branched chain keto acid dehydrogenase E1, beta polypeptide


BCKDHB (may also be known as: None)




Branched-chain keto acid dehydrogenase is a multienzyme complex associated with the inner membrane of mitochondria, and functions in the catabolism of branched-chain amino acids. The complex consists of multiple copies of 3 components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). This gene encodes the E1 beta subunit, and mutations therein have been associated with maple syrup urine disease (MSUD), type 1B, a disease characterized by a maple syrup odor to the urine in addition to mental and physical retardation, and feeding problems. Alternative splicing at this locus results in transcript variants with different 3' non-coding regions, but encoding the same isoform. [provided by RefSeq, Jul 2008]


tag-173 Caenorhabditis elegans
CG17691 Drosophila melanogaster
bckdhb Danio rerio
Bckdhb Mus musculus
Bckdhb Rattus norvegicus

Links to external resources

Changes associated with this gene

GO Terms

GO IDGO TermGO Category
GO:0007584 response to nutrient biological_process
GO:0009083 branched chain family amino acid catabolic process biological_process
GO:0034641 cellular nitrogen compound metabolic process biological_process
GO:0044281 small molecule metabolic process biological_process
GO:0051384 response to glucocorticoid stimulus biological_process
GO:0051591 response to cAMP biological_process
GO:0005739 mitochondrion cellular_component
GO:0005759 mitochondrial matrix cellular_component
GO:0005947 mitochondrial alpha-ketoglutarate dehydrogenase complex cellular_component
GO:0003824 catalytic activity molecular_function
GO:0003826 alpha-ketoacid dehydrogenase activity molecular_function
GO:0003863 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity molecular_function
GO:0005515 protein binding molecular_function
GO:0016831 carboxy-lyase activity molecular_function
GO:0032403 protein complex binding molecular_function