Methylmalonic acidemias, also called methylmalonic acidurias, are a group of inherited metabolic disorders, that prevent the body from properly breaking down proteins and fats. This leads to a buildup of a toxic level of methylmalonic acid in body liquids and tissues. Due to the disturbed branched-chain amino acids (BCAA) metabolism, they are among the classical organic acidemias. Methylmalonic acidemias have varying diagnoses, treatment requirements, and prognoses, which are determined by the specific genetic mutation causing the inherited form of the disorder. The first symptoms may begin as early as the first day of life or as late as adulthood. Symptoms can range from mild to life-threatening. Some forms can result in death if undiagnosed or left untreated. Methylmalonic acidemias are found with an equal frequency across ethnic boundaries.
Signs and symptoms Depending on the affected gene(s) and mutation, the present symptoms can range from mild to life-threatening.
Acidosis Cardiomyopathy Coma Dehydration Developmental delays Dysmorphic features Encephalopathy, progressive Failure to thrive Gastrointestinal disease Hepatomegaly Hyperammonemia Hyperglycinemia/ Hyperglycinuria Hypoglycemia Hypotonia Infections, recurrent Ketonemia/ Ketonuria Kidney failure Lethargy Low concentrations of red blood cells, white blood cells and blood platelets Memory problems Pancreatitis Respiratory distress Speech delay Seizure Stroke Vomiting As a rule, methylmalonic acidemias are not apparent at birth as symptoms do not present themselves until proteins are added to the infant's diet. Because of this, symptoms typically manifest anytime within the first year of life. However, there are also forms that only develop symptoms in adulthood.
Cause
Genetic
Methylmalonic acidemias have an autosomal recessive inheritance pattern, which means the defective gene is located on an autosome, and two copies of the gene—one from each parent—must be inherited to be affected by the disorder. The parents of a child with an autosomal recessive disorder are carriers of one copy of the defective gene, but are usually not affected by the disorder. The exception is methylmalonic acidemia and homocystinuria, cblX type due to variants in HCFC1 gene, which is inherited in an X-linked recessive manner. The following are the known genotypes responsible for isolated methylmalonic acidemias:
The mut type can further be divided into mut0 and mut- subtypes, with mut0 characterized by a complete lack of methylmalonyl-CoA mutase and more severe symptoms and mut- characterized by a decreased amount of mutase activity. Furthermore, the following genes are also responsible for methylmalonic acidemias:
Nutritional Though not always grouped together with the inherited versions, a severe nutritional vitamin B12 deficiency can also result in syndrome with identical symptoms and treatments as the genetic methylmalonic acidemias. Methylmalonyl-CoA requires vitamin B12 to form succinyl-CoA. When the amount of B12 is insufficient for the conversion of cofactor methylmalonyl-CoA into succinyl-CoA, the buildup of unused methylmalonyl-CoA eventually leads to methylmalonic acidemia. This diagnosis is often used as an indicator of vitamin B12 deficiency in serum.
Pathophysiology
In methylmalonic acidemias, the body is unable to break down properly:
essential amino acids: methionine, valine, threonine and isoleucine propionic acid from intestinal fermentation odd-chain fatty acids cholesterol side chain As a result, methylmalonic acid builds up in liquids and tissues. Those afflicted with this disorder are either lacking functional copies or adequate levels of one or more of the following enzymes:
methylmalonyl-CoA mutase (MUT) acyl-CoA synthetase family member 3 (ACSF3) methylmalonyl-CoA epimerase (MCEE) enzymes involved in adenosylcobalamin synthesis These are briefly introduced below:
Methylmalonyl-CoA mutase
It is estimated that as many as 60% of isolated methylmalonic acidemia cases are the result of a mutated MMUT gene, which encodes the protein methylmalonyl-CoA mutase. This enzyme is responsible for the digestion of potentially toxic derivatives of the breakdown of the above-mentioned amino acids and fats, primarily cholesterol, particularly this enzyme converts methylmalonyl-CoA into succinyl-CoA. Without this enzyme, the body has no means to neutralize or remove methylmalonic acid and related compounds. The action of this enzyme can also be crippled by mutations in the MMAA, MMAB, and MMADHC genes, each of which encodes a protein required for normal functioning of methylmalonyl-CoA mutase.
Acyl-CoA synthetase family member 3 CMAMMA is probably the most common form of methylmalonic acidemias based on its allele frequency, but is rarely diagnosed due to slippage through routine newborn screening, wide symptom variety, and, in some cases, symptoms only appearing in adulthood. Pathogenic mutations of the ACSF3 gene lead to a defect of the mitochondrial enzyme acyl-CoA synthetase family member 3 (ACSF3), resulting in accumulation of methylmalonic acid and malonic acid. The enzyme's dual role is the conversion of methylmalonic acid into methylmalonyl-CoA and of malonic acid into malonyl-CoA, the latter being required for mitochondrial fatty acid synthesis (mtFAS) and mitochondrial protein malonylation. CMAMMA can therefore be defined not only as an organic acidemia but also as a defect of mitochondrial fatty acid synthesis and of protein malonylation.
Methylmalonyl-CoA epimerase Mutations in the MCEE gene, which encodes the methylmalonyl-CoA epimerase protein, also referred to as methylmalonyl racemase, will cause a much milder form of the disorder than the related methylmalonyl-CoA mutase variant. Like the mutase, the epimerase also functions in breaking down the same substances, but to a significantly lesser extent than the mutase does. The phenotypic differences caused by a deficiency of the epimerase as opposed to the mutase are so mild that there is debate within the medical community as to whether or not this genetic deficiency can be considered a disorder or clinical syndrome.
Adenosylcobalamin Also known as vitamin B12, this form of cobalamin is a required cofactor of methylmalonyl-CoA mutase. Even with a functional version of the enzyme at physiologically normal levels, if B12 cannot be converted to this active form (due to defects in the Adenosylcobalamin synthesis system or cobalamin transporters), the mutase will be unable to function.
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