The AMP deaminase of the mollusk Helix pomatia is an unexpected member of the adenosine deaminase-related growth factor (ADGF) family

We report here the first occurrence of an adenosine deaminase-related growth factor (ADGF) that deaminates adenosine 5' monophosphate (AMP) in preference to adenosine. The ADGFs are a group of secreted deaminases found throughout the animal kingdom that affect the extracellular concentration of...

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Published inPloS one Vol. 18; no. 7; p. e0286435
Main Authors Tzertzinis, George, Ganatra, Mehul B, Ruse, Cristian, Taron, Christopher H, Causey, Bryce, Wang, Liang, Schildkraut, Ira
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 20.07.2023
Subjects
Adenosine
Adenosine - metabolism
Adenosine deaminase
Adenosine Deaminase - metabolism
Adenosine Monophosphate
Adenylic acid
Amino acid sequence
Amino acids
AMP
AMP Deaminase
Animals
Biochemical characteristics
Biochemistry
Biology and Life Sciences
Cloning
Enzymes
Growth factors
Helix pomatia
Intercellular Signaling Peptides and Proteins
Mass spectrometry
Medicine and Health Sciences
Mollusca - metabolism
Mollusks
Peptides
Properties
Proteins
Research and Analysis Methods
Scientific imaging
Substrates
United States
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Summary:We report here the first occurrence of an adenosine deaminase-related growth factor (ADGF) that deaminates adenosine 5' monophosphate (AMP) in preference to adenosine. The ADGFs are a group of secreted deaminases found throughout the animal kingdom that affect the extracellular concentration of adenosine by converting it to inosine. The AMP deaminase studied here was first isolated and biochemically characterized from the roman snail Helix pomatia in 1983. Determination of the amino acid sequence of the AMP deaminase enabled sequence comparisons to protein databases and revealed it as a member of the ADGF family. Cloning and expression of its cDNA in Pichia pastoris allowed the comparison of the biochemical characteristics of the native and recombinant forms of the enzyme and confirmed they correspond to the previously reported activity. Uncharacteristically, the H. pomatia AMP deaminase was determined to be dissimilar to the AMP deaminase family by sequence comparison while demonstrating similarity to the ADGFs despite having AMP as its preferred substrate rather than adenosine.
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Current address: Moderna Therapeutics, Cambridge, MA, United States of America
Competing Interests: I have read the journal’s policy and the authors of this manuscript have the following competing interests. George Tzertzinis, Mehul B. Ganatra, Cristian Ruse, Christopher H. Taron, Bryce Causey, Liang Wang, Ira Schildkraut are/were employees of New England Biolabs, a manufacturer and vendor of molecular biology reagents. New England Biolabs funded the work and paid the salaries of all authors. There are no patents, products in development or marketed products to declare. This does not alter our adherence to PLOS ONE policies on sharing data and materials.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0286435