Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase, Testicular Tissue Protein Li 14, EC 2.7.1.
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ADK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (22-362a.a.) and having a molecular mass of 40.5kDa.
ADK is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Adenosine kinase (ADK) is a key enzyme regulating levels of adenosine and adenine nucleotides. It plays a vital role in various physiological processes, particularly in the cardiovascular, nervous, respiratory, and immune systems. ADK inhibitors are of significant pharmacological interest for their potential as anti-inflammatory agents and for increasing adenosine levels in the blood vessels.
Recombinant ADK, expressed in E. coli, is a single polypeptide chain devoid of glycosylation. It encompasses amino acids 22 to 362, resulting in a molecular weight of 40.5 kDa. The protein includes an N-terminal His-tag (21 amino acids) and is purified using proprietary chromatographic methods.
The ADK protein solution is provided at a concentration of 0.5 mg/ml and contains the following components: 20% glycerol, 20 mM Tris-HCl buffer (pH 8.0), 1 mM DTT, 1 mM EDTA, and 50 mM NaCl.
The specific activity of the enzyme is measured to be greater than 30 pmol/min/µg. Specific activity represents the amount of enzyme required to convert 1.0 picomole of adenosine to AMP per minute. This measurement is conducted at 37°C and pH 7.5 using a coupled enzyme assay system involving pyruvate kinase (PK) and lactate dehydrogenase (LDH).
Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase, Testicular Tissue Protein Li 14, EC 2.7.1.
MGSSHHHHHH SSGLVPRGSH MRENILFGMG NPLLDISAVV DKDFLDKYSL KPNDQILAED KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA ATFFGCIGID KFGEILKRKA AEAHVDAHYY EQNEQPTGTC AACITGDNRS LIANLAAANC YKKEKHLDLE KNWMLVEKAR
VCYIAGFFLT VSPESVLKVA HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN ETEAATFARE QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR TGCTFPEKPD
FH.
Human recombinant adenosine kinase is typically produced in Escherichia coli (E. coli) and is available in a purified, active form. The enzyme consists of 362 amino acids and has a molecular mass of approximately 40.5 kDa . It is often tagged with a His tag at the N-terminus to facilitate purification through standard chromatography techniques .
Adenosine kinase is involved in the regulation of intra- and extracellular adenosine concentrations. Adenosine itself is an important modulator of central nervous system functions and acts as a signaling molecule in various physiological processes, including hypoxia, inflammation, and nociception . By phosphorylating adenosine, ADK helps regulate these processes and maintain cellular homeostasis.
The activity of adenosine kinase is critical for several biological functions. Inhibition of ADK can lead to an increase in local adenosine concentrations, which has been shown to reduce seizure susceptibility and nociception in vivo . Dysregulation of ADK activity is associated with various pathologies, including diabetes, epilepsy, and cancer . As a result, ADK is considered a potential therapeutic target for drug discovery, with adenosine-regulating drugs being tested as new analgesic and anti-inflammatory agents .
Adenosine kinase is responsible for the phosphorylation and subsequent clinical activity of several therapeutically useful nucleosides. These include the antiviral drug ribavirin, the immunosuppressive drug mizoribine, and the anticancer C-nucleoside tiazofurin . The enzyme’s role in these processes highlights its importance in the development of new therapeutic agents.
The X-ray crystallographic structure of human adenosine kinase has been described, providing a structural basis for the rational design and optimization of new ADK inhibitors . This structural information is invaluable for researchers aiming to develop novel drugs that target ADK and modulate its activity for therapeutic purposes.