An Aeroplysinin-1 Specific Nitrile Hydratase Isolated from the Marine Sponge Aplysina cavernicola
A nitrile hydratase (NHase) that specifically accepts the nitrile aeroplysinin-1 (1) as a substrate and converts it into the dienone amide verongiaquinol (7) was isolated, partially purified and characterized from the Mediterranean sponge Aplysina cavernicola; although it is currently not known whet...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2013-08-01
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| Series: | Marine Drugs |
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| Online Access: | http://www.mdpi.com/1660-3397/11/8/3046 |
| _version_ | 1828352834332000256 |
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| author | Peter Proksch Lutz Schmitt Bartosz Lipowicz Nils Hanekop |
| author_facet | Peter Proksch Lutz Schmitt Bartosz Lipowicz Nils Hanekop |
| author_sort | Peter Proksch |
| collection | DOAJ |
| description | A nitrile hydratase (NHase) that specifically accepts the nitrile aeroplysinin-1 (1) as a substrate and converts it into the dienone amide verongiaquinol (7) was isolated, partially purified and characterized from the Mediterranean sponge Aplysina cavernicola; although it is currently not known whether the enzyme is of sponge origin or produced by its symbiotic microorganisms. The formation of aeroplysinin-1 and of the corresponding dienone amide is part of the chemical defence system of A. cavernicola. The latter two compounds that show strong antibiotic activity originate from brominated isoxazoline alkaloids that are thought to protect the sponges from invasion of bacterial pathogens. The sponge was shown to contain at least two NHases as two excised protein bands from a non denaturating Blue Native gel showed nitrile hydratase activity, which was not observed for control samples. The enzymes were shown to be manganese dependent, although cobalt and nickel ions were also able to recover the activity of the nitrile hydratases. The temperature and pH optimum of the studied enzymes were found at 41 °C and pH 7.8. The enzymes showed high substrate specificity towards the physiological substrate aeroplysinin-1 (1) since none of the substrate analogues that were prepared either by partial or by total synthesis were converted in an in vitro assay. Moreover de-novo sequencing by mass spectrometry was employed to obtain information about the primary structure of the studied NHases, which did not reveal any homology to known NHases. |
| first_indexed | 2024-04-14T01:58:42Z |
| format | Article |
| id | doaj.art-2cafdce90f5c43139464130de8f6b2a4 |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-04-14T01:58:42Z |
| publishDate | 2013-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-2cafdce90f5c43139464130de8f6b2a42022-12-22T02:18:53ZengMDPI AGMarine Drugs1660-33972013-08-011183046306710.3390/md11083046An Aeroplysinin-1 Specific Nitrile Hydratase Isolated from the Marine Sponge Aplysina cavernicolaPeter ProkschLutz SchmittBartosz LipowiczNils HanekopA nitrile hydratase (NHase) that specifically accepts the nitrile aeroplysinin-1 (1) as a substrate and converts it into the dienone amide verongiaquinol (7) was isolated, partially purified and characterized from the Mediterranean sponge Aplysina cavernicola; although it is currently not known whether the enzyme is of sponge origin or produced by its symbiotic microorganisms. The formation of aeroplysinin-1 and of the corresponding dienone amide is part of the chemical defence system of A. cavernicola. The latter two compounds that show strong antibiotic activity originate from brominated isoxazoline alkaloids that are thought to protect the sponges from invasion of bacterial pathogens. The sponge was shown to contain at least two NHases as two excised protein bands from a non denaturating Blue Native gel showed nitrile hydratase activity, which was not observed for control samples. The enzymes were shown to be manganese dependent, although cobalt and nickel ions were also able to recover the activity of the nitrile hydratases. The temperature and pH optimum of the studied enzymes were found at 41 °C and pH 7.8. The enzymes showed high substrate specificity towards the physiological substrate aeroplysinin-1 (1) since none of the substrate analogues that were prepared either by partial or by total synthesis were converted in an in vitro assay. Moreover de-novo sequencing by mass spectrometry was employed to obtain information about the primary structure of the studied NHases, which did not reveal any homology to known NHases.http://www.mdpi.com/1660-3397/11/8/3046spongesAplysina cavernicolaalkaloidsbiotransformationnitrile hydratase |
| spellingShingle | Peter Proksch Lutz Schmitt Bartosz Lipowicz Nils Hanekop An Aeroplysinin-1 Specific Nitrile Hydratase Isolated from the Marine Sponge Aplysina cavernicola Marine Drugs sponges Aplysina cavernicola alkaloids biotransformation nitrile hydratase |
| title | An Aeroplysinin-1 Specific Nitrile Hydratase Isolated from the Marine Sponge Aplysina cavernicola |
| title_full | An Aeroplysinin-1 Specific Nitrile Hydratase Isolated from the Marine Sponge Aplysina cavernicola |
| title_fullStr | An Aeroplysinin-1 Specific Nitrile Hydratase Isolated from the Marine Sponge Aplysina cavernicola |
| title_full_unstemmed | An Aeroplysinin-1 Specific Nitrile Hydratase Isolated from the Marine Sponge Aplysina cavernicola |
| title_short | An Aeroplysinin-1 Specific Nitrile Hydratase Isolated from the Marine Sponge Aplysina cavernicola |
| title_sort | aeroplysinin 1 specific nitrile hydratase isolated from the marine sponge aplysina cavernicola |
| topic | sponges Aplysina cavernicola alkaloids biotransformation nitrile hydratase |
| url | http://www.mdpi.com/1660-3397/11/8/3046 |
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