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Structure of human serum cholinesterase
Author(s) -
Lockridge Oksana
Publication year - 1988
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950090406
Subject(s) - serine , glycoprotein , biochemistry , cholinesterase , acetylcholinesterase , proteases , protein subunit , esterase , disulfide bond , homology (biology) , cysteine , torpedo , sequence homology , chemistry , enzyme , biology , peptide sequence , gene , endocrinology , acetylcholine receptor , receptor
Human cholinesterase has recently been sequenced and cloned. It is a glycoprotein of 4 identical subunits, each subunit containing 9 carbohydrate chains and 3.5 disulfide bonds. Protein folding is likely to be very similar in human cholinesterase and Torpedo acetylcholinesterase. The cholinesterases have no significant sequence homology with the serine proteases and seem to belong to a separate serine esterase family.