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Structural features of cytochrome P450 1A associated with the absence of EROD activity in liver of the loricariid catfish Pterygoplichthys sp

The Amazon catfish genus Pterygoplichthys (Loricariidae, Siluriformes) is closely related to the loricariid genus Hypostomus, in which at least two species lack detectable ethoxyresorufin-O-deethylase (EROD) activity, typically catalyzed by cytochrome P450 1 (CYP1) enzymes. Pterygoplichthys sp. live...

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Published in:Gene 2011-12, Vol.489 (2), p.111-118
Main Authors: Parente, Thiago E.M., Rebelo, Mauro F., da-Silva, Manuela L., Woodin, Bruce R., Goldstone, Jared V., Bisch, Paulo M., Paumgartten, Francisco J.R., Stegeman, John J.
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creator Parente, Thiago E.M.
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Stegeman, John J.
description The Amazon catfish genus Pterygoplichthys (Loricariidae, Siluriformes) is closely related to the loricariid genus Hypostomus, in which at least two species lack detectable ethoxyresorufin-O-deethylase (EROD) activity, typically catalyzed by cytochrome P450 1 (CYP1) enzymes. Pterygoplichthys sp. liver microsomes also lacked EROD, as well as activity with other substituted resorufins, but aryl hydrocarbon receptor agonists induced hepatic CYP1A mRNA and protein suggesting structural/functional differences in Pterygoplichthys CYP1s from those in other vertebrates. Comparing the sequences of CYP1As of Pterygoplichthys sp. and of two phylogenetically related siluriform species that do catalyze EROD (Ancistrus sp., Loricariidae and Corydoras sp., Callichthyidae) showed that these three proteins share amino acids at 17 positions that are not shared by any fish in a set of 24 other species. Pterygoplichthys and Ancistrus (the loricariids) have an additional 22 amino acid substitutions in common that are not shared by Corydoras or by other fish species. Pterygoplichthys has six exclusive amino acid substitutions. Molecular docking and dynamics simulations indicate that Pterygoplichthys CYP1A has a weak affinity for ER, which binds infrequently in a productive orientation, and in a less stable conformation than in CYP1As of species that catalyze EROD. ER also binds with the carbonyl moiety proximal to the heme iron. Pterygoplichthys CYP1A has amino acid substitutions that reduce the frequency of correctly oriented ER in the AS preventing the detection of EROD activity. The results indicate that loricariid CYP1As may have a peculiar substrate selectivity that differs from CYP1As of most vertebrate. [Display omitted] ► EROD was not detected in Pterygoplichthys liver microsomes ► CYP1A protein and mRNA were induced by treatments with AhR agonists. ► CYP1A coding region exhibits six exclusive amino acids substitutions. ► EROD substrate docked infrequently and in an unusual position at the active site.
doi_str_mv 10.1016/j.gene.2011.07.023
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Pterygoplichthys sp. liver microsomes also lacked EROD, as well as activity with other substituted resorufins, but aryl hydrocarbon receptor agonists induced hepatic CYP1A mRNA and protein suggesting structural/functional differences in Pterygoplichthys CYP1s from those in other vertebrates. Comparing the sequences of CYP1As of Pterygoplichthys sp. and of two phylogenetically related siluriform species that do catalyze EROD (Ancistrus sp., Loricariidae and Corydoras sp., Callichthyidae) showed that these three proteins share amino acids at 17 positions that are not shared by any fish in a set of 24 other species. Pterygoplichthys and Ancistrus (the loricariids) have an additional 22 amino acid substitutions in common that are not shared by Corydoras or by other fish species. Pterygoplichthys has six exclusive amino acid substitutions. Molecular docking and dynamics simulations indicate that Pterygoplichthys CYP1A has a weak affinity for ER, which binds infrequently in a productive orientation, and in a less stable conformation than in CYP1As of species that catalyze EROD. ER also binds with the carbonyl moiety proximal to the heme iron. Pterygoplichthys CYP1A has amino acid substitutions that reduce the frequency of correctly oriented ER in the AS preventing the detection of EROD activity. The results indicate that loricariid CYP1As may have a peculiar substrate selectivity that differs from CYP1As of most vertebrate. [Display omitted] ► EROD was not detected in Pterygoplichthys liver microsomes ► CYP1A protein and mRNA were induced by treatments with AhR agonists. ► CYP1A coding region exhibits six exclusive amino acids substitutions. ► EROD substrate docked infrequently and in an unusual position at the active site.</description><identifier>ISSN: 0378-1119</identifier><identifier>EISSN: 1879-0038</identifier><identifier>DOI: 10.1016/j.gene.2011.07.023</identifier><identifier>PMID: 21840383</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>agonists ; Amino acid ; Amino Acid Substitution ; amino acids ; Ancistrus ; Animals ; Base Sequence ; beta-Naphthoflavone - pharmacology ; Biotransformation ; Callichthyidae ; catfish ; Catfishes - metabolism ; Corydoras ; CYP1A ; cytochrome P-450 ; Cytochrome P-450 CYP1A1 - chemistry ; Cytochrome P-450 CYP1A1 - genetics ; Cytochrome P-450 CYP1A1 - metabolism ; Enzyme Induction ; enzymes ; Ethoxiresorufin ; Fish Proteins - chemistry ; Fish Proteins - genetics ; Fish Proteins - metabolism ; heme iron ; Hypostomus ; liver ; Liver - enzymology ; Liver - metabolism ; liver microsomes ; Loricariidae ; messenger RNA ; Microsomes, Liver - enzymology ; Microsomes, Liver - metabolism ; Oxazines - pharmacology ; phylogeny ; Polychlorinated Biphenyls - pharmacology ; Pterygoplichthys ; Receptors, Aryl Hydrocarbon - agonists ; Receptors, Aryl Hydrocarbon - metabolism ; RNA, Messenger - biosynthesis ; RNA, Messenger - genetics ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Analysis, Protein ; Siluriformes ; Substrate Specificity</subject><ispartof>Gene, 2011-12, Vol.489 (2), p.111-118</ispartof><rights>2011 Elsevier B.V.</rights><rights>Copyright © 2011 Elsevier B.V. All rights reserved.</rights><rights>2011 Elsevier B.V. All rights reserved. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c510t-8f082b3ac6d0afad84f63c915e1f82925ec6b130f4abfacfcdc2ab050f86ff3a3</citedby><cites>FETCH-LOGICAL-c510t-8f082b3ac6d0afad84f63c915e1f82925ec6b130f4abfacfcdc2ab050f86ff3a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21840383$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Parente, Thiago E.M.</creatorcontrib><creatorcontrib>Rebelo, Mauro F.</creatorcontrib><creatorcontrib>da-Silva, Manuela L.</creatorcontrib><creatorcontrib>Woodin, Bruce R.</creatorcontrib><creatorcontrib>Goldstone, Jared V.</creatorcontrib><creatorcontrib>Bisch, Paulo M.</creatorcontrib><creatorcontrib>Paumgartten, Francisco J.R.</creatorcontrib><creatorcontrib>Stegeman, John J.</creatorcontrib><title>Structural features of cytochrome P450 1A associated with the absence of EROD activity in liver of the loricariid catfish Pterygoplichthys sp</title><title>Gene</title><addtitle>Gene</addtitle><description>The Amazon catfish genus Pterygoplichthys (Loricariidae, Siluriformes) is closely related to the loricariid genus Hypostomus, in which at least two species lack detectable ethoxyresorufin-O-deethylase (EROD) activity, typically catalyzed by cytochrome P450 1 (CYP1) enzymes. Pterygoplichthys sp. liver microsomes also lacked EROD, as well as activity with other substituted resorufins, but aryl hydrocarbon receptor agonists induced hepatic CYP1A mRNA and protein suggesting structural/functional differences in Pterygoplichthys CYP1s from those in other vertebrates. Comparing the sequences of CYP1As of Pterygoplichthys sp. and of two phylogenetically related siluriform species that do catalyze EROD (Ancistrus sp., Loricariidae and Corydoras sp., Callichthyidae) showed that these three proteins share amino acids at 17 positions that are not shared by any fish in a set of 24 other species. Pterygoplichthys and Ancistrus (the loricariids) have an additional 22 amino acid substitutions in common that are not shared by Corydoras or by other fish species. Pterygoplichthys has six exclusive amino acid substitutions. 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Pterygoplichthys sp. liver microsomes also lacked EROD, as well as activity with other substituted resorufins, but aryl hydrocarbon receptor agonists induced hepatic CYP1A mRNA and protein suggesting structural/functional differences in Pterygoplichthys CYP1s from those in other vertebrates. Comparing the sequences of CYP1As of Pterygoplichthys sp. and of two phylogenetically related siluriform species that do catalyze EROD (Ancistrus sp., Loricariidae and Corydoras sp., Callichthyidae) showed that these three proteins share amino acids at 17 positions that are not shared by any fish in a set of 24 other species. Pterygoplichthys and Ancistrus (the loricariids) have an additional 22 amino acid substitutions in common that are not shared by Corydoras or by other fish species. Pterygoplichthys has six exclusive amino acid substitutions. Molecular docking and dynamics simulations indicate that Pterygoplichthys CYP1A has a weak affinity for ER, which binds infrequently in a productive orientation, and in a less stable conformation than in CYP1As of species that catalyze EROD. ER also binds with the carbonyl moiety proximal to the heme iron. Pterygoplichthys CYP1A has amino acid substitutions that reduce the frequency of correctly oriented ER in the AS preventing the detection of EROD activity. The results indicate that loricariid CYP1As may have a peculiar substrate selectivity that differs from CYP1As of most vertebrate. [Display omitted] ► EROD was not detected in Pterygoplichthys liver microsomes ► CYP1A protein and mRNA were induced by treatments with AhR agonists. ► CYP1A coding region exhibits six exclusive amino acids substitutions. ► EROD substrate docked infrequently and in an unusual position at the active site.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>21840383</pmid><doi>10.1016/j.gene.2011.07.023</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
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identifier ISSN: 0378-1119
ispartof Gene, 2011-12, Vol.489 (2), p.111-118
issn 0378-1119
1879-0038
language eng
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source ScienceDirect Freedom Collection 2022-2024
subjects agonists
Amino acid
Amino Acid Substitution
amino acids
Ancistrus
Animals
Base Sequence
beta-Naphthoflavone - pharmacology
Biotransformation
Callichthyidae
catfish
Catfishes - metabolism
Corydoras
CYP1A
cytochrome P-450
Cytochrome P-450 CYP1A1 - chemistry
Cytochrome P-450 CYP1A1 - genetics
Cytochrome P-450 CYP1A1 - metabolism
Enzyme Induction
enzymes
Ethoxiresorufin
Fish Proteins - chemistry
Fish Proteins - genetics
Fish Proteins - metabolism
heme iron
Hypostomus
liver
Liver - enzymology
Liver - metabolism
liver microsomes
Loricariidae
messenger RNA
Microsomes, Liver - enzymology
Microsomes, Liver - metabolism
Oxazines - pharmacology
phylogeny
Polychlorinated Biphenyls - pharmacology
Pterygoplichthys
Receptors, Aryl Hydrocarbon - agonists
Receptors, Aryl Hydrocarbon - metabolism
RNA, Messenger - biosynthesis
RNA, Messenger - genetics
Sequence Alignment
Sequence Analysis, DNA
Sequence Analysis, Protein
Siluriformes
Substrate Specificity
title Structural features of cytochrome P450 1A associated with the absence of EROD activity in liver of the loricariid catfish Pterygoplichthys sp
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