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show all sequences of 1.14.11.3

JBP1 and JBP2 proteins are Fe2+/2-oxoglutarate-dependent dioxygenases regulating hydroxylation of thymidine residues in trypanosome DNA

Cliffe, L.J.; Hirsch, G.; Wang, J.; Ekanayake, D.; Bullard, W.; Hu, M.; Wang, Y.; Sabatini, R.; J. Biol. Chem. 287, 19886-19895 (2012)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ascorbate
-
Leishmania major
ascorbate
-
Leishmania tarentolae
ascorbate
-
Trypanosoma brucei
ascorbate
-
Trypanosoma cruzi
Cloned(Commentary)
Commentary
Organism
recombinant expression of His-tagged JBP1 in Escherichia coli strain BL21-DE3 T1R
Trypanosoma cruzi
Engineering
Amino acid exchange
Commentary
Organism
additional information
mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine
Leishmania major
additional information
mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine
Leishmania tarentolae
additional information
mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine
Trypanosoma brucei
additional information
mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine
Trypanosoma cruzi
Inhibitors
Inhibitors
Commentary
Organism
Structure
2,4-pyridinedicarboxylic acid
competitive inhibition
Leishmania major
2,4-pyridinedicarboxylic acid
competitive inhibition
Leishmania tarentolae
2,4-pyridinedicarboxylic acid
competitive inhibition
Trypanosoma brucei
2,4-pyridinedicarboxylic acid
competitive inhibition
Trypanosoma cruzi
dimethyloxoglycine
competitive inhibition
Leishmania major
dimethyloxoglycine
competitive inhibition
Leishmania tarentolae
dimethyloxoglycine
competitive inhibition
Trypanosoma brucei
dimethyloxoglycine
competitive inhibition
Trypanosoma cruzi
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
dependent on
Leishmania major
Fe2+
dependent on
Leishmania tarentolae
Fe2+
dependent on
Trypanosoma brucei
Fe2+
dependent on
Trypanosoma cruzi
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
thymidine + 2-oxoglutarate + O2
Trypanosoma brucei
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
thymidine + 2-oxoglutarate + O2
Trypanosoma cruzi
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
thymidine + 2-oxoglutarate + O2
Leishmania tarentolae
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
thymidine + 2-oxoglutarate + O2
Leishmania major
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
thymidine + 2-oxoglutarate + O2
Trypanosoma brucei 427
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Leishmania major
-
-
-
Leishmania tarentolae
-
-
-
Trypanosoma brucei
-
line 221a
-
Trypanosoma brucei 427
-
line 221a
-
Trypanosoma cruzi
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged JBP1 from Escherichia coli strain BL21-DE3 T1R by metal affinty chromatography
Trypanosoma cruzi
Source Tissue
Source Tissue
Commentary
Organism
Textmining
bloodstream form
-
Trypanosoma brucei
-
metacyclic form
infective
Leishmania tarentolae
-
promastigote
-
Leishmania major
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Trypanosoma brucei
?
-
-
-
-
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Trypanosoma cruzi
?
-
-
-
-
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Leishmania tarentolae
?
-
-
-
-
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Leishmania major
?
-
-
-
-
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Trypanosoma brucei 427
?
-
-
-
-
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma brucei
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma cruzi
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Leishmania tarentolae
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Leishmania major
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma brucei
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma cruzi
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Leishmania tarentolae
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Leishmania major
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma brucei 427
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma brucei 427
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Leishmania major
37
-
assay at
Leishmania tarentolae
37
-
assay at
Trypanosoma brucei
37
-
assay at
Trypanosoma cruzi
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Leishmania major
8
-
assay at
Leishmania tarentolae
8
-
assay at
Trypanosoma brucei
8
-
assay at
Trypanosoma cruzi
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ascorbate
-
Leishmania major
ascorbate
-
Leishmania tarentolae
ascorbate
-
Trypanosoma brucei
ascorbate
-
Trypanosoma cruzi
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of His-tagged JBP1 in Escherichia coli strain BL21-DE3 T1R
Trypanosoma cruzi
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine
Leishmania major
additional information
mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine
Leishmania tarentolae
additional information
mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine
Trypanosoma brucei
additional information
mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine
Trypanosoma cruzi
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2,4-pyridinedicarboxylic acid
competitive inhibition
Leishmania major
2,4-pyridinedicarboxylic acid
competitive inhibition
Leishmania tarentolae
2,4-pyridinedicarboxylic acid
competitive inhibition
Trypanosoma brucei
2,4-pyridinedicarboxylic acid
competitive inhibition
Trypanosoma cruzi
dimethyloxoglycine
competitive inhibition
Leishmania major
dimethyloxoglycine
competitive inhibition
Leishmania tarentolae
dimethyloxoglycine
competitive inhibition
Trypanosoma brucei
dimethyloxoglycine
competitive inhibition
Trypanosoma cruzi
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
dependent on
Leishmania major
Fe2+
dependent on
Leishmania tarentolae
Fe2+
dependent on
Trypanosoma brucei
Fe2+
dependent on
Trypanosoma cruzi
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
thymidine + 2-oxoglutarate + O2
Trypanosoma brucei
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
thymidine + 2-oxoglutarate + O2
Trypanosoma cruzi
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
thymidine + 2-oxoglutarate + O2
Leishmania tarentolae
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
thymidine + 2-oxoglutarate + O2
Leishmania major
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
thymidine + 2-oxoglutarate + O2
Trypanosoma brucei 427
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
5-hydroxymethyluridine + succinate + CO2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged JBP1 from Escherichia coli strain BL21-DE3 T1R by metal affinty chromatography
Trypanosoma cruzi
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
bloodstream form
-
Trypanosoma brucei
-
metacyclic form
infective
Leishmania tarentolae
-
promastigote
-
Leishmania major
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Trypanosoma brucei
?
-
-
-
-
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Trypanosoma cruzi
?
-
-
-
-
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Leishmania tarentolae
?
-
-
-
-
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Leishmania major
?
-
-
-
-
additional information
thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated
725475
Trypanosoma brucei 427
?
-
-
-
-
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma brucei
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma cruzi
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Leishmania tarentolae
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Leishmania major
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma brucei
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma cruzi
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Leishmania tarentolae
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Leishmania major
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
thymidine + 2-oxoglutarate + O2
JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma brucei 427
5-hydroxymethyluridine + succinate + CO2
-
-
-
?
thymidine + 2-oxoglutarate + O2
telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner
725475
Trypanosoma brucei 427
5-hydroxymethyluridine + succinate + CO2
mass spectrometric product determination
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Leishmania major
37
-
assay at
Leishmania tarentolae
37
-
assay at
Trypanosoma brucei
37
-
assay at
Trypanosoma cruzi
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Leishmania major
8
-
assay at
Leishmania tarentolae
8
-
assay at
Trypanosoma brucei
8
-
assay at
Trypanosoma cruzi
General Information
General Information
Commentary
Organism
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
Leishmania major
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
Leishmania tarentolae
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
Trypanosoma brucei
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
Trypanosoma cruzi
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
Leishmania major
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
Leishmania tarentolae
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
Trypanosoma brucei
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
Trypanosoma cruzi
metabolism
JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA
Leishmania major
metabolism
JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA
Leishmania tarentolae
metabolism
JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA
Trypanosoma brucei
metabolism
JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA
Trypanosoma cruzi
additional information
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
Leishmania major
additional information
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
Leishmania tarentolae
additional information
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
Trypanosoma brucei
additional information
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
Trypanosoma cruzi
physiological function
the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo
Leishmania major
physiological function
the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo
Leishmania tarentolae
physiological function
the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo
Trypanosoma brucei
physiological function
the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo
Trypanosoma cruzi
General Information (protein specific)
General Information
Commentary
Organism
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
Leishmania major
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
Leishmania tarentolae
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
Trypanosoma brucei
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
Trypanosoma cruzi
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
Leishmania major
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
Leishmania tarentolae
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
Trypanosoma brucei
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
Trypanosoma cruzi
metabolism
JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA
Leishmania major
metabolism
JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA
Leishmania tarentolae
metabolism
JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA
Trypanosoma brucei
metabolism
JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA
Trypanosoma cruzi
additional information
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
Leishmania major
additional information
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
Leishmania tarentolae
additional information
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
Trypanosoma brucei
additional information
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
Trypanosoma cruzi
physiological function
the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo
Leishmania major
physiological function
the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo
Leishmania tarentolae
physiological function
the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo
Trypanosoma brucei
physiological function
the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo
Trypanosoma cruzi
Other publictions for EC 1.14.11.3
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)
725475
Cliffe
JBP1 and JBP2 proteins are Fe2 ...
Leishmania major, Leishmania tarentolae, Trypanosoma brucei, Trypanosoma brucei 427, Trypanosoma cruzi
J. Biol. Chem.
287
19886-19895
2012
4
-
1
-
4
-
8
-
-
4
-
5
-
14
-
-
1
-
-
3
-
-
15
-
4
-
-
-
4
-
-
-
-
-
-
4
-
1
-
-
4
-
-
8
-
-
-
4
-
5
-
-
-
1
-
3
-
-
15
-
4
-
-
-
4
-
-
-
-
20
20
-
-
-
439170
Stubbe
Identification of two alpha-ke ...
Rhodotorula glutinis
J. Biol. Chem.
260
9972-9975
1985
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
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1
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-
-
1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
1
-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439137
Warn-Cramer
Markedly different ascorbate d ...
Rhodotorula glutinis
J. Biol. Chem.
258
10551-10557
1983
-
-
-
-
-
-
-
-
-
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1
-
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2
-
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1
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-
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1
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-
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-
-
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-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
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1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439172
Holme
Purification of thymidine 2'-h ...
Neurospora crassa, Neurospora crassa STA 4
Acta Chem. Scand.
37
743-745
1983
-
-
-
-
-
-
-
-
-
-
2
-
-
7
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439141
Wondrack
Thymine 7-hydroxylase and pyri ...
Rhodotorula glutinis
J. Biol. Chem.
253
6511-6515
1978
2
-
-
-
-
-
-
-
-
1
-
-
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1
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-
-
-
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-
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-
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2
-
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-
-
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-
-
-
-
-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439174
Bankel
Thymidine 2-hydroxylation in N ...
Neurospora crassa, Neurospora crassa STA 4
J. Biol. Chem.
247
6128-6134
1972
2
-
-
-
-
-
14
8
-
1
1
-
-
7
-
-
-
-
-
-
-
-
11
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
14
-
8
-
1
1
-
-
-
-
-
-
-
-
-
11
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
439175
Liu
Stoichiometry of the pyrimidin ...
Neurospora crassa 1A, Neurospora crassa
Biochemistry
11
2172-2176
1972
2
-
-
-
-
-
-
-
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1
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7
-
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-
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1
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2
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1
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-
-
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-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439176
Shaffer
Substrate specificity of the h ...
Neurospora crassa 1A, Neurospora crassa
Biochim. Biophys. Acta
258
387-394
1972
1
-
-
-
-
-
1
-
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1
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2
-
7
-
-
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-
-
-
-
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2
-
-
-
-
-
-
-
-
-
-
-
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1
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-
-
-
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-
-
1
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-
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1
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2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439177
Shaffer
The cell-free conversion of a ...
Neurospora crassa 1A, Neurospora crassa
Biochem. Biophys. Res. Commun.
33
806-811
1968
1
-
-
-
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1
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7
-
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1
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1
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