BRENDA - Enzyme Database show
show all sequences of 1.14.11.6

Base J glucosyltransferase does not regulate the sequence specificity of J synthesis in trypanosomatid telomeric DNA

Bullard, W.; Cliffe, L.; Wang, P.; Wang, Y.; Sabatini, R.; Mol. Biochem. Parasitol. 204, 77-80 (2015)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
thymine + 2-oxoglutarate + O2
Leishmania major
-
5-hydroxymethyluracil + succinate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Leishmania major
Q4QFY1
-
-
Leishmania major
Q4QHM7
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
thymine + 2-oxoglutarate + O2
-
745735
Leishmania major
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
thymine + 2-oxoglutarate + O2
the telomeric repeat sequence GGGTTA is able to stimulate J synthesis, while mutated telomeric sequences (GGGTTT, GGGATT, or GGGAAA) are unable to support J synthesis
745735
Leishmania major
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
thymine + 2-oxoglutarate + O2
Leishmania major
-
5-hydroxymethyluracil + succinate + CO2
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
thymine + 2-oxoglutarate + O2
-
745735
Leishmania major
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
thymine + 2-oxoglutarate + O2
the telomeric repeat sequence GGGTTA is able to stimulate J synthesis, while mutated telomeric sequences (GGGTTT, GGGATT, or GGGAAA) are unable to support J synthesis
745735
Leishmania major
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
telomeric DNA of Trypanosomatids possesses a modified thymine base, called base J or beta-D-glucopyranosyloxymethyluracil, that is synthesized in a two-step process. The base is hydroxylated by a thymidine hydroxylase forming hydroxymethyluracil (hmU), a glucose moiety is then attached by the J-associated glucosyltransferase (JGT). Both JBP1 and JBP2 stimulate de novo thymidine hydroxylation in vivo. DNA Jaylation is largely regulated by cis-acting sequences and is thus genetically encoded. The key regulatory step of J synthesis seems to be the first step catalyzed by JBP1 and JBP2. The specificity of base J localization is probably due to the JBP enzymes generating 5-hydroxymethyluracil at only specific sites throughout the genome; telomeric DNA of Trypanosomatids possesses a modified thymine base, called base J or beta-D-glucopyranosyloxymethyluracil, that is synthesized in a two-step process. The base is hydroxylated by a thymidine hydroxylase forming hydroxymethyluracil (hmU), a glucose moiety is then attached by the J-associated glucosyltransferase (JGT). Both JBP1 and JBP2 stimulate de novo thymidine hydroxylation in vivo. DNA Jaylation is largely regulated by cis-acting sequences and is thus genetically encoded. The key regulatory step of J synthesis seems to be the first step catalyzed by JBP1 and JBP2. The specificity of base J localization is probably due to the JBP enzymes generating 5-hydroxymethyluracil at only specific sites throughout the genome
Leishmania major
General Information (protein specific)
General Information
Commentary
Organism
physiological function
telomeric DNA of Trypanosomatids possesses a modified thymine base, called base J or beta-D-glucopyranosyloxymethyluracil, that is synthesized in a two-step process. The base is hydroxylated by a thymidine hydroxylase forming hydroxymethyluracil (hmU), a glucose moiety is then attached by the J-associated glucosyltransferase (JGT). Both JBP1 and JBP2 stimulate de novo thymidine hydroxylation in vivo. DNA Jaylation is largely regulated by cis-acting sequences and is thus genetically encoded. The key regulatory step of J synthesis seems to be the first step catalyzed by JBP1 and JBP2. The specificity of base J localization is probably due to the JBP enzymes generating 5-hydroxymethyluracil at only specific sites throughout the genome
Leishmania major
Other publictions for EC 1.14.11.6
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745735
Bullard
Base J glucosyltransferase do ...
Leishmania major
Mol. Biochem. Parasitol.
204
77-80
2015
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1
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745921
Li
Molecular basis for the subst ...
Neurospora crassa
Nucleic Acids Res.
43
10026-10038
2015
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1
1
19
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4
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19
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1
1
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3
1
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1
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3
3
697315
Neidigh
Cloning and characterization o ...
Rhodotorula glutinis
Chem. Res. Toxicol.
22
885-893
2009
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4
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9
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1
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700084
Vainio
Evidence that J-binding protei ...
Leishmania tarentolae
Mol. Biochem. Parasitol.
164
157-161
2009
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1
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6
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1
1
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700501
Cliffe
JBP1 and JBP2 are two distinct ...
Trypanosoma brucei
Nucleic Acids Res.
37
1452-1462
2009
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1
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5
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1
1
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689246
Yu
The protein that binds to DNA ...
Leishmania tarentolae, Trypanosoma brucei
Nucleic Acids Res.
35
2107-2115
2007
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2
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8
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658220
Smiley
Genes of the thymidine salvage ...
Rhodotorula glutinis
Biochim. Biophys. Acta
1723
256-264
2005
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439133
Lai
-
Characterization of a novel, s ...
Rhodotorula glutinis
J. Am. Chem. Soc.
117
5023-5030
1995
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439134
Thornburg
Mechanism-based inactivation o ...
Rhodotorula glutinis
Biochemistry
32
14034-14042
1993
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1
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1
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1
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439135
Thornburg
A non-heme iron protein with h ...
Rhodotorula glutinis
Biochemistry
32
14023-14033
1993
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2
10
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1
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3
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2
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11
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10
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11
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439136
Thornburg
Mechanism-based inhibition of ...
Rhodotorula glutinis
J. Am. Chem. Soc.
111
7632-7633
1989
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439137
Warn-Cramer
Markedly different ascorbate d ...
Rhodotorula glutinis
J. Biol. Chem.
258
10551-10557
1983
2
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1
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1
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439138
Holme
Studies on the partial reactio ...
Neurospora crassa, Neurospora crassa STA 4
Biochim. Biophys. Acta
704
278-283
1982
1
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1
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1
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7
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1
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12
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12
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439139
Hsu
Uracils uncoupling of the deca ...
Neurospora crassa, Neurospora crassa uc-1
J. Biol. Chem.
256
6098-6101
1981
2
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439140
Wondrack
Substitution of nucleoside tri ...
Rhodotorula glutinis
J. Biol. Chem.
254
26-29
1979
7
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1
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7
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439141
Wondrack
Thymine 7-hydroxylase and pyri ...
Rhodotorula glutinis
J. Biol. Chem.
253
6511-6515
1978
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439142
Bankel
Thymine 7-hydroxylase from Neu ...
Neurospora crassa, Neurospora crassa STA 4
Biochim. Biophys. Acta
481
431-437
1977
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15
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439143
Holme
A kinetic study of thymine 7-h ...
Neurospora crassa, Neurospora crassa STA 4
Biochemistry
14
4999-5003
1975
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439144
Liu
Catalysis of three sequential ...
Neurospora crassa 1A, Neurospora crassa
Arch. Biochem. Biophys.
159
180-187
1973
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3
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439145
Bankel
Oxygenases involved in thymine ...
Neurospora crassa, Neurospora crassa STA 4
FEBS Lett.
21
135-138
1972
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439146
McCroskey
-
Studies pertaining to the puri ...
Neurospora crassa, Neurospora crassa 1A
Biochim. Biophys. Acta
277
264-277
1971
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1
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7
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1
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1
2
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439147
Abbott
Conversion of thymine to 5-hyd ...
Neurospora crassa, Neurospora crassa 1A
J. Biol. Chem.
239
156-159
1964
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7
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