Branched chain amino acid transaminase 1

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Branched chain amino acid transaminase 1 (BCAT1) is an enzyme that in humans is encoded by the BCAT1 gene. This enzyme is part of the amino acid metabolism process, specifically the branched-chain amino acid (BCAA) catabolic pathway.

Function[edit | edit source]

BCAT1 is a cytosolic enzyme and is primarily expressed in the liver, kidney, and brain. It catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. The catabolism of these amino acids is critical for the maintenance of nitrogen balance within the body.

Structure[edit | edit source]

The BCAT1 enzyme is a dimer composed of two identical subunits. Each subunit is composed of about 365 amino acid residues. The enzyme contains a pyridoxal phosphate (PLP) binding site, which is essential for its catalytic activity.

Clinical significance[edit | edit source]

Alterations in the expression of the BCAT1 gene have been associated with various diseases. Overexpression of BCAT1 has been observed in several types of cancer, including glioblastoma, ovarian cancer, and breast cancer. In these cases, the increased BCAT1 activity contributes to the survival and proliferation of cancer cells.

See also[edit | edit source]

References[edit | edit source]




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Contributors: Prab R. Tumpati, MD