Is argininosuccinic acid an amino acid?

Showing metabocard for Argininosuccinic acid (HMDB0000052) Arginosuccinic acid is a basic amino acid. Some cells synthesize it from citrulline, aspartic acid and use it as a precursor for arginine in the urea cycle or Citrulline-NO cycle.

What causes Argininosuccinic aciduria?

Argininosuccinic aciduria is caused by alterations (mutations) in the ASL gene. Genes provide instructions for creating proteins that play a critical role in many functions of the body. When a mutation of a gene occurs, the protein product may be faulty, inefficient, or absent.

What is ASA disease?

Argininosuccinic aciduria (ASA) is a condition that causes dangerous amounts of ammonia to build up in the body. ASA is considered an amino acid condition because people with ASA are unable to process a waste product, ammonia, that is produced when the body breaks down amino acids.

What does Argininosuccinate synthase do?

Argininosuccinate synthase or synthetase (ASS; EC 6.3. 4.5) is an enzyme that catalyzes the synthesis of argininosuccinate from citrulline and aspartate. In humans, argininosuccinate synthase is encoded by the ASS gene located on chromosome 9.

How argininosuccinate is formed?

Formation of Argininosuccinate The reaction is driven forward by hydrolysis of pyrophosphate to inorganic phosphate. Argininosuccinate formation is considered as the rate-limiting step for urea synthesis. This reaction incorporates the second nitrogen atom of the urea molecule donated by aspartate.

What is the function of argininosuccinate in urea cycle?

Argininosuccinate lyase (ASL) hydrolyzes argininosuccinate to arginine and fumarate. It has a similar distribution to ASS [50]. In the liver, its main function is ureagenesis: liberated arginine is subsequently used in the urea cycle and hence there is no net arginine production [60].

What is the cause of Argininosuccinate lyase deficiency?

Defect: Argininosuccinate Lyase (ASL) Deficiency, also known as Argininosuccinic Aciduria (AA), is the result of a mutated or deficient argininosuccinate lyase enzyme. This defective or deficient enzyme leads to inadequate ureagenesis, accumulation of argininosuccinic acid, and deficient endogenous arginine production.

What is acid Uria?

Abstract. Organic acidemias or acidurias are a class of disorders characterized by the excretion of organic acids in the urine. This class of inborn error is typically caused by a deficiency in enzymatic activity involved with the catabolism of amino acids, though other biochemical pathways may be involved as well.

Is Tyrosinemia curable?

There is currently no cure for tyrosinemia type 1. Individuals with this condition need to be on a special diet restricted in two amino acids , tyrosine and phenylalanine, throughout life. Affected individuals may also be treated with a medication called nitisinone.

What is Argininemia?

Argininemia (ARG) is a condition that causes harmful amounts of arginine and ammonia to build up in the body. It is considered an amino acid condition because people affected with ARG are unable to break down an amino acid, a small molecule that makes up proteins, known as arginine.

What is a positive Asa?

High levels of argininosuccinic acid can indicate that your child has a metabolic disorder called argininosuccinic acidemia (ASA). A positive result does not mean you baby has ASA, but more testing is needed to know for sure.

How do you say Argininosuccinic aciduria?

What is ornithine transcarbamylase?

Ornithine transcarbamylase deficiency is an inherited disorder that causes ammonia to accumulate in the blood. Ammonia, which is formed when proteins are broken down in the body, is toxic if the levels become too high. The nervous system is especially sensitive to the effects of excess ammonia.

Where does cleavage of argininosuccinate take place?

The enzyme’s cleavage of the argininosuccinate, to form fumarate and arginine, occurs through an E1cb elimination reaction. The base initiates the reaction by deprotonating the carbon adjacent to the arginine, or leaving group.

What is ornithine made from?

Ornithine itself is a non-protein amino acid formed mainly from L-glumate in plants, and synthesized from the urea cycle in animals as a result of the reaction catalyzed by enzymes in arginine.

Why is urea cycle called ornithine?

The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH₂)₂CO from ammonia (NH₃). This cycle occurs in ureotelic organisms. The urea cycle converts highly toxic ammonia to urea for excretion.

Where is arginase found in the body?

In most mammals, two isozymes of this enzyme exist; the first, Arginase I, functions in the urea cycle, and is located primarily in the cytoplasm of the liver. The second isozyme, Arginase II, has been implicated in the regulation of the arginine/ornithine concentrations in the cell.

Can the Argininosuccinate synthetase deficiency be treated?

The main treatments for CTLN1 include a low-protein, high-calorie diet with amino acid supplements, particularly arginine. The Ucyclyd protocol, using buphenyl and ammonul, is used for treatment as well. Hyperammonemia is treated with hemodialysis; intravenous arginine, sodium benzoate, and sodium phenylacetate.

What is ornithine used for?

Ornithine is commonly used by mouth for improving athletic performance. It is also used for weight loss, wound healing, and to increase sleep quality. But there is limited scientific research to support these other uses. Don’t confuse ornithine with ornithine alpha-ketoglutarate (OKG) or L-Ornithine-L-Aspartate.

Where is citrulline produced?

small intestine Citrulline is an intermediate metabolic amino acid produced mainly by enterocytes of the small intestine.

How is ammonia broken down?

When you eat proteins, the body breaks them down into amino acids. Ammonia is produced from leftover amino acids, and it must be removed from the body. The liver produces several chemicals (enzymes) that change ammonia into a form called urea, which the body can remove in the urine.

Where is Argininosuccinate synthetase found?

outer mitochondrial membrane Argininosuccinate synthase is located on the outer mitochondrial membrane [5], utilizing both citrulline and aspartate to produce argininosuccinate. Argininosuccinate lyase catalyzes the cleavage of argininosuccinate to produce arginine and fumarate.

How is Argininosuccinase deficiency treated?

Intravenous benzoate, arginine, and phenylacetate administration may be indicated as initial therapy for hyperammonemia, but such combined therapy is appropriate only prior to specific diagnosis. Hemodialysis, if available, reduces the blood ammonia levels more efficiently and quickly.

How do you pronounce Argininosuccinate?

What is homocystinuria?

Homocystinuria (HCU) is a rare but potentially serious inherited condition. It means the body can’t process the amino acid methionine. This causes a harmful build-up of substances in the blood and urine.

Is Argininosuccinate toxic?

Argininosuccinic aciduria, is an inherited disorder that causes the accumulation of argininosuccinic acid (also known as ASA) in the blood and urine. Some patients may also have an elevation of ammonia, a toxic chemical, which can affect the nervous system.

What enzyme causes Citrullinemia?

Citrullinemia type I (CTLN1) is a rare autosomal recessive genetic disorder that includes a neonatal acute (classic) form, a milder late-onset form, a form that begins during or after pregnancy, and an asymptomatic form. CTLN1 is caused by deficiency or absence of the enzyme argininosuccinate synthetase (ASS).

What are the symptoms of tyrosinemia?

Symptoms and physical findings associated with tyrosinemia type I appear in the first months of life and include failure to gain weight and grow at the expected rate (failure to thrive), fever, diarrhea, vomiting, an abnormally enlarged liver (hepatomegaly), and yellowing of the skin and the whites of the eyes ( …

Can adults have tyrosinemia?

The less common type is seen in older children and adults. Tyrosinemia 1 in infants: Babies usually show effects of the condition within the first few months of life.

Is tyrosinemia hereditary?

Tyrosinemia is hereditary; in order to have the disease, a child must get a mutation in the gene for tyrosinemia from each parent. In families where both parents carry a mutation, there is a one in four risk that a child will have tyrosinemia.