The Experts below are selected from a list of 168 Experts worldwide ranked by ideXlab platform
Jing-ke Weng - One of the best experts on this subject based on the ideXlab platform.
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monoamine biosynthesis via a noncanonical calcium activatable aromatic amino acid decarboxylase in Psilocybin Mushroom
ACS Chemical Biology, 2018Co-Authors: Michael P Torrensspence, Chun-ting Liu, Tomáš Pluskal, Yin Kwan Chung, Jing-ke WengAbstract:Aromatic l-amino acid decarboxylases (AAADs) are a phylogenetically diverse group of enzymes responsible for the decarboxylation of aromatic amino acid substrates into their corresponding aromatic arylalkylamines. AAADs have been extensively studied in mammals and plants as they catalyze the first step in the production of neurotransmitters and bioactive phytochemicals, respectively. Unlike mammals and plants, the hallucinogenic Psilocybin Mushroom Psilocybe cubensis reportedly employs an unrelated phosphatidylserine-decarboxylase-like enzyme to catalyze l-tryptophan decarboxylation, the first step in Psilocybin biosynthesis. To explore the origin of this chemistry in Psilocybin Mushroom, we generated the first de novo transcriptomes of P. cubensis and investigated several putative l-tryptophan-decarboxylase-like enzymes. We report the biochemical characterization of a noncanonical AAAD from P. cubensis ( PcncAAAD) that exhibits substrate permissiveness toward l-phenylalanine, l-tyrosine, and l-tryptophan, as well as chloro-tryptophan derivatives. The crystal structure of PcncAAAD revealed the presence of a unique C-terminal appendage domain featuring a novel double-β-barrel fold. This domain is required for PcncAAAD activity and regulates catalytic rate and thermal stability through calcium binding. PcncAAAD likely plays a role in Psilocybin production in P. cubensis and offers a new tool for metabolic engineering of aromatic-amino-acid-derived natural products.
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Monoamine Biosynthesis via a Noncanonical Calcium-Activatable Aromatic Amino Acid Decarboxylase in Psilocybin Mushroom
2018Co-Authors: Michael Patrick Torrens-spence, Chun-ting Liu, Tomáš Pluskal, Yin Kwa Chung, Jing-ke WengAbstract:Aromatic l-amino acid decarboxylases (AAADs) are a phylogenetically diverse group of enzymes responsible for the decarboxylation of aromatic amino acid substrates into their corresponding aromatic arylalkylamines. AAADs have been extensively studied in mammals and plants as they catalyze the first step in the production of neurotransmitters and bioactive phytochemicals, respectively. Unlike mammals and plants, the hallucinogenic Psilocybin Mushroom Psilocybe cubensis reportedly employs an unrelated phosphatidylserine-decarboxylase-like enzyme to catalyze l-tryptophan decarboxylation, the first step in Psilocybin biosynthesis. To explore the origin of this chemistry in Psilocybin Mushroom, we generated the first de novo transcriptomes of P. cubensis and investigated several putative l-tryptophan-decarboxylase-like enzymes. We report the biochemical characterization of a noncanonical AAAD from P. cubensis (PcncAAAD) that exhibits substrate permissiveness toward l-phenylalanine, l-tyrosine, and l-tryptophan, as well as chloro-tryptophan derivatives. The crystal structure of PcncAAAD revealed the presence of a unique C-terminal appendage domain featuring a novel double-β-barrel fold. This domain is required for PcncAAAD activity and regulates catalytic rate and thermal stability through calcium binding. PcncAAAD likely plays a role in Psilocybin production in P. cubensis and offers a new tool for metabolic engineering of aromatic-amino-acid-derived natural products
Yin Kwan Chung - One of the best experts on this subject based on the ideXlab platform.
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monoamine biosynthesis via a noncanonical calcium activatable aromatic amino acid decarboxylase in Psilocybin Mushroom
ACS Chemical Biology, 2018Co-Authors: Michael P Torrensspence, Chun-ting Liu, Tomáš Pluskal, Yin Kwan Chung, Jing-ke WengAbstract:Aromatic l-amino acid decarboxylases (AAADs) are a phylogenetically diverse group of enzymes responsible for the decarboxylation of aromatic amino acid substrates into their corresponding aromatic arylalkylamines. AAADs have been extensively studied in mammals and plants as they catalyze the first step in the production of neurotransmitters and bioactive phytochemicals, respectively. Unlike mammals and plants, the hallucinogenic Psilocybin Mushroom Psilocybe cubensis reportedly employs an unrelated phosphatidylserine-decarboxylase-like enzyme to catalyze l-tryptophan decarboxylation, the first step in Psilocybin biosynthesis. To explore the origin of this chemistry in Psilocybin Mushroom, we generated the first de novo transcriptomes of P. cubensis and investigated several putative l-tryptophan-decarboxylase-like enzymes. We report the biochemical characterization of a noncanonical AAAD from P. cubensis ( PcncAAAD) that exhibits substrate permissiveness toward l-phenylalanine, l-tyrosine, and l-tryptophan, as well as chloro-tryptophan derivatives. The crystal structure of PcncAAAD revealed the presence of a unique C-terminal appendage domain featuring a novel double-β-barrel fold. This domain is required for PcncAAAD activity and regulates catalytic rate and thermal stability through calcium binding. PcncAAAD likely plays a role in Psilocybin production in P. cubensis and offers a new tool for metabolic engineering of aromatic-amino-acid-derived natural products.
Michael P Torrensspence - One of the best experts on this subject based on the ideXlab platform.
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monoamine biosynthesis via a noncanonical calcium activatable aromatic amino acid decarboxylase in Psilocybin Mushroom
ACS Chemical Biology, 2018Co-Authors: Michael P Torrensspence, Chun-ting Liu, Tomáš Pluskal, Yin Kwan Chung, Jing-ke WengAbstract:Aromatic l-amino acid decarboxylases (AAADs) are a phylogenetically diverse group of enzymes responsible for the decarboxylation of aromatic amino acid substrates into their corresponding aromatic arylalkylamines. AAADs have been extensively studied in mammals and plants as they catalyze the first step in the production of neurotransmitters and bioactive phytochemicals, respectively. Unlike mammals and plants, the hallucinogenic Psilocybin Mushroom Psilocybe cubensis reportedly employs an unrelated phosphatidylserine-decarboxylase-like enzyme to catalyze l-tryptophan decarboxylation, the first step in Psilocybin biosynthesis. To explore the origin of this chemistry in Psilocybin Mushroom, we generated the first de novo transcriptomes of P. cubensis and investigated several putative l-tryptophan-decarboxylase-like enzymes. We report the biochemical characterization of a noncanonical AAAD from P. cubensis ( PcncAAAD) that exhibits substrate permissiveness toward l-phenylalanine, l-tyrosine, and l-tryptophan, as well as chloro-tryptophan derivatives. The crystal structure of PcncAAAD revealed the presence of a unique C-terminal appendage domain featuring a novel double-β-barrel fold. This domain is required for PcncAAAD activity and regulates catalytic rate and thermal stability through calcium binding. PcncAAAD likely plays a role in Psilocybin production in P. cubensis and offers a new tool for metabolic engineering of aromatic-amino-acid-derived natural products.
Ferianto, Damianus Diaz - One of the best experts on this subject based on the ideXlab platform.
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TINJAUAN PELAKSANAAN KETENTUAN PIDANA UNDANGUNDANG NOMOR 35 TAHUN 2009 TERHADAP PENYALAHGUNAAN MAGIC Mushroom
UAJY, 2014Co-Authors: Ferianto, Damianus DiazAbstract:Narcotic is substance or drug derived from plants or not plants, whether synthesis and semisynthesis, that can cause to drop or change consciousness, loss of sense, reduce to losing painfull and may inflict dependence distinguished into classesclasses as attached in this legislation. One example of phenomenon that now has potential as a serious problem which must be examined and dealt with the issue be solved, is widespread abuse of magic Mushroom which according to Act No. 35 of 2009 is the one that is included in the list of narcotic group I, namely substance group of psilosibin where the content of these substances exist in the magic Mushroom or Psilocybin Mushroom. Magic Mushroom is a psychedelic Mushroom species, commonly called gold caps, golden tops, cubes, purple rings or boomers. In Indonesia the knowledge of this fungus as a cow dung fungus which this fungus belong to the genus psilocybe. Mushroom Psilocybe Cubensis or cow dung fungus can be found throughout South America, Asia, Europe and Australia. Psilocybe Cubensis is a type of fungus that grows and lives above the suface of the dung breed like cows, buffaloes, bulls and others. This fungus can grow in any climate, in the mountins or at the edge of sea. From an understanding of criminal provisions and rules according to Act No. 35 of 2009 about narcotics group I above, has been very clearly mentioned that the magic Mushroom as narcotics group I in the form of the plant should not be misused with the left free to be sold or produced, distributed and consumed by the public at large. This fungus is not the usual type of Mushrooms that are fit to be consumed, but rather a fungus that can cause hallucinations. It should not need to doubt any longer that all the rules about the crime that exists in Act No. 35 of 2009 is a crime. The most fundamental reason is the narcotic drugs should only be used for the treatment and the importance of science, then when there is an act outside those interests should be a crime
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TINJAUAN PELAKSANAAN KETENTUAN PIDANA UNDANGUNDANG NOMOR 35 TAHUN 2009 TERHADAP PENYALAHGUNAAN MAGIC Mushroom
2014Co-Authors: Ferianto, Damianus DiazAbstract:Narcotic is substance or drug derived from plants or not plants, whether synthesis and semisynthesis, that can cause to drop or change consciousness, loss of sense, reduce to losing painfull and may inflict dependence distinguished into classesclasses as attached in this legislation. One example of phenomenon that now has potential as a serious problem which must be examined and dealt with the issue be solved, is widespread abuse of magic Mushroom which according to Act No. 35 of 2009 is the one that is included in the list of narcotic group I, namely substance group of psilosibin where the content of these substances exist in the magic Mushroom or Psilocybin Mushroom. Magic Mushroom is a psychedelic Mushroom species, commonly called gold caps, golden tops, cubes, purple rings or boomers. In Indonesia the knowledge of this fungus as a cow dung fungus which this fungus belong to the genus psilocybe. Mushroom Psilocybe Cubensis or cow dung fungus can be found throughout South America, Asia, Europe and Australia. Psilocybe Cubensis is a type of fungus that grows and lives above the suface of the dung breed like cows, buffaloes, bulls and others. This fungus can grow in any climate, in the mountins or at the edge of sea. From an understanding of criminal provisions and rules according to Act No. 35 of 2009 about narcotics group I above, has been very clearly mentioned that the magic Mushroom as narcotics group I in the form of the plant should not be misused with the left free to be sold or produced, distributed and consumed by the public at large. This fungus is not the usual type of Mushrooms that are fit to be consumed, but rather a fungus that can cause hallucinations. It should not need to doubt any longer that all the rules about the crime that exists in Act No. 35 of 2009 is a crime. The most fundamental reason is the narcotic drugs should only be used for the treatment and the importance of science, then when there is an act outside those interests should be a crime
Chun-ting Liu - One of the best experts on this subject based on the ideXlab platform.
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monoamine biosynthesis via a noncanonical calcium activatable aromatic amino acid decarboxylase in Psilocybin Mushroom
ACS Chemical Biology, 2018Co-Authors: Michael P Torrensspence, Chun-ting Liu, Tomáš Pluskal, Yin Kwan Chung, Jing-ke WengAbstract:Aromatic l-amino acid decarboxylases (AAADs) are a phylogenetically diverse group of enzymes responsible for the decarboxylation of aromatic amino acid substrates into their corresponding aromatic arylalkylamines. AAADs have been extensively studied in mammals and plants as they catalyze the first step in the production of neurotransmitters and bioactive phytochemicals, respectively. Unlike mammals and plants, the hallucinogenic Psilocybin Mushroom Psilocybe cubensis reportedly employs an unrelated phosphatidylserine-decarboxylase-like enzyme to catalyze l-tryptophan decarboxylation, the first step in Psilocybin biosynthesis. To explore the origin of this chemistry in Psilocybin Mushroom, we generated the first de novo transcriptomes of P. cubensis and investigated several putative l-tryptophan-decarboxylase-like enzymes. We report the biochemical characterization of a noncanonical AAAD from P. cubensis ( PcncAAAD) that exhibits substrate permissiveness toward l-phenylalanine, l-tyrosine, and l-tryptophan, as well as chloro-tryptophan derivatives. The crystal structure of PcncAAAD revealed the presence of a unique C-terminal appendage domain featuring a novel double-β-barrel fold. This domain is required for PcncAAAD activity and regulates catalytic rate and thermal stability through calcium binding. PcncAAAD likely plays a role in Psilocybin production in P. cubensis and offers a new tool for metabolic engineering of aromatic-amino-acid-derived natural products.
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Monoamine Biosynthesis via a Noncanonical Calcium-Activatable Aromatic Amino Acid Decarboxylase in Psilocybin Mushroom
2018Co-Authors: Michael Patrick Torrens-spence, Chun-ting Liu, Tomáš Pluskal, Yin Kwa Chung, Jing-ke WengAbstract:Aromatic l-amino acid decarboxylases (AAADs) are a phylogenetically diverse group of enzymes responsible for the decarboxylation of aromatic amino acid substrates into their corresponding aromatic arylalkylamines. AAADs have been extensively studied in mammals and plants as they catalyze the first step in the production of neurotransmitters and bioactive phytochemicals, respectively. Unlike mammals and plants, the hallucinogenic Psilocybin Mushroom Psilocybe cubensis reportedly employs an unrelated phosphatidylserine-decarboxylase-like enzyme to catalyze l-tryptophan decarboxylation, the first step in Psilocybin biosynthesis. To explore the origin of this chemistry in Psilocybin Mushroom, we generated the first de novo transcriptomes of P. cubensis and investigated several putative l-tryptophan-decarboxylase-like enzymes. We report the biochemical characterization of a noncanonical AAAD from P. cubensis (PcncAAAD) that exhibits substrate permissiveness toward l-phenylalanine, l-tyrosine, and l-tryptophan, as well as chloro-tryptophan derivatives. The crystal structure of PcncAAAD revealed the presence of a unique C-terminal appendage domain featuring a novel double-β-barrel fold. This domain is required for PcncAAAD activity and regulates catalytic rate and thermal stability through calcium binding. PcncAAAD likely plays a role in Psilocybin production in P. cubensis and offers a new tool for metabolic engineering of aromatic-amino-acid-derived natural products
