Cysteine conjugate beta-lyase activity in three species of parasitic helminth.
Living organisms employ a variety of metabolic pathways when detoxifying xenobiotic compounds, including the formation of cysteine S-conjugates via glutathione conjugation. However, cysteine conjugate beta-lyase (CCBL) catalysed beta-cleavage, of certain cysteine conjugates, is known to cause cytotoxicity. This study represents the first investigation into the expression of CCBL and other associated enzymes in helminth species. A survey of the three major groups of parasitic helminths [cestodes (Moniezia expansa), digeneans (Fasciola hepatica) and nematodes (Necator americanus, Heligmosomoides polygyrus)] has been made. The presence of CCBL enzymes within Moniezia expansa, Necator americanus and Heligmosomoides polygyrus has been established. Each species was screened for gamma-glutamyl transpeptidase activity and transaminase activity towards L-aspartate, L-alanine, L-albizziin and L-phenylalanine. Aspartate and alanine aminotransferase activity were detected in all four species tested. Gamma-glutamyl transpeptidase activity was only detected in Moniezia expansa and Necator americanus.
Adcock
H J
HJ
Department of Chemistry, De Montfort University, The Gateway, Leicester, UK.
Brophy
P M
PM
Teesdale-Spittle
P H
PH
Buckberry
L D
LD
D000409:Alanine / Q000378:metabolism; D000818:Animals; D001224:Aspartic Acid / Q000378:metabolism; D013437:Carbon-Sulfur Lyases / Q000378:metabolism*; D002589:Cestoda / Q000201:enzymology; D005210:Fasciola hepatica / Q000201:enzymology; D015801:Helminth Proteins / Q000378:metabolism*; D009348:Nematoda / Q000201:enzymology; D013045:Species Specificity; D000637:Transaminases / Q000378:metabolism; D005723:gamma-Glutamyltransferase / Q000378:metabolism
D015801:Helminth Proteins; D001224:Aspartic Acid; D005723:gamma-Glutamyltransferase; D000637:Transaminases; D013437:Carbon-Sulfur Lyases; C019969:S-alkylcysteine lyase; D000409:Alanine