EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.108 | - |
Pyrococcus horikoshii |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.108 | - |
Pyrococcus horikoshii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.5.1.108 | C163A | difference in the EPR spectrum of the reduced form, pronounced rhombic main features with greatly increased g-value anisotropy, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600 | Pyrococcus horikoshii |
2.5.1.108 | C163A | mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster | Pyrococcus horikoshii |
2.5.1.108 | C259A/C287A | homodimeric mutant enzyme not stable. It is inactive and cannot bind a [4Fe-4S] cluster. Heterodimeric enzyme with a wild-type subunit and a mutant subunit is active | Pyrococcus horikoshii |
2.5.1.108 | C287A | difference in the EPR spectrum, g-tensors are more axial than wild type, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600 | Pyrococcus horikoshii |
2.5.1.108 | C287A | mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster | Pyrococcus horikoshii |
2.5.1.108 | C59A | difference in the EPR spectrum, g-tensors are more axial than wild type, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600 | Pyrococcus horikoshii |
2.5.1.108 | C59A | mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster | Pyrococcus horikoshii |
2.5.1.108 | C59A/C287A | inactive mutant lacks the Fe-S cluster. A heterodimer of wild-type subunit and C59A/C287A mutant subunit is stable and active | Pyrococcus horikoshii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.108 | Iron-sulfur cluster | each monomer contains three conserved cysteine residues that can bind a [4Fe-4S] cluster. In the reduced state, the [4Fe-4S] cluster can provide one electron to reductively cleave the bound S-adenosyl-L-methionine molecule. The chemistry requires only one [4Fe-4S] cluster to be present in the Dph2 dimer although each monomer can bind a [4Fe-4S] cluster | Pyrococcus horikoshii | |
2.5.1.108 | Iron-sulfur cluster | each monomer of the dimeric enzyme contains three conserved cysteine residues that can bind a [4Fe4S] cluster. In the reduced state, the [4Fe4S] cluster can provide one electron to reductively cleave the bound S-adenosyl-L-methionine molecule | Pyrococcus horikoshii |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.5.1.108 | 34000 | - |
2 * 34000, SDS-PAGE | Pyrococcus horikoshii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.108 | S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] | Pyrococcus horikoshii | first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2 | S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2] | - |
? | |
2.5.1.108 | S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2] | Pyrococcus horikoshii | the enzyme is involved in diphthamide biosynthesis | S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2] | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.108 | Pyrococcus horikoshii | O58832 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.5.1.108 | - |
Pyrococcus horikoshii |
2.5.1.108 | wild-type and mutant enzymes | Pyrococcus horikoshii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.108 | S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] | - |
Pyrococcus horikoshii | S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2] | - |
? | |
2.5.1.108 | S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] | first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2 | Pyrococcus horikoshii | S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2] | - |
? | |
2.5.1.108 | S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2] | the enzyme is involved in diphthamide biosynthesis | Pyrococcus horikoshii | S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2] | - |
? | |
2.5.1.108 | S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2] | the 3-amino-3-carboxypropyl radical is added to the imidazole ring in the pathway towards the formation of the product | Pyrococcus horikoshii | S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2] | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.108 | homodimer | - |
Pyrococcus horikoshii |
2.5.1.108 | homodimer | 2 * 34000, SDS-PAGE | Pyrococcus horikoshii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.108 | PhDph2 | - |
Pyrococcus horikoshii |
2.5.1.108 | S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase | - |
Pyrococcus horikoshii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.5.1.108 | 65 | - |
assay at | Pyrococcus horikoshii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.5.1.108 | 7.4 | - |
assay at | Pyrococcus horikoshii |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.5.1.108 | physiological function | first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2 | Pyrococcus horikoshii |