ATP N-glycosidase - a novel ATP-converting activity from a marine sponge Axinella polypoides.

  title={ATP N-glycosidase - a novel ATP-converting activity from a marine sponge Axinella polypoides.},
  author={T{\~o}nu Reintamm and Annika Lopp and Anne Kuusksalu and T{\~o}nis Pehk and Merike Kelve},
  journal={European journal of biochemistry},
  volume={270 20},
A novel nucleosidase enzymatic activity was discovered in the marine sponge Axinella polypoides. This enzyme, designated as ATP N-glycosidase, converts adenosine-5'-triphosphate into adenine and ribose-5-triphosphate. The crude extract of A. polypoides was capable of hydrolysing 25 micro mol ATP.min-1 per g wet weight of sponge. The catalytic activity of a sponge crude extract per mg total protein is comparable with specific activities of purified plant adenosine and bacterial AMP nucleosidases… 
ADP-ribosyl cyclases generate two unusual adenine homodinucleotides with cytotoxic activity on mammalian cells.
It is shown that cyclases from lower and higher Metazoa also synthesize three adenylic dinucleotides from cADPR and adenine: diadenosine diphosphate and two isomers thereof, which are naturally occurring nucleotides containing an N-glycosidic bond different from the usual C1'-N9.
Metabolism of diadenosine tetraphosphate (Ap4A) and related nucleotides in plants; review with historical and general perspective.
  • A. Guranowski
  • Biology
    Frontiers in bioscience : a journal and virtual library
  • 2004
The ubiquity of both the compounds and enzymes that can synthesize them (certain ligases and transferases), the demonstration that certain plant ligases can synthesizing pnAs and ApnNs in vitro, and the existence in plants of specific and nonspecific degradative enzymes strongly suggest that these various pnNs and NpnN's do indeed occur and play a biological role in plant cells.
Analogs of diadenosine tetraphosphate (Ap4A).
This review summarizes the knowledge of analogs and derivatives of diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A), the most extensively studied member of the dinucleoside 5',4"'- P1, Pn-polyphosphate family, and their practical applications.
Biological Activities of the Marine Sponge Axinella
The sponge class Demospongiae is known to produce the largest number and diversity of secondary metabolites isolated from marine invertebrates, and there is some evidence that they provide chemical defenses against predators5-7.
Biological Activities of the Marine Sponge
Marine natural products have attracted the attention of biologists and chemists on the world over for the last five decades. The ocean is considered to be a source of potential drugs. Covering around
Proteoglycans from Marine Sponges and Their Biomedical Applications
The interaction of proteins with GAG may have potential significant implications for biomedical roles including anticoagulant, antibacterial, antiviral, anti-inflammatory, and so on, and as an alternative therapeutic agent in the field of biochemical/pharmacological/microbial/molecular biology.
Methylene analogues of adenosine 5'-tetraphosphate. Their chemical synthesis and recognition by human and plant mononucleoside tetraphosphatases and dinucleoside tetraphosphatases.
Novel nucleotides are synthesized that are identified as being the strongest inhibitors ever reported for the (asymmetrical) din nucleoside tetraphosphatases and should prove valuable tools for further studies on the cellular functions of mono- and dinucleoside polyphosphates and on the enzymes involved in their metabolism.


Enzyme-Substrate Interactions in the Purine-specific Nucleoside Hydrolase from Trypanosoma vivax*
Site-directed mutagenesis indicates that the purine specificity of the IAG-NHs is imposed by a parallel aromatic stacking interaction involving Trp83 and Trp260 and the pH profiles of k cat and k cat/K m indicate the existence of one or more proton donors, possibly involved in leaving group activation.
Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax.
The purine salvage pathway of parasitic protozoa is currently considered as a target for drug development because these organisms cannot synthesize purines de novo. Insight into the structure and
Purification and some properties of NAD-degrading purine nucleosidase from Aspergillus niger.
An enzyme which degrades NAD at the adenine-ribose linkage has been purified from the mycelial extract of Aspergillus niger and the substrate specificity showed that the enzyme may be classified as a N-ribosyl-purine ribohydrolase.
Unifying mechanism for Aplysia ADP-ribosyl cyclase and CD38/NAD(+) glycohydrolases.
A 'partitioning' reaction scheme for the Aplysia enzyme is proposed, similar to that established previously for mammalian CD38/NAD(+) glycohydrolases, which involves the formation of a single oxocarbenium-type intermediate that partitions to cADP-ribose and solvolytic products via competing pathways.
Purification, Characterization, and Gene Cloning of Purine Nucleosidase from Ochrobactrum anthropi
The deduced 363-amino-acid sequence including a 22-residue leader peptide is in agreement with the enzyme molecular mass and the amino acid sequences of NH2-terminal and internal peptides, and the enzyme is homologous to known nucleosidases from protozoan parasites.
Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity.
An examination of the parameters required for enzymatic activity indicate that the nucleosidase functions over a broad range of pH and temperature, with acidic conditions and temperatures of 37-45 degrees C being optimal.