PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease

Peptidylarginine deiminase (PAD, EC 3.5.3.15) enzymes catalyze the conversion of protein‐bound arginine to citrulline. This post‐translational modification may have a big impact on the structure and function of the target protein. In this review, we will discuss the effects of citrullination and its...

Full description

Saved in:
Bibliographic Details
Published in:BioEssays 2003-11, Vol.25 (11), p.1106-1118
Main Authors: Vossenaar, Erik R., Zendman, Albert J.W., van Venrooij, Walther J., Pruijn, Ger J.M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Arthritis, Rheumatoid - enzymology
Humans
Hydrolases - classification
Hydrolases - genetics
Hydrolases - metabolism
Isoenzymes - classification
Isoenzymes - genetics
Isoenzymes - metabolism
Molecular Sequence Data
Multigene Family
Multiple Sclerosis - enzymology
Phylogeny
Protein Conformation
Protein-Arginine Deiminases
Psoriasis - enzymology
Sequence Alignment
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Peptidylarginine deiminase (PAD, EC 3.5.3.15) enzymes catalyze the conversion of protein‐bound arginine to citrulline. This post‐translational modification may have a big impact on the structure and function of the target protein. In this review, we will discuss the effects of citrullination and its involvement in several human diseases, including rheumatoid arthritis and multiple sclerosis. So far, four isotypes of PAD have been described in mammals. We describe the existence of PAD in non‐mammalian vertebrates and the existence of a fifth mammalian PAD. In addition, tissue‐specific expression, genomic organization and evolutionary conservation of the different PAD isotypes will be discussed in detail. This article contains supplementary material which may be viewed at the BioEssays website at http://www.interscience.wiley.com/jpages/0265‐9247/suppmat/2003/25/v25.1106.html. BioEssays 25:1106–1118, 2003. © 2003 Wiley Periodicals, Inc.
ISSN:0265-9247
1521-1878
DOI:10.1002/bies.10357