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N2635

Sigma-Aldrich

Nucleoside 5′-Diphosphate Kinase from bovine liver

buffered aqueous glycerol solution, ≥1,000 units/mg protein (biuret)

Synonym(s):

NDK, UDPkinase, nonmetastatic23(NM23), uridine diphosphate kinase, ATP:nucleoside diphosphate phosphotransferase, NDPK

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

bovine liver

form

buffered aqueous glycerol solution

specific activity

≥1,000 units/mg protein (biuret)

storage condition

(Tightly closed)

technique(s)

activity assay: suitable

foreign activity

lactic dehydrogenase, myokinase, β-NADH oxidase, nucleoside monophosphokinase and ATPase ≤0.1%

storage temp.

2-8°C

General description

Research area: Cell Signaling

Nucleoside 5′-Diphosphate Kinase (NDK) is a ubiquitous housekeeping enzyme. Nucleoside Diphosphate Kinase exists in two isoforms in eukaryotic cells, NDK-A and NDK-B. These enzymes are found expressed both in the mitochondria and the cytoplasm.

Application

Nucleoside 5′-Diphosphate Kinase has been used:
  • nucleoside diphosphate kinase (NDPK) assays
  • coupled NDPK-luciferase assay to determine the amounts of Ras-bound guanosine triphosphate (GTP)
  • non-metastatic protein 23 (NM23) growth stimulation assay
  • in a study to assess inhibition of type I Fc epsilon receptor mediated Ca2+ influx and mediator secretion in rat mucosal mast cells
  • in a study to investigate protein synthesis in rabbit reticulocytes

Biochem/physiol Actions

Nucleoside 5′-Diphosphate Kinases (NDKs) aid in the synthesis of nucleoside triphosphates (NTPs) by transferring a phosphate group from ATP to nucleoside diphosphates (NDPs). NDKs provide NTPs for nucleic acid synthesis, cytidine 5′-triphosphate (CTP) for lipid synthesis, uridine 5′-triphosphate (UTP) for polysaccharide synthesis, and guanosine triphosphate (GTP) for protein elongation, signal transduction, and microtubule polymerization.

Unit Definition

One unit will convert 1.0 μmole each of TDP and ATP to TTP and ADP per min at pH 7.6 at 25 °C in a coupled system with PK/LDH.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Krisztina Takács-Vellai et al.
Cellular and molecular life sciences : CMLS, 72(8), 1447-1462 (2014-12-30)
In textbooks of biochemistry, nucleoside diphosphate conversion to a triphosphate by nucleoside diphosphate 'kinases' (NDPKs, also named NME or NM23 proteins) merits a few lines of text. Yet this essential metabolic function, mediated by a multimeric phosphotransferase protein, has effects
Maja Herak Bosnar et al.
Molecular and cellular biochemistry, 329(1-2), 63-71 (2009-04-18)
The family of Nm23/NDPK (nucleoside diphosphate kinase) proteins regulates a vast variety of cellular processes and, therefore, participates in important physiological events like proliferation, differentiation, molecular transport, and apoptosis. The majority of experimental data concerning this gene family has been
Shaobai Huang et al.
Annals of botany, 96(4), 703-715 (2005-07-20)
Anoxia-tolerant plant tissues synthesize a number of proteins during anoxia, in addition to the 'classical anaerobic proteins' involved in glycolysis and fermentation. The present study used a model system of rice coleoptile tips to elucidate patterns of protein synthesis in
Harjeet Kaur et al.
The Biochemical journal, 393(Pt 1), 235-243 (2005-09-15)
In growth-factor-stimulated signal transduction, cell-surface receptors recruit PI3Ks (phosphoinositide 3-kinases) and Ras-specific GEFs (guanine nucleotide-exchange factors) to the plasma membrane, where they produce 3'-phosphorylated phosphoinositide lipids and Ras-GTP respectively. As a direct example of pathway networking, Ras-GTP also recruits and
R Roy et al.
Biochemical and biophysical research communications, 122(3), 1418-1425 (1984-08-16)
Under standard conditions, in the presence of GTP, highly purified eIF-2 and Co-eIF-2 factor preparations efficiently stimulated AUG-codon dependent but not physiological mRNA-dependent Met-tRNAf binding to 40S ribosomes. Replacement of GTP by a nonhydrolyzable GTP analog, GMP-PNP, in the above

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