Search results for NDP

Showing 21 results out of 32

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Chemical Compound (4 results from a total of 4)

NDP

Identifier: R-ALL-8870906
Compartment: extracellular region
Primary external reference: ChEBI: nucleoside diphosphate: 16862

NDP

Identifier: R-ALL-6806885
Compartment: cytosol
Primary external reference: ChEBI: nucleoside diphosphate: 16862

NDP

Identifier: R-ALL-30181
Compartment: nucleoplasm
Primary external reference: ChEBI: nucleoside diphosphate: 16862
Identifier: R-ALL-8866401
Compartment: cytosol
Primary external reference: ChEBI: nucleoside 5'-diphosphate(3-): 57930

Interactor (1 results from a total of 1)

NDP

Identifier: Q00604
Species: Homo sapiens
Primary external reference: UniProt: Q00604

Set (5 results from a total of 5)

Identifier: R-ALL-482803
Compartment: mitochondrial matrix
Identifier: R-ALL-482627
Compartment: cytosol
Identifier: R-ALL-6788801
Compartment: mitochondrial matrix
Identifier: R-ALL-6788807
Compartment: nucleoplasm
Identifier: R-ALL-6788782
Compartment: cytosol

Reaction (5 results from a total of 15)

Identifier: R-HSA-482621
Species: Homo sapiens
Compartment: cytosol
Cytosolic nucleoside diphosphate kinases catalyze the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ADP to form the corresponding nucleoside 5'-diphosphates and ATP. These kinases are ubiquitously expressed enzymes with broad substrate specificities (Berg and Joklik 1954; Parks and Agarwal 1973). Three human cytosolic nucleoside diphosphate kinase proteins, NME1, 2, and 3, have been characterized biochemically (Gilles et al. 1991; Schaertl et al. 1998; Erent et al. 2001; Chen et al. 2003). All are catalytically active as hexamers: homohexamers of NME1, 2, and 3 have been described, as have heterohexamers containing all possible combinations of NME1 and 2 (Gilles et al. 1991; Erent et al. 2001).

While the high ratio of ATP to ADP concentrations in the cytosol normally favors the conversion of (d)NDP and ATP to (d)NTP and ADP, the reversibility of the reactions and the overlapping substrate specificities of the enzymes suggest that this group of reverse reactions can buffer the intracellular nucleotide pool and regulate the relative concentrations of individual nucleoside di- and tri-phosphates in the pool.

Identifier: R-HSA-482619
Species: Homo sapiens
Compartment: cytosol
Cytosolic nucleoside diphosphate kinases catalyze the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ATP to form the corresponding nucleoside 5'-triphosphates and ADP. These kinases are ubiquitously expressed enzymes with broad substrate specificities (Berg and Joklik 1954; Parks and Agarwal 1973). Three human cytosolic nucleoside diphosphate kinase proteins, NME1, 2, and 3, have been characterized biochemically (Gilles et al. 1991; Schaertl et al. 1998; Erent et al. 2001; Chen et al. 2003). All are catalytically active as hexamers: homohexamers of NME1, 2, and 3 have been described, as have heterohexamers containing all possible combinations of NME1 and 2 (Gilles et al. 1991; Erent et al. 2001).

While cytosolic nucleoside diphosphate kinases can efficiently use several nucleotide triphosphates as a phosphate donor, the high concentrations of ATP relative to other nucleoside triphosphates in vivo makes it the likely major phosphate donor in these reactions and only reactions with ATP as the phosphate donor are annotated. All of these phosphorylation reactions are freely reversible in vitro (Parks and Agarwal 1973; Schaertl et al. 1998), but the high ratio of ATP to ADP concentrations in the cytosol should favor the conversion of (d)NDP and ATP to (d)NTP and ADP.

Identifier: R-HSA-482804
Species: Homo sapiens
Compartment: mitochondrial matrix, mitochondrial inner membrane
Nucleoside diphosphate kinase NME4 associated with the inner mitochondrial membrane (Tokarska-Schlattner et al. 2008) catalyzes the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ATP to form the corresponding nucleoside 5'-triphosphates and ADP. The active form of the enzyme is a hexamer of NME4 polypeptides whose amino-terminal 33 residues, a mitochondrial translocation signal, have been removed (Milon et al. 2000). The substrate specificity of NME4 has not been examined in detail but is inferred to be broad like that of the homologous NME1, 2, and 3 kinases (Schaertl et al. 1998).
Identifier: R-HSA-482812
Species: Homo sapiens
Compartment: mitochondrial matrix, mitochondrial inner membrane
Nucleoside diphosphate kinase NME4 associated with the inner mitochondrial membrane (Tokarska-Schlattner et al. 2008) catalyzes the reversible reaction of ribonucleoside and deoxyribonucleoside 5'-diphosphates with ADP to form the corresponding nucleoside 5'-diphosphates and ATP. The active form of the enzyme is a hexamer of NME4 polypeptides whose amino-terminal 33 residues, a mitochondrial translocation signal, have been removed (Milon et al. 2000). The substrate specificity of NME4 has not been examined in detail, but is inferred to be broad like that of the homologous NME1, 2, and 3 kinases (Schaertl et al. 1998).
Identifier: R-HSA-6788798
Species: Homo sapiens
Compartment: mitochondrial matrix
Adenylate kinases (AKs) are nucleoside monophosphate kinases, which catalyze the phosphorylation of AMP by using ATP or GTP as phosphate donors. AKs are thus involved in maintaining the homeostasis of cellular nucleotides. CMP, dCMP and dAMP are other substrates phosphorylated with less efficiency by AKs. When GTP is the phosphate donor, only AMP and CMP are efficiently phosphorylated. Adenylate kinase 4 (AK4) can mediate nucleotide homeostasis in the mitochondrion (Panayiotou et al. 2010).

Protein (5 results from a total of 6)

Identifier: R-HSA-60026
Species: Homo sapiens
Compartment: mitochondrial inner membrane
Primary external reference: UniProt: NME4: O00746
Identifier: R-HSA-60022
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: NME1: P15531
Identifier: R-HSA-60024
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: NME2: P22392
Identifier: R-HSA-6803324
Species: Homo sapiens
Compartment: ficolin-1-rich granule lumen
Primary external reference: UniProt: NME2: P22392
Identifier: R-HSA-6806464
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: P22392

Pathway (1 results from a total of 1)

Identifier: R-HSA-499943
Species: Homo sapiens
Compartment: cytosol, mitochondrial intermembrane space, nucleoplasm, mitochondrial inner membrane, mitochondrial matrix
An array of kinases catalyze the reversible phosphorylation of nucleotide monophosphates to form nucleotide diphosphates and triphosphates.

Nucleoside monophosphate kinases catalyze the reversible phosphorylation of nucleoside and deoxynucleoside 5'-monophosphates to form the corresponding nucleoside 5'-diphosphates. Most appear to have restricted specificities for nucleoside monophosphates, and to use ATP preferentially (Van Rompay et al. 2000; Anderson 1973; Noda 1973). The total number of human enzymes that catalyze these reactions in vivo is not clear. In six cases, a well-defined biochemical activity has been associated with a purified protein, and these are annotated here. However, additional nucleoside monophosphate kinase-like human proteins have been identified in molecular cloning studies whose enzymatic activities are unknown, and several distinctive nucleoside monophosphate kinase activities detected in cell extracts, e.g., a GTP-requiring adenylate kinase activity (Wilson et al. 1976) and one or more guanylate kinase activities (Jamil et al. 1975) have not been unambiguously associated with specific human proteins.

The nucleoside monophosphates against which each of the six well-characterized enzymes is active is shown in the table (Van Rompay et al. 2000). All six efficiently use ATP as a phosphate donor, but have some activity with other nucleoside triphosphates as well in vitro. The high concentrations of ATP relative to other nucleoside triphosphates in vivo makes it the likely major phosphate donor in these reactions under most conditions.

All of these phosphorylation reactions are freely reversible in vitro when carried out with purified enzymes and substrates, having equilibrium constants near 1. In vivo, high ratios of ATP to ADP are likely to favor the forward direction of these reactions, i.e., the conversion of (d)NMP and ATP to (d)NDP and ADP. At the same time, the reversibility of the reactions and the overlapping substrate specificities of the enzymes raises the possibility that this group of reactions can buffer the intracellular nucleotide pool and regulate the relative concentrations of individual nucleotides in the pool: if any one molecule builds up to unusually high levels, multiple routes appear to be open not only to dispose of it but to use it to increase the supply of less abundant nucleotides.

Ribonucleotide reductase catalyzes the synthesis of deoxyribonucleotide diphosphates from ribonucleotide diphosphates.

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