ArticleMarine biotechnology (New York, N.Y.)2011
Molecular characterization of adenosine 5'-monophosphate deaminase--the key enzyme responsible for the umami taste of nori (Porphyra yezoensis Ueda, Rhodophyta).
Article in Marine biotechnology (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 15 citations in OpenAlex.
- The fructose survival hypothesis for obesity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Review
- Proteomics and Metabolomics Profiling of Pork Exudate Reveals Meat Spoilage during Storage.Metabolites · 2022Article
- Impact of Chilling Rate on the Evolution of Volatile and Non-Volatile Compounds in Raw Lamb Meat during Refrigeration.Foods (Basel, Switzerland) · 2021Article
- Umami-induced obesity and metabolic syndrome is mediated by nucleotide degradation and uric acid generation.Nature metabolism · 2021Article
- Perspective: A Historical and Scientific Perspective of Sugar and Its Relation with Obesity and Diabetes.Advances in nutrition (Bethesda, Md.) · 2017Review
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
The enzyme adenosine 5'-monophosphate deaminase (AMPD, EC 3.5.4.6) catalyzes the conversion of adenosine 5'-monophosphate to inosine 5'-mononucleotide (IMP). IMP is generally known as the compound responsible for the umami taste of the edible red alga Porphyra yezoensis Ueda that is known in Japan as nori. Therefore, we suspect that AMPD plays a key role in providing a favorable nori taste. In this study, we undertake the molecular characterization of nori-derived AMPD. The nori AMPD protein has a molecular mass of 55 kDa as estimated from both gel filtration and sodium dodecyl sulfate polyacrylamide gel electrophoresis. The calculated molecular mass from the amino acid sequence deduced from cDNA is 57.1 kDa. The isoelectric point is 5.71. The coding region of AMPD consists of 1,566 bp encoding 522 amino acids and possesses a transmembrane domain and two N-glycosylation sites. The sequence identity of nori AMPD in human and yeast AMPDs was found to be less than 50% and 20% in DNA and amino acid sequences, respectively. Proline in the conserved motif of [SA]-[LIVM]-[NGS]-[STA]-D-D-P was found to be converted to glutamate. These results indicate that nori AMPD is a novel type of AMPD.
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