ArticleMarine drugs2011
Molecular evolution of multiple arylalkylamine N-acetyltransferase (AANAT) in fish.
Article in Marine drugs, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Functional Characterization of SerotoninAntioxidants (Basel, Switzerland) · 2022Article
- Melatonin biosynthesis pathways in nature and its production in engineered microorganisms.Synthetic and systems biotechnology · 2022Review
- Evolutionary Genomics Reveals Multiple Functions of ArylalkylamineFrontiers in genetics · 2022Review
- Melatonin and Pathological Cell Interactions: Mitochondrial Glucose Processing in Cancer Cells.International journal of molecular sciences · 2021Review
- Resource: A multi-species multi-timepoint transcriptome database and webpage for the pineal gland and retina.Journal of pineal research · 2020Article
- Growth and survival of Takifugu rubripes larvae cultured under different light conditions.Fish physiology and biochemistry · 2019Article
- A Comparative Genomic Survey Provides Novel Insights into Molecular Evolution of l-Aromatic Amino Acid Decarboxylase in Vertebrates.Molecules (Basel, Switzerland) · 2018Article
- A Comparative Genomic and Transcriptomic Survey Provides Novel Insights into N-Acetylserotonin Methyltransferase (ASMT) in Fish.Molecules (Basel, Switzerland) · 2017Article
- The Role of Melatonin as a Hormone and an Antioxidant in the Control of Fish Reproduction.Frontiers in endocrinology · 2016Review
- Molecular Evolution of Aralkylamine N-Acetyltransferase in Fish: A Genomic Survey.International journal of molecular sciences · 2015Article
- Drastic neofunctionalization associated with evolution of the timezyme AANAT 500 Mya.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The timing of Timezyme diversification in vertebrates.PloS one · 2014Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Arylalkylamine N-acetyltransferase (AANAT) catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to arylalkylamines, including indolethylamines and phenylethylamines. Multiple aanats are present in teleost fish as a result of whole genome and gene duplications. Fish aanat1a and aanat2 paralogs display different patterns of tissue expression and encode proteins with different substrate preference: AANAT1a is expressed in the retina, and acetylates both indolethylamines and phenylethylamines; while AANAT2 is expressed in the pineal gland, and preferentially acetylates indolethylamines. The two enzymes are therefore thought to serve different roles. Here, the molecular changes that led to their specialization were studied by investigating the structure-function relationships of AANATs in the gilthead seabream (sb, Sperus aurata). Acetylation activity of reciprocal mutated enzymes pointed to specific residues that contribute to substrate specificity of the enzymes. Inhibition tests followed by complementary analyses of the predicted three-dimensional models of the enzymes, suggested that both phenylethylamines and indolethylamines bind to the catalytic pocket of both enzymes. These results suggest that substrate selectivity of AANAT1a and AANAT2 is determined by the positioning of the substrate within the catalytic pocket, and its accessibility to catalysis. This illustrates the evolutionary process by which enzymes encoded by duplicated genes acquire different activities and play different biological roles.
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