From transglutaminases (TGs) to arylamine N-acetyltransferases (NATs): Insight into the role of a spatially conserved aromatic amino acid position in the active site of these two families of enzymes-Reference-Cited by-同舟云学术

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From transglutaminases (TGs) to arylamine N-acetyltransferases (NATs): Insight into the role of a spatially conserved aromatic amino acid position in the active site of these two families of enzymes

Published:2020-04 Issue:2 Volume:525 Page:308-312
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Xu Ximing,Zhang Wenchao,Berthelet Jérémy,Liu Rongxing,Michail Christina,Chaffotte Alain F.,Dupret Jean-Marie,Rodrigues-Lima Fernando

Funder

Centre National de la Recherche Scientifique

Université Paris Diderot

China Scholarship Council

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference32 articles.

1. Structural aspects of transglutaminase 2: functional, structural, and regulatory diversity;Lee;Apoptosis : Int. J. Program. Cell Death,2017

2. Conserved tryptophan in the core domain of transglutaminase is essential for catalytic activity;Murthy;Proc. Natl. Acad. Sci. U.S.A.,2002

3. Transglutaminases in monocytes and macrophages;Sun;Med. Sci.,2018

4. Evolutionary specialization of a tryptophan indole group for transition-state stabilization by eukaryotic transglutaminases;Iismaa;Proc. Natl. Acad. Sci. U.S.A.,2003

5. Molecular genetics and function of NAT1 and NAT2: role in aromatic amine metabolism and carcinogenesis;Hein;Mutat. Res.,2002

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