Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases

Abstract

The complete amino acid sequence of a mammalian acetylcholinesterase from fetal bovine serum (FBS ACHE) is presented. This enzyme has a high degree of sequence identity with other cholinesterases, liver carboxyesterases, esterase-6, lysophospholipase, and thyroglobulin. The locations of 191 amino acids in 10 regions of the FBS enzyme were compared with corresponding sequences of Torpedo, human, and Drosophila AChEs and human serum butyrylcholinesterase (BChE). In one region there is a marked difference in both the number of amino acids and their sequence between mammalian AChE and other AChEs and the human serum BChE. The amino acid sequence of FBS AChE showed overall homologies of 90% with human ACHE, 60% with T. californica ACHE, 50% with human serum BChE, and 39% with Drosophila AChE in these regions.

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

“…In glutactin, a 1,023-amino acid residue glycoprotein located in basement membranes of Drosophila, it is the N-terminal segment that is homologous to esterases. Although the sequence identity of these three nonhydrolytic proteins with other proteins in this Shimada et al, 1990Shimada et al, 1989Kawaguchi et al, 1989Longhi et al, 1992Schumacher et al, 1986Sikorav et al, 1987Rachinsky et al, 1990Doctor et al, 1990Soreq et al, 1990Hall and Spierer, 1986Hall and Malcolm, 1991Lockridge et al, 1987Rachinsky et al, 1990Jbilo and Chatonnet, 1990Robbi et al, 1990Munger et al, 1992Long et al, 1991Korza and Ozols, 1988Ozols, 1989Ovnic et al, 1991Long et al, 1988Takagi et al, 1988Oakeshott et al, 1987Collet et al, 1990Hanzlik et al, 1989Mouches et al, 1990Han et al, 1987Kissel et al, 1989 Hui andKissel, 1990;Nilsson et al, 1990;Baba et al, 1991Kyger et al, 1989Rubino et al, 1989Bomblies et al, 1990 de la Escalera et al ., 1990Olson et al, 1990Mercken et al, 1985 family is within 16-28%, there is no evolutionary pressure to maintain the geometry of the active site. One may, therefore, predict that their 3D structures will show more divergence from GCL and TcAChE than other proteins in this group.…”

The monoclonal antibody 2G8 is carbohydrate‐specific and distinguishes between different forms of vertebrate cholinesterases

“…From the primary structure of AChE from Torpedo californica [23] and Torpedo marmorata [24], it can be deduced that both asymmetric and globular forms of the enzyme contain four potential N-linked glycosylation sites. G4 AChE from fetal bovine serum contains five potential sites [28] while butyrylcholinesterase (BtChE) from human serum contains nine [25]. Within one species, composition and structure of oligosaccharide chains may vary between AChE from different tissues.…”

Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom.

“…1.7], one of the key proteins in chemical nerve impulse transmission at cholinergic synapses. The primary structure of AcChoEase from different organisms has been derived from cloned cDNAs (1,(13)(14)(15)(16)(17). Most investigations so far have focused on the enzyme from the electric organ of Torpedo.…”