Carotenoid cleavage enzymes evolved convergently to generate the visual chromophore

The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11- cis -retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-c...

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Published inNature chemical biology Vol. 20; no. 6; pp. 779 - 788
Main Authors Solano, Yasmeen J., Everett, Michael P., Dang, Kelly S., Abueg, Jude, Kiser, Philip D.
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.06.2024
Nature Publishing Group
Subjects
631/45/49/1141
631/535/1266
631/92/173
Animals
Binding
Biochemical Engineering
Biochemistry
Biochemistry & Molecular Biology
Bioorganic Chemistry
Carotene
Carotenoids
Carotenoids - chemistry
Carotenoids - metabolism
Catalytic Domain
Cell Biology
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Chromophores
cis-trans-Isomerases - chemistry
cis-trans-Isomerases - genetics
cis-trans-Isomerases - metabolism
Cleavage
Dioxygenases - chemistry
Dioxygenases - genetics
Dioxygenases - metabolism
Enzymes
Epithelium
Evolution
Evolution, Molecular
Humans
Inactivation
Insects
Isomerization
Models, Molecular
Mutagenesis
Oxygenation
Retina
Retinal pigment epithelium
Retinaldehyde
Retinaldehyde - chemistry
Retinaldehyde - metabolism
Substrates
Vertebrates
Visual system
β-Carotene
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Abstract The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11- cis -retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-carotene oxygenase 1 and retinal pigment epithelium 65 (RPE65), to form 11- cis -retinaldehyde from carotenoid substrates, whereas invertebrates such as insects use a single enzyme known as Neither Inactivation Nor Afterpotential B (NinaB). RPE65 and NinaB couple trans–cis isomerization with hydrolysis and oxygenation, respectively, but the mechanistic relationship of their isomerase activities remains unknown. Here we report the structure of NinaB, revealing details of its active site architecture and mode of membrane binding. Structure-guided mutagenesis studies identify a residue cluster deep within the NinaB substrate-binding cleft that controls its isomerization activity. Our data demonstrate that isomerization activity is mediated by distinct active site regions in NinaB and RPE65—an evolutionary convergence that deepens our understanding of visual system diversity. NinaB is an isomerooxygenase that generates visual chromophore (11- cis -retinal) from carotenoid substrates. Here Solano et al. reveal the structural basis for NinaB isomerase activity, providing new insights into the evolution of visual chromophore synthesis by carotenoid cleavage enzymes.
AbstractList The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11-cis-retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-carotene oxygenase 1 and retinal pigment epithelium 65 (RPE65), to form 11-cis-retinaldehyde from carotenoid substrates, whereas invertebrates such as insects use a single enzyme known as Neither Inactivation Nor Afterpotential B (NinaB). RPE65 and NinaB couple trans-cis isomerization with hydrolysis and oxygenation, respectively, but the mechanistic relationship of their isomerase activities remains unknown. Here we report the structure of NinaB, revealing details of its active site architecture and mode of membrane binding. Structure-guided mutagenesis studies identify a residue cluster deep within the NinaB substrate-binding cleft that controls its isomerization activity. Our data demonstrate that isomerization activity is mediated by distinct active site regions in NinaB and RPE65-an evolutionary convergence that deepens our understanding of visual system diversity.
Abstract The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11- cis -retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-carotene oxygenase 1 and retinal pigment epithelium 65 (RPE65), to form 11- cis -retinaldehyde from carotenoid substrates, whereas invertebrates such as insects use a single enzyme known as Neither Inactivation Nor Afterpotential B (NinaB). RPE65 and NinaB couple trans–cis isomerization with hydrolysis and oxygenation, respectively, but the mechanistic relationship of their isomerase activities remains unknown. Here we report the structure of NinaB, revealing details of its active site architecture and mode of membrane binding. Structure-guided mutagenesis studies identify a residue cluster deep within the NinaB substrate-binding cleft that controls its isomerization activity. Our data demonstrate that isomerization activity is mediated by distinct active site regions in NinaB and RPE65—an evolutionary convergence that deepens our understanding of visual system diversity.
The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11- cis -retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-carotene oxygenase 1 and retinal pigment epithelium 65 (RPE65), to form 11- cis -retinaldehyde from carotenoid substrates, whereas invertebrates such as insects use a single enzyme known as Neither Inactivation Nor Afterpotential B (NinaB). RPE65 and NinaB couple trans–cis isomerization with hydrolysis and oxygenation, respectively, but the mechanistic relationship of their isomerase activities remains unknown. Here we report the structure of NinaB, revealing details of its active site architecture and mode of membrane binding. Structure-guided mutagenesis studies identify a residue cluster deep within the NinaB substrate-binding cleft that controls its isomerization activity. Our data demonstrate that isomerization activity is mediated by distinct active site regions in NinaB and RPE65—an evolutionary convergence that deepens our understanding of visual system diversity. NinaB is an isomerooxygenase that generates visual chromophore (11- cis -retinal) from carotenoid substrates. Here Solano et al. reveal the structural basis for NinaB isomerase activity, providing new insights into the evolution of visual chromophore synthesis by carotenoid cleavage enzymes.
The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11-cis-retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-carotene oxygenase 1 and retinal pigment epithelium 65 (RPE65), to form 11-cis-retinaldehyde from carotenoid substrates, whereas invertebrates such as insects use a single enzyme known as Neither Inactivation Nor Afterpotential B (NinaB). RPE65 and NinaB couple trans-cis isomerization with hydrolysis and oxygenation, respectively, but the mechanistic relationship of their isomerase activities remains unknown. Here we report the structure of NinaB, revealing details of its active site architecture and mode of membrane binding. Structure-guided mutagenesis studies identify a residue cluster deep within the NinaB substrate-binding cleft that controls its isomerization activity. Our data demonstrate that isomerization activity is mediated by distinct active site regions in NinaB and RPE65-an evolutionary convergence that deepens our understanding of visual system diversity.The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11-cis-retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-carotene oxygenase 1 and retinal pigment epithelium 65 (RPE65), to form 11-cis-retinaldehyde from carotenoid substrates, whereas invertebrates such as insects use a single enzyme known as Neither Inactivation Nor Afterpotential B (NinaB). RPE65 and NinaB couple trans-cis isomerization with hydrolysis and oxygenation, respectively, but the mechanistic relationship of their isomerase activities remains unknown. Here we report the structure of NinaB, revealing details of its active site architecture and mode of membrane binding. Structure-guided mutagenesis studies identify a residue cluster deep within the NinaB substrate-binding cleft that controls its isomerization activity. Our data demonstrate that isomerization activity is mediated by distinct active site regions in NinaB and RPE65-an evolutionary convergence that deepens our understanding of visual system diversity.
The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11-cis-retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-carotene oxygenase 1 and retinal pigment epithelium 65 (RPE65), to form 11-cis-retinaldehyde from carotenoid substrates, whereas invertebrates such as insects use a single enzyme known as Neither Inactivation Nor Afterpotential B (NinaB). RPE65 and NinaB couple trans–cis isomerization with hydrolysis and oxygenation, respectively, but the mechanistic relationship of their isomerase activities remains unknown. Here we report the structure of NinaB, revealing details of its active site architecture and mode of membrane binding. Structure-guided mutagenesis studies identify a residue cluster deep within the NinaB substrate-binding cleft that controls its isomerization activity. Our data demonstrate that isomerization activity is mediated by distinct active site regions in NinaB and RPE65—an evolutionary convergence that deepens our understanding of visual system diversity.NinaB is an isomerooxygenase that generates visual chromophore (11-cis-retinal) from carotenoid substrates. Here Solano et al. reveal the structural basis for NinaB isomerase activity, providing new insights into the evolution of visual chromophore synthesis by carotenoid cleavage enzymes.
Abstract The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11-cis-retinaldehyde chromophore. This visual chromophore is enzymatically produced through the action of carotenoid cleavage dioxygenases. Vertebrates require two carotenoid cleavage dioxygenases, β-carotene oxygenase 1 and retinal pigment epithelium 65 (RPE65), to form 11-cis-retinaldehyde from carotenoid substrates, whereas invertebrates such as insects use a single enzyme known as Neither Inactivation Nor Afterpotential B (NinaB). RPE65 and NinaB coupletrans–cisisomerization with hydrolysis and oxygenation, respectively, but the mechanistic relationship of their isomerase activities remains unknown. Here we report the structure of NinaB, revealing details of its active site architecture and mode of membrane binding. Structure-guided mutagenesis studies identify a residue cluster deep within the NinaB substrate-binding cleft that controls its isomerization activity. Our data demonstrate that isomerization activity is mediated by distinct active site regions in NinaB and RPE65—an evolutionary convergence that deepens our understanding of visual system diversity.
Author Dang, Kelly S.
Solano, Yasmeen J.
Kiser, Philip D.
Everett, Michael P.
Abueg, Jude
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  doi: 10.1021/acs.biochem.7b00251
  contributor:
    fullname: X Sui
– volume: 31
  start-page: 455
  year: 2010
  ident: 1554_CR77
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.21334
  contributor:
    fullname: O Trott
– volume: 66
  start-page: 486
  year: 2010
  ident: 1554_CR72
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444910007493
  contributor:
    fullname: P Emsley
SSID ssj0036618
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Snippet The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11- cis -retinaldehyde chromophore. This visual chromophore is...
The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11-cis-retinaldehyde chromophore. This visual chromophore is...
Abstract The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11- cis -retinaldehyde chromophore. This visual...
Abstract The retinal light response in animals originates from the photoisomerization of an opsin-coupled 11-cis-retinaldehyde chromophore. This visual...
SourceID pubmedcentral
osti
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pubmed
springer
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 779
SubjectTerms 631/45/49/1141
631/535/1266
631/92/173
Animals
Binding
Biochemical Engineering
Biochemistry
Biochemistry & Molecular Biology
Bioorganic Chemistry
Carotene
Carotenoids
Carotenoids - chemistry
Carotenoids - metabolism
Catalytic Domain
Cell Biology
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Chromophores
cis-trans-Isomerases - chemistry
cis-trans-Isomerases - genetics
cis-trans-Isomerases - metabolism
Cleavage
Dioxygenases - chemistry
Dioxygenases - genetics
Dioxygenases - metabolism
Enzymes
Epithelium
Evolution
Evolution, Molecular
Humans
Inactivation
Insects
Isomerization
Models, Molecular
Mutagenesis
Oxygenation
Retina
Retinal pigment epithelium
Retinaldehyde
Retinaldehyde - chemistry
Retinaldehyde - metabolism
Substrates
Vertebrates
Visual system
β-Carotene
Title Carotenoid cleavage enzymes evolved convergently to generate the visual chromophore
URI https://link.springer.com/article/10.1038/s41589-024-01554-z
https://www.ncbi.nlm.nih.gov/pubmed/38355721
https://www.proquest.com/docview/3062788646
https://www.proquest.com/docview/2927212359
https://www.osti.gov/biblio/2469552
https://pubmed.ncbi.nlm.nih.gov/PMC11142922
Volume 20
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