Structural highlights
Function
ENTP4_HUMAN Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP.
Publication Abstract from PubMed
The ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are a family of enzymes found on the cell surface and in the lumen of certain organelles that are major regulators of purinergic signaling. Their intracellular roles, however, have not been clearly defined. NTPDase4 (UDPase, ENTPD4) is a Golgi protein potentially involved in nucleotide recycling as part of protein glycosylation, and is also found in lysosomes, where its purpose is unknown. To further our understanding of NTPDase4 function, we determined its crystal structure. The enzyme adopts a wide open, inactive conformation. Differences in the nucleotide-binding site relative to its homologs could account for its substrate selectivity. The putative membrane-interacting loop of cell-surface NTPDases is drastically altered in NTPDase4, potentially affecting its inter-domain dynamics at the Golgi membrane. This article is protected by copyright. All rights reserved.
Crystal structure of the nucleotide-metabolizing enzyme NTPDase4.,Gorelik A, Labriola JM, Illes K, Nagar B Protein Sci. 2020 Aug 6. doi: 10.1002/pro.3926. PMID:32767432[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gorelik A, Labriola JM, Illes K, Nagar B. Crystal structure of the nucleotide-metabolizing enzyme NTPDase4. Protein Sci. 2020 Aug 6. doi: 10.1002/pro.3926. PMID:32767432 doi:http://dx.doi.org/10.1002/pro.3926
