2016
DOI: 10.3109/14756366.2016.1158170
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Purification and characterization of a Cys-Gly hydrolase from the gastropod mollusk,Patella caerulea

Abstract: A magnesium-dependent cysteinyl-glycine hydrolyzing enzyme from the gastropod mollusk Patella caerulea was purified to electrophoretic homogeneity through a simple and rapid purification protocol. The molecular masses of the native protein and the subunit suggest that the enzyme has a homohexameric structure. Structural data in combination with kinetic parameters determined with Cys-Gly and compared with Leu-Gly as a substrate, indicate that the purified enzyme is a member of the peptidase family M17. The find… Show more

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Cited by 2 publications
(3 citation statements)
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“…In this study, Family T3 peptidases (MEROPS database) found in the DG, SG and CG of P. canaliculata (Table S2), fulfill intracellular functions (excepting A0S2T7PH69) as all members have a threonine residue in their catalytic site and are self‐processing proteins with aminopeptidase and aminotransferase activities in their mature forms 30 . Although the physiological role of threonine peptidases of Family T3 eucaryotes is still under study, some reports suggest (a) associations with catalytic subunits of eukaryotic proteasomes where cellular protein turnover occurs, and (b) regulation of prooxidative state by preventing oxidative damage to macromolecules through the regulation of glutathione levels 76,77 …”
Section: Discussionmentioning
confidence: 89%
See 1 more Smart Citation
“…In this study, Family T3 peptidases (MEROPS database) found in the DG, SG and CG of P. canaliculata (Table S2), fulfill intracellular functions (excepting A0S2T7PH69) as all members have a threonine residue in their catalytic site and are self‐processing proteins with aminopeptidase and aminotransferase activities in their mature forms 30 . Although the physiological role of threonine peptidases of Family T3 eucaryotes is still under study, some reports suggest (a) associations with catalytic subunits of eukaryotic proteasomes where cellular protein turnover occurs, and (b) regulation of prooxidative state by preventing oxidative damage to macromolecules through the regulation of glutathione levels 76,77 …”
Section: Discussionmentioning
confidence: 89%
“…30 Although the physiological role of threonine peptidases of Family T3 eucaryotes is still under study, some reports suggest (a) associations with catalytic subunits of eukaryotic proteasomes where cellular protein turnover occurs, and (b) regulation of prooxidative state by preventing oxidative damage to macromolecules through the regulation of glutathione levels. 76,77 4.2 Diversity and origin of lipases Pomacea canaliculata consumes lipids such as fatty acids. Macrophytes can have ≤4% of fatty acids and triacylglycerols.…”
Section: Threonine Peptidasesmentioning
confidence: 99%
“…In the network (Figure ), glycine and glutamate were the node molecules. Glycine is the smallest of the 20 amino acids commonly found in proteins, but it is not essential to human diet, as it is biosynthesized in the body from the amino acid serine (Cappiello et al, ). In most organisms, the enzyme serine hydroxymethyltransferase catalyzes this transformation via the cafactor pyridoxal phosphate.…”
Section: Discussionmentioning
confidence: 99%