BCHE Rabbit Polyclonal Antibody

Function

Present in most cells except erythrocytes, butyrylcholine esterase (BChE), also designated acylcholine acylhydrolase or pseudocholinesterase, has esterase activity as well as aryl acylamidase activity. It hydrolyzes acylcholine into choline and carboxylate. BChE is synthesized in the liver and is highly reactive with organophosphate esters. BChE can form a homotetramer composed of two dimers linked by a disulfide bond. Defects in the gene encoding BChE are associated with the disease hypocholinesterasemia. Inhibition of BChE effects the toxicity of organophosphates in the respiratory system suggesting that BChE may play a role in respiratory function. In addition, BChE may play an important pharmocological role by hydrolyzing toxic esters. This suggests an involvement of BChE in a treatment for intoxication with substances such as cocaine.

Background References

1. Chilukuri N et al. Adenovirus-transduced human butyrylcholinesterase in mouse blood functions as a bioscavenger of chemical warfare nerve agents. Mol Pharmacol 76:612-617 (2009).

2. Amitay M et al. The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger. Proteins 77:370-377 (2009).

Sequence Similarity

Belongs to the type-B carboxylesterase/lipase family.

Tissue Specificity

Detected in blood plasma (at protein level). Present in most cells except erythrocytes.

Post-translational Modification

N-glycosylated. No other PTM detected. 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.

Subcellular Location

Secreted.

UNIPROT

SwissProt: P06276 Human

Synonyms