Enzymes
| UniProtKB help_outline | 1 proteins |
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Reaction participants Show >> << Hide
- Name help_outline a 2'-deoxyribonucleoside 3'-phosphate Identifier CHEBI:131705 Charge -2 Formula C5H8O6PR SMILEShelp_outline [C@H]1(O[C@H](CO)[C@H](C1)OP(=O)([O-])[O-])* 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; 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 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 2'-deoxyribonucleoside Identifier CHEBI:18274 Charge 0 Formula C5H9O3R SMILEShelp_outline OC[C@H]1O[C@@H]([*])C[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 52 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 992 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:10092 | RHEA:10093 | RHEA:10094 | RHEA:10095 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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The enzymatic cleavage of phosphate termini from polynucleotides.
Becker A., Hurwitz J.
J. Biol. Chem. 242:936-950(1967) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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3'-Phosphatase activity in T4 polynucleotide kinase.
Cameron V., Uhlenbeck O.C.
The purification of T4 polynucleotide kinase results in the copurification of an activity which will specifically remove the 3'-terminal phosphate from a variety of deoxyribonucleotides and ribonucleotides in the absence of ATP. This phosphatase activity requires magnesium, has a pH optiumum of 6. ... >> More
The purification of T4 polynucleotide kinase results in the copurification of an activity which will specifically remove the 3'-terminal phosphate from a variety of deoxyribonucleotides and ribonucleotides in the absence of ATP. This phosphatase activity requires magnesium, has a pH optiumum of 6.0, and is more active with deoxyribonucleotides than ribonucleotides. T4 polynucleotide kinase and the 3'-phosphatase activity copurify by gradient elution column chromatography on DEAE-cellulose, phosphocellulose, and hydroxylapatite. The two activities are included in and comigrate on Sephadex G-200. Polyacrylamide gel electrophoresis at PH 9.2 results in conigration of the two activities together with the major protein band. The two activities respond in parallel to heat inactivation at 35 degrees C and ATP, a substrate for the kinase only, protects both activities from heat inactivation. It is therefore suggested that the two activities are functions of the same protein molecule. << Less