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Benjamin F Cravatt - One of the best experts on this subject based on the ideXlab platform.
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chemical and mutagenic investigations of fatty acid amide hydrolase evidence for a family of serine hydrolases with distinct catalytic properties
Biochemistry, 1999Co-Authors: Matthew P Patricelli, Martha Lovato, Benjamin F CravattAbstract:Fatty acid amide hydrolase (FAAH) is a Membrane-Bound Enzyme responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide. FAAH's primary structure identif...
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conserved chromosomal location and genomic structure of human and mouse fatty acid amide hydrolase genes and evaluation of clasper as a candidate neurological mutation
Genomics, 1998Co-Authors: Minghong Wan, Benjamin F Cravatt, Huijun Z Ring, Xianyu Zhang, Uta FranckeAbstract:Fatty-acid amide hydrolase (FAAH) is a Membrane-Bound Enzyme that degrades neuromodulatory fatty acid amides, such as oleamide and anandamide, and is expressed in the mammalian central nervous system. To evaluate FAAH genes as candidates for neurogenetic diseases in humans and mice, we have mapped the loci in both species and have determined their intron-exon structures. The human FAAH gene was mapped to region 1p34-p35, closely linked to D1S197 and D1S443, by using PCR analysis of somatic cell hybrid (SCH) and radiation hybrid mapping panels. Analysis of an SCH mapping panel and a mouse interspecific backcross panel has localized the Faah gene to the conserved syntenic region on mouse chromosome 4, close to the neurological mutation clasper. Faah gene rearrangements were excluded by Southern blot analysis of clasper DNA. No sequence abnormality was detected in PCR products containing the 15 exons and splice junctions of the mouse Faah gene. FAAH protein levels were normal in clasper mouse tissues as determined by Enzyme activity assays and Western blotting.
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fatty acid amide hydrolase the degradative Enzyme for anandamide and oleamide has selective distribution in neurons within the rat central nervous system
Journal of Neuroscience Research, 1997Co-Authors: Elizabeth A. Thomas, Norton B Gilula, Patria E. Danielson, Benjamin F Cravatt, Gregor J SutcliffeAbstract:Fatty acid amide hydrolase (FAAH) is a Membrane-Bound Enzyme activity that degrades neuromodulatory fatty acid amides, including oleamide and anandamide. A single 2.5-kb FAAH mRNA is distributed throughout the rat CNS and accumulates progressively between embryonic day 14 and postnatal day 10, remains high until postnatal day 30, then decreases into adulthood. FAAH enzymatic activity, as measured in dissected brain regions, was well correlated with the distribution of its messenger RNA. In situ hybridization revealed profound distribution of FAAH mRNA in neuronal cells throughout the CNS. The most prominent signals were detected in the neocortex, hippocampal formation, amygdala, and cerebellum. The FAAH distribution in the CNS suggests that degradation of neuromodulatory fatty acid amides at their sites of action influences their effects on sleep, euphoria, and analgesia.
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molecular characterization of an Enzyme that degrades neuromodulatory fatty acid amides
Nature, 1996Co-Authors: Benjamin F Cravatt, Stephen P Mayfield, Dale L Boger, Dan K Giang, Richard A. Lerner, Norton B GilulaAbstract:ENDOGENOUS neuromodulatory molecules are commonly coupled to specific metabolic Enzymes to ensure rapid signal inactivation. Thus, acetylcholine is hydrolysed by acetylcholine esterase1 and tryptamine neurotransmitters like serotonin are degraded by monoamine oxidases2. Previously, we reported the structure and sleep-inducing properties of cis-9-octadecenamide, a lipid isolated from the cerebrospinal fluid of sleep-deprived cats3, cis-9-Octadecenamide, or oleamide, has since been shown to affect serotonergic systems4 and block gap-junction communication in glial cells (our unpublished results). We also identified a Membrane-Bound Enzyme activity that hydrolyses oleamide to its inactive acid, oleic acid3. We now report the mechanism-based isolation, cloning and expression of this Enzyme activity, originally named oleamide hydrolase5, from rat liver plasma mem-branes. We also show that oleamide hydrolase converts anandamide, a fatty-acid amide identified as the endogenous ligand for the cannabinoid receptor6, to arachidonic acid, indi-cating that oleamide hydrolase may serve as the general inactivating Enzyme for a growing family of bioactive signalling molecules, the fatty-acid amides6–8. Therefore we will hereafter refer to oleamide hydrolase as fatty-acid amide hydrolase, in recognition of the plurality of fatty-acid amides that the Enzyme can accept as substrates.
Norton B Gilula - One of the best experts on this subject based on the ideXlab platform.
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fatty acid amide hydrolase the degradative Enzyme for anandamide and oleamide has selective distribution in neurons within the rat central nervous system
Journal of Neuroscience Research, 1997Co-Authors: Elizabeth A. Thomas, Norton B Gilula, Patria E. Danielson, Benjamin F Cravatt, Gregor J SutcliffeAbstract:Fatty acid amide hydrolase (FAAH) is a Membrane-Bound Enzyme activity that degrades neuromodulatory fatty acid amides, including oleamide and anandamide. A single 2.5-kb FAAH mRNA is distributed throughout the rat CNS and accumulates progressively between embryonic day 14 and postnatal day 10, remains high until postnatal day 30, then decreases into adulthood. FAAH enzymatic activity, as measured in dissected brain regions, was well correlated with the distribution of its messenger RNA. In situ hybridization revealed profound distribution of FAAH mRNA in neuronal cells throughout the CNS. The most prominent signals were detected in the neocortex, hippocampal formation, amygdala, and cerebellum. The FAAH distribution in the CNS suggests that degradation of neuromodulatory fatty acid amides at their sites of action influences their effects on sleep, euphoria, and analgesia.
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molecular characterization of an Enzyme that degrades neuromodulatory fatty acid amides
Nature, 1996Co-Authors: Benjamin F Cravatt, Stephen P Mayfield, Dale L Boger, Dan K Giang, Richard A. Lerner, Norton B GilulaAbstract:ENDOGENOUS neuromodulatory molecules are commonly coupled to specific metabolic Enzymes to ensure rapid signal inactivation. Thus, acetylcholine is hydrolysed by acetylcholine esterase1 and tryptamine neurotransmitters like serotonin are degraded by monoamine oxidases2. Previously, we reported the structure and sleep-inducing properties of cis-9-octadecenamide, a lipid isolated from the cerebrospinal fluid of sleep-deprived cats3, cis-9-Octadecenamide, or oleamide, has since been shown to affect serotonergic systems4 and block gap-junction communication in glial cells (our unpublished results). We also identified a Membrane-Bound Enzyme activity that hydrolyses oleamide to its inactive acid, oleic acid3. We now report the mechanism-based isolation, cloning and expression of this Enzyme activity, originally named oleamide hydrolase5, from rat liver plasma mem-branes. We also show that oleamide hydrolase converts anandamide, a fatty-acid amide identified as the endogenous ligand for the cannabinoid receptor6, to arachidonic acid, indi-cating that oleamide hydrolase may serve as the general inactivating Enzyme for a growing family of bioactive signalling molecules, the fatty-acid amides6–8. Therefore we will hereafter refer to oleamide hydrolase as fatty-acid amide hydrolase, in recognition of the plurality of fatty-acid amides that the Enzyme can accept as substrates.
Ulf Eriksson - One of the best experts on this subject based on the ideXlab platform.
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the identification of a 9 cis retinol dehydrogenase in the mouse embryo reveals a pathway for synthesis of 9 cis retinoic acid
Proceedings of the National Academy of Sciences of the United States of America, 1998Co-Authors: Anna Romert, Andras Simon, Paulina Tuvendal, Lennart Dencker, Ulf ErikssonAbstract:The ligand-controlled retinoic acid (RA) receptors and retinoid X receptors are important for several physiological processes, including normal embryonic development, but little is known about how their ligands, all-trans and 9-cis RA, are generated. Here we report the identification of a stereo-specific 9-cis retinol dehydrogenase, which is abundantly expressed in embryonic tissues known to be targets in the retinoid signaling pathway. The Membrane-Bound Enzyme is a member of the short-chain alcohol dehydrogenase/reductase superfamily, able to oxidize 9-cis retinol into 9-cis retinaldehyde, an intermediate in 9-cis RA biosynthesis. Analysis by nonradioactive in situ hybridization in mouse embryos shows that expression of the Enzyme is temporally and spatially well controlled during embryogenesis with prominent expression in parts of the developing central nervous system, sensory organs, somites and myotomes, and several tissues of endodermal origin. The identification of this Enzyme reveals a pathway in RA biosynthesis, where 9-cis retinol is generated for subsequent oxidation to 9-cis RA.
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primary structure of human 11 cis retinol dehydrogenase and organization and chromosomal localization of the corresponding gene
Genomics, 1996Co-Authors: Andras Simon, Jacob Lagercrantz, Svetlana Bajalicalagercrantz, Ulf ErikssonAbstract:Abstract The universal chromophore of visual pigments in higher animals is 11- cis retinaldehyde. The final step in the biosynthetic pathway generating this compound is catalyzed by 11- cis retinol dehydrogenase, a Membrane-Bound Enzyme abundantly expressed in the retinal pigment epithelium of the eye. In this work we demonstrate that the primary structure of human 11- cis retinol dehydrogenase is highly conserved with 91% identity to the bovine Enzyme. The gene encoding 11- cis retinol dehydrogenase spans over ≈4.1 kb of DNA and is divided into four translated exons. Analysis of a panel of somatic cells hybrids and fluorescence in situ hybridization on metaphase chromosomes revealed that the gene is located on chromosome 12q13–q14. Due to the unique role of 11- cis retinol dehydrogenase in the generation of visual pigments, it is a candidate gene for involvement in hereditary eye disease.
Kazunobu Matsushita - One of the best experts on this subject based on the ideXlab platform.
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formation of 4 keto d aldopentoses and 4 pentulosonates 4 keto d pentonates with unidentified membrane bound Enzymes from acetic acid bacteria
Bioscience Biotechnology and Biochemistry, 2011Co-Authors: Osao Adachi, Toshiharu Yakushi, Roque Alberto Hours, Emiko Shinagawa, Yoshihiko Akakabe, Kazunobu MatsushitaAbstract:In our previous study, a new microbial reaction yielding 4-keto-D-arabonate from 2,5-diketo-D-gluconate was identified with Gluconacetobacter liquefaciens RCTMR 10. It appeared that decarboxylation and dehydrogenation took place together in the reaction. To analyze the nature of the reaction, investigations were done with the membrane fraction of the organism, and 4-keto-D-arabinose was confirmed as the direct precursor of 4-keto-D-arabonate. Two novel Membrane-Bound Enzymes, 2,5-diketo-D-gluconate decarboxylase and 4-keto-D-aldopentose 1-dehydrogenase, were involved in the reaction. Alternatively, D-arabonate was oxidized to 4-keto-D-arabonate by another Membrane-Bound Enzyme, D-arabonate 4-dehydrogenase. More directly, D-arabinose oxidation was examined with growing cells and with the membrane fraction of G. suboxydans IFO 12528. 4-Keto-D-arabinose, the same intermediate as that from 2,5-diketo-D-gluconate, was detected, and it was oxidized to 4-keto-D-arabonate. Likewise, D-ribose was oxidized to 4-keto-D-ribose and then it was oxidized to 4-keto-D-ribonate. In addition to 4-keto-D-aldopentose 1-dehydrogenase, the presence of a novel Membrane-Bound Enzyme, D-aldopentose 4-dehydrogenase, was confirmed in the membrane fraction. The formation of 4-keto-D-aldopentoses and 4-keto-D-pentonates (4-pentulosonates) was finally confirmed as reaction products of four different novel Membrane-Bound Enzymes.
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Alcohol dehydrogenase of acetic acid bacteria: structure, mode of action, and applications in biotechnology
Applied Microbiology and Biotechnology, 2010Co-Authors: Toshiharu Yakushi, Kazunobu MatsushitaAbstract:Pyrroquinoline quinone-dependent alcohol dehydrogenase (PQQ-ADH) of acetic acid bacteria is a Membrane-Bound Enzyme involved in the acetic acid fermentation by oxidizing ethanol to acetaldehyde coupling with reduction of membranous ubiquinone (Q), which is, in turn, re-oxidized by ubiquinol oxidase, reducing oxygen to water. PQQ-ADHs seem to have co-evolved with the organisms fitting to their own habitats. The Enzyme consists of three subunits and has a pyrroloquinoline quinone, 4 heme c moieties, and a tightly bound Q as the electron transfer mediators. Biochemical, genetic, and electrochemical studies have revealed the unique properties of PQQ-ADH since it was purified in 1978. The Enzyme is unique to have ubiquinol oxidation activity in addition to Q reduction. This mini-review focuses on the molecular properties of PQQ-ADH, such as the roles of the subunits and the cofactors, particularly in intramolecular electron transport of the Enzyme from ethanol to Q. Also, we summarize biotechnological applications of PQQ-ADH as to enantiospecific oxidations for production of the valuable chemicals and bioelectrocatalysis for sensors and fuel cells using indirect and direct electron transfer technologies and discuss unsolved issues and future prospects related to this elaborate Enzyme.
Gregor J Sutcliffe - One of the best experts on this subject based on the ideXlab platform.
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Rapid Communication Fatty Acid Amide Hydrolase, the Degradative Enzyme for Anandamide and Oleamide, Has Selective Distribution in Neurons Within the Rat Central Nervous System
2014Co-Authors: Gregor J SutcliffeAbstract:Fatty acid amide hydrolase (FAAH) is a Membrane-Bound Enzyme activity that degrades neuromodula-tory fatty acid amides, including oleamide and anan-damide. A single 2.5-kb FAAH mRNA is distributed throughout the rat CNS and accumulates progres-sively between embryonic day 14 and postnatal day 10, remains high until postnatal day 30, then decreases into adulthood. FAAH enzymatic activity, as mea-sured in dissected brain regions, was well correlated with the distribution of its messenger RNA. In situ hybridization revealed profound distribution of FAAH mRNA in neuronal cells throughout the CNS. The most prominent signals were detected in the neocor-tex, hippocampal formation, amygdala, and cerebel-lum. The FAAH distribution in the CNS suggests that degradation of neuromodulatory fatty acid amides at their sites of action influences their effects on sleep, euphoria, and analgesia. J. Neurosci. Res. 50:1047
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fatty acid amide hydrolase the degradative Enzyme for anandamide and oleamide has selective distribution in neurons within the rat central nervous system
Journal of Neuroscience Research, 1997Co-Authors: Elizabeth A. Thomas, Norton B Gilula, Patria E. Danielson, Benjamin F Cravatt, Gregor J SutcliffeAbstract:Fatty acid amide hydrolase (FAAH) is a Membrane-Bound Enzyme activity that degrades neuromodulatory fatty acid amides, including oleamide and anandamide. A single 2.5-kb FAAH mRNA is distributed throughout the rat CNS and accumulates progressively between embryonic day 14 and postnatal day 10, remains high until postnatal day 30, then decreases into adulthood. FAAH enzymatic activity, as measured in dissected brain regions, was well correlated with the distribution of its messenger RNA. In situ hybridization revealed profound distribution of FAAH mRNA in neuronal cells throughout the CNS. The most prominent signals were detected in the neocortex, hippocampal formation, amygdala, and cerebellum. The FAAH distribution in the CNS suggests that degradation of neuromodulatory fatty acid amides at their sites of action influences their effects on sleep, euphoria, and analgesia.