BCHE
Function
Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.
Involvement in disease
Butyrylcholinesterase deficiency
BCHED
An autosomal recessive metabolic condition characterized by increased sensitivity to certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium. BCHED results in slower hydrolysis of these drugs and, consequently, a prolonged neuromuscular block, leading to apnea. The duration of the prolonged apnea varies significantly depending on the extent of the enzyme deficiency.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
N-glycosylated. No other PTM detected (PubMed:20946535). The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid molecules (Neu5Ac) making up approximately 33% and 47% of the total N-glycans, respectively. Only low amounts of fucosylated diantennary N-glycans are detected (approximately 2%). Triantennary N-glycans with or without fucose amount to approximately 13%, whereas 5% of the total N-glycans are of the oligomannosidic or hybrid type.
Sequence Similarities
Belongs to the type-B carboxylesterase/lipase family.
Tissue Specificity
Detected in blood plasma (at protein level). Present in most cells except erythrocytes.
Cellular localization
- Secreted
Alternative names
CHE1, BCHE, Cholinesterase, Acylcholine acylhydrolase, Butyrylcholine esterase, Choline esterase II, Pseudocholinesterase
Database links
swissprot:P06276 omim:177400 entrezGene:590
Other research areas
- Cardiovascular