BRENDA - Enzyme Database show
show all sequences of 1.14.11.6

Evidence that J-binding protein 2 is a thymidine hydroxylase catalyzing the first step in the biosynthesis of DNA base J

Vainio, S.; Genest, P.A.; ter Riet, B.; van Luenen, H.; Borst, P.; Mol. Biochem. Parasitol. 164, 157-161 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
JBP2, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes, the latter contain 4 exchanges of conserved residues
Leishmania tarentolae
Engineering
Amino acid exchange
Commentary
Organism
D416A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
Leishmania tarentolae
H414A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
Leishmania tarentolae
H465A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
Leishmania tarentolae
additional information
inactivation of both of the LtJBP2 alleles by conventional knock-out strategy, the major phenotypes of the LtJBP2-/- cells, showing reduced levels of J and serious growth defects, can be completely reversed by the presence of an ectopic copy of LtJBP2
Leishmania tarentolae
R478A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
Leishmania tarentolae
V482A/L548Q
site-directed and random mutagenesis, the mutant can complement the JBP2 knockout mutant strain
Leishmania tarentolae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
thymine + 2-oxoglutarate + O2
Leishmania tarentolae
-
5-hydroxymethyluracil + succinate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Leishmania tarentolae
B6EU02
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme is a bifunctional helicase and thymine dioxygenase
700084
Leishmania tarentolae
?
-
-
-
-
thymine + 2-oxoglutarate + O2
-
700084
Leishmania tarentolae
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
JBP2 contains a SWI2/SNF2 chromatin remodeling domain in its C-terminus, and a homologous region with JBP1 at the N-terminus
Leishmania tarentolae
Cloned(Commentary) (protein specific)
Commentary
Organism
JBP2, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes, the latter contain 4 exchanges of conserved residues
Leishmania tarentolae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D416A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
Leishmania tarentolae
H414A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
Leishmania tarentolae
H465A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
Leishmania tarentolae
additional information
inactivation of both of the LtJBP2 alleles by conventional knock-out strategy, the major phenotypes of the LtJBP2-/- cells, showing reduced levels of J and serious growth defects, can be completely reversed by the presence of an ectopic copy of LtJBP2
Leishmania tarentolae
R478A
site-directed mutagenesis, cells expressing the LtJBP2 mutant exhibits a serious growth defect
Leishmania tarentolae
V482A/L548Q
site-directed and random mutagenesis, the mutant can complement the JBP2 knockout mutant strain
Leishmania tarentolae
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 tarentolae
-
5-hydroxymethyluracil + succinate + CO2
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme is a bifunctional helicase and thymine dioxygenase
700084
Leishmania tarentolae
?
-
-
-
-
thymine + 2-oxoglutarate + O2
-
700084
Leishmania tarentolae
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
JBP2 contains a SWI2/SNF2 chromatin remodeling domain in its C-terminus, and a homologous region with JBP1 at the N-terminus
Leishmania tarentolae
General Information
General Information
Commentary
Organism
physiological function
the genomic DNA of kinetoplastid parasites contains a unique modified base beta-D-glucosylhydroxymethyluracil or base J. J-binding protein, JBP, 1 and 2, which regulate the levels of J in the genome, are catalyzing the first step in J biosynthesis. JBP2, like JBP1, is a thymidine hydroxylase. Unlike JBP1, JBP2 is dispensable for Leishmania, mutational analysis, overview
Leishmania tarentolae
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the genomic DNA of kinetoplastid parasites contains a unique modified base beta-D-glucosylhydroxymethyluracil or base J. J-binding protein, JBP, 1 and 2, which regulate the levels of J in the genome, are catalyzing the first step in J biosynthesis. JBP2, like JBP1, is a thymidine hydroxylase. Unlike JBP1, JBP2 is dispensable for Leishmania, mutational analysis, overview
Leishmania tarentolae
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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745921
Li
Molecular basis for the subst ...
Neurospora crassa
Nucleic Acids Res.
43
10026-10038
2015
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1
19
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697315
Neidigh
Cloning and characterization o ...
Rhodotorula glutinis
Chem. Res. Toxicol.
22
885-893
2009
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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
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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
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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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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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11
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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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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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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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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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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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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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439147
Abbott
Conversion of thymine to 5-hyd ...
Neurospora crassa, Neurospora crassa 1A
J. Biol. Chem.
239
156-159
1964
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