Enzymes
Product List
AGA Human
Aspartylglucosaminidase Human Recombinant
AGA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
AGA Human, sf9
Aspartylglucosaminidase Human Recombinant, sf9
ANSA E.coli
Cytoplasmic L-asparaginase I E.Coli Recombinant
ANSA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ASRGL1 Human
ASRGL1 Human Recombinant
ASRGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
L-Asparaginase
L-Asparaginase
L-Asparaginase purified from E.coli ASI.357 is a tetrameric polypeptide chain having a molecular mass of 34,564 Dalton.
Introduction
Asparaginase is an enzyme that catalyzes the hydrolysis of the amino acid asparagine into aspartic acid and ammonia . It is primarily classified into two types based on its source: bacterial asparaginase and plant asparaginase . Bacterial asparaginases are further divided into subtypes I and II, depending on their intra- or extracellular localization .
Asparaginase exhibits several key biological properties. It is produced by a variety of organisms, including bacteria, fungi, plants, and animals . The enzyme is predominantly expressed in microorganisms such as Escherichia coli and Erwinia chrysanthemi . The tissue distribution of asparaginase varies, with significant expression in the liver and kidneys .
The primary biological function of asparaginase is to catalyze the degradation of asparagine, an essential amino acid for leukemic cells, into ammonia and aspartate . This activity inhibits protein biosynthesis in lymphoblasts, making it a crucial enzyme in the treatment of acute lymphoblastic leukemia (ALL) . Additionally, asparaginase plays a role in immune responses and pathogen recognition by depleting asparagine, which is vital for the survival of certain pathogens .
Asparaginase exerts its effects by hydrolyzing asparagine into aspartic acid and ammonia . This depletion of asparagine leads to the inhibition of protein synthesis in leukemic cells, ultimately causing apoptotic cell death . The enzyme interacts with various molecules and cells, including binding partners such as asparagine and aspartic acid . The downstream signaling cascades involve the activation of apoptotic pathways in leukemic cells .
The expression and activity of asparaginase are regulated through multiple mechanisms. Transcriptional regulation involves the control of gene expression by various transcription factors . Post-translational modifications, such as phosphorylation and glycosylation, also play a role in modulating the enzyme’s activity . Additionally, the enzyme’s activity can be influenced by the availability of substrates and cofactors .
Asparaginase has several applications in biomedical research, diagnostic tools, and therapeutic strategies. In biomedical research, it is used to study the metabolism of asparagine and its role in cancer . As a diagnostic tool, asparaginase activity can be measured to assess the presence of certain cancers . Therapeutically, asparaginase is a key component in the treatment of acute lymphoblastic leukemia (ALL) and lymphoblastic lymphoma . It is also used in the food industry to reduce the formation of acrylamide, a carcinogenic compound, during the cooking process .
Throughout the life cycle, asparaginase plays a vital role in various physiological processes. During development, it is involved in the biosynthesis of amino acids and proteins . In aging, the enzyme’s activity may decline, leading to alterations in amino acid metabolism . In disease states, such as cancer, asparaginase is crucial for depleting asparagine and inhibiting the growth of cancer cells .
