Enzymatic formation of apo-carotenoids from the xanthophyll carotenoids lutein, zeaxanthin and β-cryptoxanthin by ferret carotene-9′,10′-monooxygenase

[Display omitted] ▸ Vertebrate CMO2 enzymatically cleaves xanthophylls at the 9,10 and 9′,10′ double bond. ▸ Lutein and zeaxanthin are preferentially cleaved over β-cryptoxanthin. ▸ 3-OH-β-apo-10′-carotenal is oxidized to 3-OH-β-apo-10′-carotenoic acid. Xanthophyll carotenoids, such as lutein, zeaxa...

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Published in:	Archives of biochemistry and biophysics Vol. 506; no. 1; pp. 109 - 121
Main Authors:	Mein, Jonathan R., Dolnikowski, Gregory G., Ernst, Hansgeorg, Russell, Robert M., Wang, Xiang-Dong
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 01.02.2011
Subjects:	Animals Apo-carotenoid beta-cryptoxanthin beta-ionone Carotenoids - biosynthesis Carotenoids - chemistry Cell Line Chromatography, High Pressure Liquid CMO1 CMO2 Cryptoxanthins enzyme kinetics Fatty Acid Desaturases - genetics Fatty Acid Desaturases - metabolism ferrets Ferrets - genetics Ferrets - metabolism Gas Chromatography-Mass Spectrometry high performance liquid chromatography in vitro studies In Vitro Techniques Kinetics Liver - metabolism lutein Lutein - metabolism Metabolism Oxidation-Reduction Recombinant Proteins - genetics Recombinant Proteins - metabolism Spodoptera Substrate Specificity vitamin A Xanthophyll Xanthophylls - metabolism zeaxanthin Zeaxanthins CMO2 CMO1 Metabolism Xanthophyll Apo-carotenoid
ISSN:	0003-9861, 1096-0384, 1096-0384
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Abstract	[Display omitted] ▸ Vertebrate CMO2 enzymatically cleaves xanthophylls at the 9,10 and 9′,10′ double bond. ▸ Lutein and zeaxanthin are preferentially cleaved over β-cryptoxanthin. ▸ 3-OH-β-apo-10′-carotenal is oxidized to 3-OH-β-apo-10′-carotenoic acid. Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15′-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9′,10′-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC–MS and GC–MS, we identified both volatile and non-volatile apo-carotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10′-carotenal, 3-OH-β-apo-10′-carotenal, and β-apo-10′-carotenal, indicating cleavage at both the 9,10 and 9′,10′ carbon–carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10′-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD+, in vitro incubation of 3-OH-β-apo-10′-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10′-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function.
AbstractList	Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15′-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9′,10′-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC–MS and GC–MS, we identified both volatile and non-volatile apo-carotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10′-carotenal, 3-OH-β-apo-10′-carotenal, and β-apo-10′-carotenal, indicating cleavage at both the 9,10 and 9′,10′ carbon–carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10′-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD⁺, in vitro incubation of 3-OH-β-apo-10′-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10′-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function. [Display omitted] ▸ Vertebrate CMO2 enzymatically cleaves xanthophylls at the 9,10 and 9′,10′ double bond. ▸ Lutein and zeaxanthin are preferentially cleaved over β-cryptoxanthin. ▸ 3-OH-β-apo-10′-carotenal is oxidized to 3-OH-β-apo-10′-carotenoic acid. Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15′-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9′,10′-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC–MS and GC–MS, we identified both volatile and non-volatile apo-carotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10′-carotenal, 3-OH-β-apo-10′-carotenal, and β-apo-10′-carotenal, indicating cleavage at both the 9,10 and 9′,10′ carbon–carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10′-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD+, in vitro incubation of 3-OH-β-apo-10′-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10′-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function. Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15'-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9',10'-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC-MS and GC-MS, we identified both volatile and non-volatile apo-carotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10'-carotenal, 3-OH-β-apo-10'-carotenal, and β-apo-10'-carotenal, indicating cleavage at both the 9,10 and 9',10' carbon-carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10'-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD(+), in vitro incubation of 3-OH-β-apo-10'-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10'-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function. Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15’-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9’,10’-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC-MS and GC-MS, we identified both volatile and non-volatile apocarotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10’-carotenal, 3-OH-β-apo-10’-carotenal, and β-apo-10’-carotenal, indicating cleavage at both the 9,10 and 9’,10’ carbon-carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10’-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD+, in vitro incubation of 3-OH-β-apo-10’-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10’-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function. Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15'-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9',10'-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC-MS and GC-MS, we identified both volatile and non-volatile apo-carotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10'-carotenal, 3-OH-β-apo-10'-carotenal, and β-apo-10'-carotenal, indicating cleavage at both the 9,10 and 9',10' carbon-carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10'-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD(+), in vitro incubation of 3-OH-β-apo-10'-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10'-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function.Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15'-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9',10'-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC-MS and GC-MS, we identified both volatile and non-volatile apo-carotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10'-carotenal, 3-OH-β-apo-10'-carotenal, and β-apo-10'-carotenal, indicating cleavage at both the 9,10 and 9',10' carbon-carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10'-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD(+), in vitro incubation of 3-OH-β-apo-10'-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10'-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function.
Author	Mein, Jonathan R. Russell, Robert M. Wang, Xiang-Dong Ernst, Hansgeorg Dolnikowski, Gregory G.
AuthorAffiliation	1 Nutrition and Cancer Biology Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111 3 Fine Chemicals and Biocatalysis Research, GVF/A-B009, BASF AG D-67056, Ludwigshafen, Germany 2 Mass Spectrometry Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111
AuthorAffiliation_xml	– name: 2 Mass Spectrometry Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111 – name: 1 Nutrition and Cancer Biology Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111 – name: 3 Fine Chemicals and Biocatalysis Research, GVF/A-B009, BASF AG D-67056, Ludwigshafen, Germany
Author_xml	– sequence: 1 givenname: Jonathan R. surname: Mein fullname: Mein, Jonathan R. organization: Nutrition and Cancer Biology Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111, USA – sequence: 2 givenname: Gregory G. surname: Dolnikowski fullname: Dolnikowski, Gregory G. organization: Mass Spectrometry Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111, USA – sequence: 3 givenname: Hansgeorg surname: Ernst fullname: Ernst, Hansgeorg organization: Fine Chemicals and Biocatalysis Research, GVF/A-B009, BASF AG, D-67056 Ludwigshafen, Germany – sequence: 4 givenname: Robert M. surname: Russell fullname: Russell, Robert M. organization: Nutrition and Cancer Biology Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111, USA – sequence: 5 givenname: Xiang-Dong surname: Wang fullname: Wang, Xiang-Dong email: xiang-dong.wang@tufts.edu organization: Nutrition and Cancer Biology Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111, USA
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/21081106$$D View this record in MEDLINE/PubMed
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Snippet	[Display omitted] ▸ Vertebrate CMO2 enzymatically cleaves xanthophylls at the 9,10 and 9′,10′ double bond. ▸ Lutein and zeaxanthin are preferentially cleaved... Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases....
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SubjectTerms	Animals Apo-carotenoid beta-cryptoxanthin beta-ionone Carotenoids - biosynthesis Carotenoids - chemistry Cell Line Chromatography, High Pressure Liquid CMO1 CMO2 Cryptoxanthins enzyme kinetics Fatty Acid Desaturases - genetics Fatty Acid Desaturases - metabolism ferrets Ferrets - genetics Ferrets - metabolism Gas Chromatography-Mass Spectrometry high performance liquid chromatography in vitro studies In Vitro Techniques Kinetics Liver - metabolism lutein Lutein - metabolism Metabolism Oxidation-Reduction Recombinant Proteins - genetics Recombinant Proteins - metabolism Spodoptera Substrate Specificity vitamin A Xanthophyll Xanthophylls - metabolism zeaxanthin Zeaxanthins
Title	Enzymatic formation of apo-carotenoids from the xanthophyll carotenoids lutein, zeaxanthin and β-cryptoxanthin by ferret carotene-9′,10′-monooxygenase
URI	https://dx.doi.org/10.1016/j.abb.2010.11.005 https://www.ncbi.nlm.nih.gov/pubmed/21081106 https://www.proquest.com/docview/1753420368 https://www.proquest.com/docview/847279018 https://pubmed.ncbi.nlm.nih.gov/PMC3026080
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