Enzymes
| UniProtKB help_outline | 80,816 proteins |
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Reaction participants Show >> << Hide
- Name help_outline a 2'-deoxyribonucleoside 5'-diphosphate Identifier CHEBI:73316 Charge -3 Formula C5H8O9P2R SMILEShelp_outline O[C@H]1C[C@H]([*])O[C@@H]1COP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 56 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[thioredoxin]-disulfide
Identifier
RHEA-COMP:10700
Reactive part
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- Name help_outline L-cystine residue Identifier CHEBI:50058 Charge 0 Formula C6H8N2O2S2 Positionhelp_outline n/n+3 SMILEShelp_outline C([C@@H](N*)CSSC[C@@H](C(=O)*)N*)(=O)* 2D coordinates Mol file for the small molecule Search links Involved in 51 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,337 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a ribonucleoside 5'-diphosphate Identifier CHEBI:57930 Charge -3 Formula C5H8O10P2R SMILEShelp_outline [C@H]1([C@H]([C@@H](O)[C@@H](O1)*)O)COP(OP([O-])(=O)[O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1,694 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[thioredoxin]-dithiol
Identifier
RHEA-COMP:10698
Reactive part
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- Name help_outline L-cysteine residue Identifier CHEBI:29950 Charge 0 Formula C3H5NOS Positionhelp_outline n SMILEShelp_outline C(=O)(*)[C@@H](N*)CS 2D coordinates Mol file for the small molecule Search links Involved in 127 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-cysteine residue Identifier CHEBI:29950 Charge 0 Formula C3H5NOS Positionhelp_outline n+3 SMILEShelp_outline C(=O)(*)[C@@H](N*)CS 2D coordinates Mol file for the small molecule Search links Involved in 127 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:23252 | RHEA:23253 | RHEA:23254 | RHEA:23255 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits.
Qiu W., Zhou B., Darwish D., Shao J., Yen Y.
Ribonucleotide reductase (RR) is a highly regulated enzyme in the deoxyribonucleotide synthesis pathway. RR is responsible for the de novo conversion of ribonucleoside diphosphates to deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. Besides two subunits, hRRM1 an ... >> More
Ribonucleotide reductase (RR) is a highly regulated enzyme in the deoxyribonucleotide synthesis pathway. RR is responsible for the de novo conversion of ribonucleoside diphosphates to deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. Besides two subunits, hRRM1 and hRRM2, p53R2 is a newly identified member of RR family that is induced by ultraviolet light in a p53-dependent manner. To understand the molecular interaction of RR subunits, we employed a eukaryotic expression system to express and purify all three subunits. After in vitro reconstitution, the results of [(3)H]CDP reduction assay showed that both eukaryotic recombinant hRRM2 and p53R2 proteins could interact with hRRM1 to form functional RR holoenzyme. The reconstituted RR activity was time-dependent and the reaction rate reached the plateau phase after 40min incubation. No matter the concentration, RR holoenzyme reconstituted from p53R2 and hRRM1 could only achieve about 40-75% kinetic activity of that from hRRM2 and hRRM1. The synthetic C-terminal heptapeptide competition assays confirmed that hRRM2 and p53R2 share the same binding site on hRRM1, but the binding site on hRRM1 demonstrated higher affinity for hRRM2 than for p53R2. In allosteric regulation assay, the effect of activation or inhibition of hRRM1 with ATP or dATP suggested that these effectors could regulate RR activity independent of different RR small subunits. Taken together, the eukaryotic expression system RR holoenzyme will provide a very useful tool to understand the molecular mechanisms of RR activity and the interactions of its subunits. << Less
Biochem. Biophys. Res. Commun. 340:428-434(2006) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.