4inc

Publication Abstract from PubMed

The histidine triad proteins (HITs) constitute a large and ubiquitous superfamily of nucleotide hydrolases. The human nucleotide binding proteins (hHints) are a distinct class of HITs noted for their acyl-AMP hydrolase and phosphoramidase activity. The first high resolution crystal structures of human Hint2 with and without bound adenosine monophosphate (AMP) are here described. The differences between hHint2 and previously known HIT-family protein structures are discussed. HIT-family enzymes have historically been divided into five classes based on their catalytic specificity: Hint, Fhit, GalT, DcpS, and Aprataxin. However, although several structures exist for enzymes in these classes, the endogenous substrates of many of these enzymes have not been identified or biochemically characterized. In order to better understand the structural relationship of the HIT enzymes, a structure-based phylogeny has been constructed that has resulted in the identification of several new putative HIT clades with potential acyl-AMP hydrolase and phosphoramidase activity. This article is protected by copyright. All rights reserved.

Structural characterization of human histidine triad nucleotide binding protein 2 (hHint2), a member of the histidine triad (HIT) superfamily.,Maize KM, Wagner CR, Finzel BC FEBS J. 2013 May 10. doi: 10.1111/febs.12330. PMID:23659632^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.