion yield. Enzyme LrNDT is immobilized on an epoxy silica monolithic resin by an in situ procedure (30% for LrNDT immobilization rate)
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additional information
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immobilization on calcium alginate or calcium pectate of the enzyme increases the 2'-deoxynucleoside synthesis effiency of the organism, method optimization, overview
additional information
Peribacillus psychrosaccharolyticus CECT 4074
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immobilization on calcium alginate or calcium pectate of the enzyme increases the 2'-deoxynucleoside synthesis effiency of the organism, method optimization, overview
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additional information
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immobilization on calcium alginate or calcium pectate of the enzyme increases the 2'-deoxynucleoside synthesis effiency of the organism, method optimization, overview
additional information
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immobilization on calcium alginate or calcium pectate of the enzyme increases the 2'-deoxynucleoside synthesis effiency of the organism, method optimization, overview
-
additional information
the structure-guided replacement of Val11 with either Ala or Ser results in variants with 2.8fold greater activity. TbPDT is covalently immobilized on glutaraldehyde-activated magnetic microspheres. MTbPDT3 is selected as the best derivative (4200 IU/g, activity recovery of 22%), and can be easily recaptured and recycled for over 25 reactions with negligible loss of activity. TbPDT is immobilized onto magnetic microspheres, which are physically characterized by scanning electron microscopy and dynamic light scattering
additional information
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the structure-guided replacement of Val11 with either Ala or Ser results in variants with 2.8fold greater activity. TbPDT is covalently immobilized on glutaraldehyde-activated magnetic microspheres. MTbPDT3 is selected as the best derivative (4200 IU/g, activity recovery of 22%), and can be easily recaptured and recycled for over 25 reactions with negligible loss of activity. TbPDT is immobilized onto magnetic microspheres, which are physically characterized by scanning electron microscopy and dynamic light scattering
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additional information
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immobilization on calcium alginate or calcium pectate of the enzyme increases the 2'-deoxynucleoside synthesis effiency of the organism, method optimization, overview
additional information
Weizmannia coagulans CECT 12
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immobilization on calcium alginate or calcium pectate of the enzyme increases the 2'-deoxynucleoside synthesis effiency of the organism, method optimization, overview
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