800-73-7

Basic information

• Product Name: [[5-(4-amino-2-oxo-pyrimidin-1-yl)-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid
• Synonyms: [[5-(4-amino-2-oxo-pyrimidin-1-yl)-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid;2'-deoxycytidine diphosphate;2'-Deoxycytidine 5'-(trihydrogen pyrophosphate);2'-Deoxycytidine pyrophosphate;5'-DCDP;Deoxycytidine 5'-diphosphate;Deoxycytidine diphosphate
• CAS NO: 800-73-7
• Molecular Formula: C₉H₁₅N₃O₁₀P₂
• Molecular Weight: 387.177
• Mol File: 800-73-7.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 726.8°Cat760mmHg
• Flash Point: 393.4°C
• Appearance: /
• Density: 2.22g/cm³
• CAS DataBase Reference: [[5-(4-amino-2-oxo-pyrimidin-1-yl)-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid(CAS DataBase Reference)
• NIST Chemistry Reference: [[5-(4-amino-2-oxo-pyrimidin-1-yl)-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid(800-73-7)
• EPA Substance Registry System: [[5-(4-amino-2-oxo-pyrimidin-1-yl)-3-hydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid(800-73-7)

Safety Data

• Hazardous Substances Data: 800-73-7(Hazardous Substances Data)

Usage

Definition

ChEBI: A 2'-deoxycytidine phosphate that is the 2'- deoxy derivative of cytidine 5'-diphosphate (CDP).

Upstream product

• 1032-65-1 cytidine 5'-(dihydrogen phosphate) 
• 63-38-7 cytidine diphosphate 
• 2056-98-6 2'-deoxycytidine 5'-triphosphate 

Downstream Products

• 820-11-1 3-phosphoglyceric acid 
• 2056-98-6 2'-deoxycytidine 5'-triphosphate 

Relevant articles and documents

A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover

Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to the corresponding deoxyribonucleotides, used in DNA synthesis and repair. Two different mechanisms help deliver the required electrons to the RNR active site. Formate can be used as reductant directly in the active site, or glutaredoxins or thioredoxins reduce a C-terminal cysteine pair, which then delivers the electrons to the active site. Here, we characterized a novel cysteine-rich C-terminal domain (CRD), which is present in most class II RNRs found in microbes. The NrdJd-type RNR from the bacterium Stackebrandtia nassauensis was used as a model enzyme. We show that the CRD is involved in both higher oligomeric state formation and electron transfer to the active site. The CRD-dependent formation of high oligomers, such as tetramers and hexamers, was induced by addition of dATP or dGTP, but not of dTTP or dCTP. The electron transfer was mediated by an array of six cysteine residues at the very C-terminal end, which also coordinated a zinc atom. The electron transfer can also occur between subunits, depending on the enzyme's oligomeric state. An investigation of the native reductant of the system revealed no interaction with glutaredoxins or thioredoxins, indicating that this class IIRNRuses a different electron source. Our results indicate that the CRD has a crucial role in catalytic turnover and a potentially new terminal reduction mechanism and suggest that the CRD is important for the activities of many class II RNRs.

Nucleoside-Triphosphatase Activity of an ATP-Dependent Enzyme, N-Methylhydantoin Amidohydrolase

N-Methylhydantoin amidohydrolase, which catalyzes ATP-dependent hydrolysis of N-methylhydantoin to N-carbamoylsarcosine, was found to hydrolyze several nucleoside triphosphates to nucleoside diphosphates not only in the presence but also in the absence of amide substrates.Amide substrates, such as N-methylhydantoin and dihydrouracil, seem to be absolutely necessary for hydrolysis of ATP and dATP.However, N-methylhydantoin inhibited the hydrolysis of nucleoside triphosphates other than ATP and dATP.The kinetic data suggest that the presence of an amide substrate changes the affinity of the enzyme toward nucleoside triphosphates.