What type of enzyme is asparagine synthetase?

Published by Anaya Cole on

What type of enzyme is asparagine synthetase?

Asparagine synthetase (or aspartate-ammonia ligase) is a chiefly cytoplasmic enzyme that generates asparagine from aspartate. This amidation reaction is similar to that promoted by glutamine synthetase.

How is asparagine synthesis?

Asparagine Synthetase (ASNS) catalyzes the synthesis of the non-essential amino acid asparagine (Asn) from aspartate (Asp) and glutamine (Gln). ASNS expression is highly regulated at the transcriptional level, being induced by both the Amino Acid Response (AAR) and the Unfolded Protein Response (UPR) pathways.

What is asparagine function?

Asparagine is needed to produce many proteins but also plays other roles. Asparagine helps to break down toxic ammonia within cells, is important for protein modification, and is needed for making a certain molecule that transmits signals in the brain (a neurotransmitter).

How does asparagine regulate Mtor?

Like glutamine, asparagine signals to mTORC1 through Arf1 in the absence of the Rag GTPases. Both the Rag-dependent and Rag-independent pathways required the lysosome and lysosomal function for mTORC1 activation. Our results show that mTORC1 is differentially regulated by amino acids through two distinct pathways.

What is the function of asparagine in the body?

Asparagine helps to break down toxic ammonia within cells, is important for protein modification, and is needed for making a certain molecule that transmits signals in the brain (a neurotransmitter).

What causes L glutamine deficiency?

Deficiency Factors Injury, surgery, burns, infections, malnutrition and high-intensity exercise are among the situations involving physical stress that engender glutamine deficiency.

What is asparagine and its function?

Asparagine, a non-essential amino acid is important in the metabolism of toxic ammonia in the body through the action of asparagine synthase which attaches ammonia to aspartic acid in an amidation reaction. Asparagine is also used as a structural component in many proteins.

What is the function of asparagine?

Why do cells need asparagine?

All cells need asparagine for their protein synthesis and growth. Normal cells will obtain the majority of its asparagine needs through its own synthesis. Cancer cells also need asparagine to grow and proliferate, even more than normal cells, but most cancer cells cannot produce enough asparagine.

Why is asparagine so important?

l-Asparagine is an amino acid required for the synthesis of many important cellular proteins in normal human cells. Many tumor cells do not have this capacity, due to a lack of the enzyme l-asparagine synthetase, and therefore require an exogenous supply of the amino acid.

What food contains asparagine?

Other asparagine-rich foods include dairy products, beef, poultry, eggs, fish, seafood, potatoes, legumes, nuts, seeds, soy, and whole grains. The scientists are considering an early-phase clinical trial that would employ a low-asparagine diet in conjunction with chemotherapy and immunotherapy.

Does glutamine cause hair loss?

Healthy levels of glutamine can prevent further hair loss and even help regrow hair. Keratin is the main component of hair, and it contains large amounts of cysteine. Cysetine is high in sulfur, and therefore plays a crucial role in healthy hair.

Is asparagine charged at physiological pH?

Charge of the amino acid side chains At pH=7, two are negative charged: aspartic acid (Asp, D) and glutamic acid (Glu, E) (acidic side chains), and three are positive charged: lysine (Lys, K), arginine (Arg, R) and histidine (His, H) (basic side chains).

What is the function of asparagine synthetase?

Asparagine synthetase: Function, structure, and role in disease Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression.

Does aspartate react with glutamine in asparagine synthesis?

Although the enzyme name leads one to focus on asparagine synthesis, given the overall reaction, the activity does consume glutamine and aspartate, and produce glutamate. Whether or not ASNS actually impacts the cellular homeostasis of one or more of the other reactants remains speculative.

What is Escherichia coli derived asparagine synthetase?

Escherichia coli derived asparagine synthetase is a dimeric protein with each subunit folding into two distinct domains. The N-terminal region consists of two layers of six-stranded antiparallel β -sheets between which is the active site responsible for the hydrolysis of glutamine.

Does asparagine synthetase contribute to chemotherapy resistance in leukemia?

Above average presence of asparagine synthetase in certain leukemia strains has been linked to be a significant contributing factor of chemotherapy resistance, particularly to the chemotherapy drug, L-asparaginase.

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