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Literature summary extracted from
- JBP1 and JBP2 proteins are Fe2+/2-oxoglutarate-dependent dioxygenases regulating hydroxylation of thymidine residues in trypanosome DNA (2012), J. Biol. Chem., 287, 19886-19895.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.11.3 | ascorbate | - |
Trypanosoma brucei |  |
| 1.14.11.3 | ascorbate | - |
Trypanosoma cruzi | |
| 1.14.11.3 | ascorbate | - |
Leishmania tarentolae | |
| 1.14.11.3 | ascorbate | - |
Leishmania major | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.11.3 | recombinant expression of His-tagged JBP1 in Escherichia coli strain BL21-DE3 T1R | Trypanosoma cruzi |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.11.3 | 2,4-pyridinedicarboxylic acid | competitive inhibition | Leishmania major | |
| 1.14.11.3 | 2,4-pyridinedicarboxylic acid | competitive inhibition | Leishmania tarentolae | |
| 1.14.11.3 | 2,4-pyridinedicarboxylic acid | competitive inhibition | Trypanosoma brucei | |
| 1.14.11.3 | 2,4-pyridinedicarboxylic acid | competitive inhibition | Trypanosoma cruzi | |
| 1.14.11.3 | dimethyloxoglycine | competitive inhibition | Leishmania major | |
| 1.14.11.3 | dimethyloxoglycine | competitive inhibition | Leishmania tarentolae | |
| 1.14.11.3 | dimethyloxoglycine | competitive inhibition | Trypanosoma brucei | |
| 1.14.11.3 | dimethyloxoglycine | competitive inhibition | Trypanosoma cruzi | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.11.3 | Fe2+ | dependent on | Trypanosoma brucei | |
| 1.14.11.3 | Fe2+ | dependent on | Trypanosoma cruzi | |
| 1.14.11.3 | Fe2+ | dependent on | Leishmania tarentolae | |
| 1.14.11.3 | Fe2+ | dependent on | Leishmania major | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.11.3 | 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 | - |
? | |
| 1.14.11.3 | 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 | - |
? | |
| 1.14.11.3 | 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 | - |
? | |
| 1.14.11.3 | 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 | - |
? | |
| 1.14.11.3 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.11.3 | Leishmania major | - |
- |
- |
| 1.14.11.3 | Leishmania tarentolae | - |
- |
- |
| 1.14.11.3 | Trypanosoma brucei | - |
line 221a | - |
| 1.14.11.3 | Trypanosoma brucei 427 | - |
line 221a | - |
| 1.14.11.3 | Trypanosoma cruzi | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.11.3 | recombinant His-tagged JBP1 from Escherichia coli strain BL21-DE3 T1R by metal affinty chromatography | Trypanosoma cruzi |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.11.3 | bloodstream form | - |
Trypanosoma brucei | - |
| 1.14.11.3 | metacyclic form | infective | Leishmania tarentolae | - |
| 1.14.11.3 | promastigote | - |
Leishmania major | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.11.3 | additional information | thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated | Trypanosoma brucei | ? | - |
? | |
| 1.14.11.3 | additional information | thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated | Trypanosoma cruzi | ? | - |
? | |
| 1.14.11.3 | additional information | thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated | Leishmania tarentolae | ? | - |
? | |
| 1.14.11.3 | additional information | thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated | Leishmania major | ? | - |
? | |
| 1.14.11.3 | additional information | thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated | Trypanosoma brucei 427 | ? | - |
? | |
| 1.14.11.3 | thymidine + 2-oxoglutarate + O2 | JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner | Trypanosoma brucei | 5-hydroxymethyluridine + succinate + CO2 | - |
? | |
| 1.14.11.3 | thymidine + 2-oxoglutarate + O2 | JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner | Trypanosoma cruzi | 5-hydroxymethyluridine + succinate + CO2 | - |
? | |
| 1.14.11.3 | thymidine + 2-oxoglutarate + O2 | JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner | Leishmania tarentolae | 5-hydroxymethyluridine + succinate + CO2 | - |
? | |
| 1.14.11.3 | thymidine + 2-oxoglutarate + O2 | JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner | Leishmania major | 5-hydroxymethyluridine + succinate + CO2 | - |
? | |
| 1.14.11.3 | 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 | Trypanosoma brucei | 5-hydroxymethyluridine + succinate + CO2 | mass spectrometric product determination | ? | |
| 1.14.11.3 | 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 | Trypanosoma cruzi | 5-hydroxymethyluridine + succinate + CO2 | mass spectrometric product determination | ? | |
| 1.14.11.3 | 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 | Leishmania tarentolae | 5-hydroxymethyluridine + succinate + CO2 | mass spectrometric product determination | ? | |
| 1.14.11.3 | 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 | Leishmania major | 5-hydroxymethyluridine + succinate + CO2 | mass spectrometric product determination | ? | |
| 1.14.11.3 | thymidine + 2-oxoglutarate + O2 | JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner | Trypanosoma brucei 427 | 5-hydroxymethyluridine + succinate + CO2 | - |
? | |
| 1.14.11.3 | 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 | Trypanosoma brucei 427 | 5-hydroxymethyluridine + succinate + CO2 | mass spectrometric product determination | ? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.11.3 | JBP1 | - |
Trypanosoma brucei |
| 1.14.11.3 | JBP1 | - |
Trypanosoma cruzi |
| 1.14.11.3 | JBP1 | - |
Leishmania tarentolae |
| 1.14.11.3 | JBP1 | - |
Leishmania major |
| 1.14.11.3 | JBP2 | - |
Trypanosoma brucei |
| 1.14.11.3 | JBP2 | - |
Trypanosoma cruzi |
| 1.14.11.3 | JBP2 | - |
Leishmania tarentolae |
| 1.14.11.3 | JBP2 | - |
Leishmania major |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.11.3 | 37 | - |
assay at | Trypanosoma brucei |
| 1.14.11.3 | 37 | - |
assay at | Trypanosoma cruzi |
| 1.14.11.3 | 37 | - |
assay at | Leishmania tarentolae |
| 1.14.11.3 | 37 | - |
assay at | Leishmania major |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.11.3 | 8 | - |
assay at | Trypanosoma brucei |
| 1.14.11.3 | 8 | - |
assay at | Trypanosoma cruzi |
| 1.14.11.3 | 8 | - |
assay at | Leishmania tarentolae |
| 1.14.11.3 | 8 | - |
assay at | Leishmania major |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.11.3 | evolution | JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family | Trypanosoma brucei |
| 1.14.11.3 | evolution | JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family | Trypanosoma cruzi |
| 1.14.11.3 | evolution | JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family | Leishmania tarentolae |
| 1.14.11.3 | evolution | JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family | Leishmania major |
| 1.14.11.3 | malfunction | mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation | Trypanosoma brucei |
| 1.14.11.3 | malfunction | mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation | Trypanosoma cruzi |
| 1.14.11.3 | malfunction | mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation | Leishmania tarentolae |
| 1.14.11.3 | malfunction | mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation | Leishmania major |
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
| 1.14.11.3 | additional information | the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity | Trypanosoma brucei |
| 1.14.11.3 | additional information | the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity | Trypanosoma cruzi |
| 1.14.11.3 | additional information | the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity | Leishmania tarentolae |
| 1.14.11.3 | additional information | the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity | Leishmania major |
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
| 1.14.11.3 | 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 |
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