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Propionyl-CoA carboxylase - A review
Parith Wongkittichote1, Nicholas Ah Mew2, Kimberly A Chapman2
1Children's National Health System, Division of Genetics and Metabolism, United States.
Molecular Genetics and Metabolism
|October 17, 2017
Summary
Propionyl-CoA carboxylase (PCC) enzyme dysfunction causes propionic acidemia, a serious inherited metabolic disorder. This review details PCC structure, function, and disease-associated human variants.
Area of Science:
- Biochemistry
- Genetics
- Metabolic Disorders
Background:
- Propionyl-CoA carboxylase (PCC) is crucial for metabolizing propionyl-CoA to methylmalonyl-CoA.
- PCC is encoded by PCCA and PCCB genes, forming a hetero-dodecameric enzyme.
- PCC dysfunction results in propionic acidemia, an inherited metabolic disorder with severe health consequences.
Purpose of the Study:
- To provide an overview of the current knowledge on PCC structure and function.
- To review updated human variants associated with PCC.
- To offer insights into the clinical aspects of propionic acidemia.
Main Methods:
- Literature review of published research on PCC.
- Compilation and analysis of human variants affecting PCCA and PCCB genes.
- Synthesis of information on the structure, function, and disease implications of PCC.
Main Results:
- Detailed description of PCC enzyme structure and catalytic function.
- An updated list of identified human variants in PCCA and PCCB genes.
- Summary of clinical manifestations and long-term complications of propionic acidemia.
Conclusions:
- PCC is essential for normal metabolism, and its variants lead to propionic acidemia.
- Understanding PCC variants aids in diagnosing and managing propionic acidemia.
- Further research into PCC structure-function relationships can inform therapeutic strategies.