Cu2+-dependent hydrolysis of O-hexyl 2,5-dichlorophenyl phosphoramidate by reptile sera
Copyright © 2023. Published by Elsevier B.V..
This study shows the EDTA-resistant, Ca2+ and Cu2+-dependent hydrolysis of O-hexyl 2,5-dichlorophenyl phosphoramidate (HDCP) compound in reptiles sera determined by spectrophotometry UV/Vis and chiral chromatography. Samples of ten reptile species were incubated with aliquot of 100 or 400 μM HDCP in presence of 100 or 300 μM Cu2+, or 2.5 mM Ca2+ or 5 mM EDTA at 37 °C for 30-60 min. The results shown an activator effect of Cu2+ on HDCP hydrolysis in freshwater turtles sera (Trachemys scripta, Chelydra serpentina and Macrochelys temminckii) because the levels of 2,5-dichlorophenol (DCP; product hydrolysis) were similar (∼37 μM DCP) to chicken serum (positive control group). The marine turtles (Chelonia mydas and Eretmochelys imbricata) and crocodiles (Crocodylusacutus and Crocodylus moreletii) showed ∼50% less HDCPase activity (13-17 μM DCP) compared to the HDCPase activity of the freshwater turtle species. Terrestrial reptile species (snakes and lizards) showed around 25% of activity (7-13 μM DCP) with both copper concentrations. These Cu2+-dependent hydrolysis were stereospecific to R(+)-HDCP (p˂0.05) in the three freshwater turtle species that showed similar hydrolysis to the chicken serum. However, the Ca2+ did not show a significant activating effect on the HDCPase activity (1-8 μM DCP) in any reptile serum. Their hydrolysis levels were very similar to those of EDTA-resistant activity. The present study demonstrates a Cu2+-dependent A-esterase (HDCPase) activity in turtles and points serum albumin as the cuproprotein responsible for this activity, reinforcing its N-terminal sequence (DAEH) as a catalytic center.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:382 |
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| Enthalten in: |
Chemico-biological interactions - 382(2023) vom: 01. Sept., Seite 110637 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ramírez-González, Laura [VerfasserIn] |
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| Links: |
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| Themen: |
789U1901C5 |
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| Anmerkungen: |
Date Completed 18.08.2023 Date Revised 18.08.2023 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.cbi.2023.110637 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM359685749 |
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| 245 | 1 | 0 | |a Cu2+-dependent hydrolysis of O-hexyl 2,5-dichlorophenyl phosphoramidate by reptile sera |
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| 520 | |a Copyright © 2023. Published by Elsevier B.V. | ||
| 520 | |a This study shows the EDTA-resistant, Ca2+ and Cu2+-dependent hydrolysis of O-hexyl 2,5-dichlorophenyl phosphoramidate (HDCP) compound in reptiles sera determined by spectrophotometry UV/Vis and chiral chromatography. Samples of ten reptile species were incubated with aliquot of 100 or 400 μM HDCP in presence of 100 or 300 μM Cu2+, or 2.5 mM Ca2+ or 5 mM EDTA at 37 °C for 30-60 min. The results shown an activator effect of Cu2+ on HDCP hydrolysis in freshwater turtles sera (Trachemys scripta, Chelydra serpentina and Macrochelys temminckii) because the levels of 2,5-dichlorophenol (DCP; product hydrolysis) were similar (∼37 μM DCP) to chicken serum (positive control group). The marine turtles (Chelonia mydas and Eretmochelys imbricata) and crocodiles (Crocodylusacutus and Crocodylus moreletii) showed ∼50% less HDCPase activity (13-17 μM DCP) compared to the HDCPase activity of the freshwater turtle species. Terrestrial reptile species (snakes and lizards) showed around 25% of activity (7-13 μM DCP) with both copper concentrations. These Cu2+-dependent hydrolysis were stereospecific to R(+)-HDCP (p˂0.05) in the three freshwater turtle species that showed similar hydrolysis to the chicken serum. However, the Ca2+ did not show a significant activating effect on the HDCPase activity (1-8 μM DCP) in any reptile serum. Their hydrolysis levels were very similar to those of EDTA-resistant activity. The present study demonstrates a Cu2+-dependent A-esterase (HDCPase) activity in turtles and points serum albumin as the cuproprotein responsible for this activity, reinforcing its N-terminal sequence (DAEH) as a catalytic center | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a A-esterase | |
| 650 | 4 | |a Copper | |
| 650 | 4 | |a Hydrolysis | |
| 650 | 4 | |a Organophosphorus | |
| 650 | 4 | |a Reptiles | |
| 650 | 4 | |a Stereoselectivity | |
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| 650 | 7 | |a phosphoramidic acid |2 NLM | |
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| 650 | 7 | |a Organophosphorus Compounds |2 NLM | |
| 650 | 7 | |a Edetic Acid |2 NLM | |
| 650 | 7 | |a 9G34HU7RV0 |2 NLM | |
| 700 | 1 | |a Undiano, Elizabeth |e verfasserin |4 aut | |
| 700 | 1 | |a Flores-Pérez, Iván |e verfasserin |4 aut | |
| 700 | 1 | |a Carrillo-D'Lacoste, Luis |e verfasserin |4 aut | |
| 700 | 1 | |a Salmerón, Mónica |e verfasserin |4 aut | |
| 700 | 1 | |a Verastegui, Alejandra |e verfasserin |4 aut | |
| 700 | 1 | |a Lara, Gabriela |e verfasserin |4 aut | |
| 700 | 1 | |a Monroy-Noyola, Antonio |e verfasserin |4 aut | |
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