PMID- 32089267
OWN - NLM
STAT- MEDLINE
DCOM- 20201109
LR  - 20201109
IS  - 1090-2104 (Electronic)
IS  - 0006-291X (Linking)
VI  - 525
IP  - 2
DP  - 2020 Apr 30
TI  - 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.
PG  - 308-312
LID - S0006-291X(20)30356-9 [pii]
LID - 10.1016/j.bbrc.2020.02.082 [doi]
AB  - Transglutaminases (TG) and arylamine N-acetyltransferases (NAT) are important 
      family of enzymes. Although they catalyze different reactions and have distinct 
      structures, these two families of enzymes share a spatially conserved catalytic 
      triad (Cys, His, Asp residues). In active TGs, a conserved Trp residue located 
      close to the triad cysteine is crucial for catalysis through stabilization of 
      transition states. Here, we show that in addition to sharing a similar catalytic 
      triad with TGs, functional NAT enzymes also possess in their active site an 
      aromatic residue (Phe, Tyr or Trp) occupying a structural position similar to the 
      Trp residue of active TGs. More importantly, as observed in active TGs, our data 
      indicates that in functional NAT enzymes this conserved aromatic residue is also 
      involved in stabilization of transition states. These results thus indicate that 
      in addition to the three triad residues, these two families of enzymes also share 
      a spatially conserved aromatic amino acid position important for catalysis. 
      Identification of residues involved in the stabilization of transition states is 
      important to develop potent inhibitors. Interestingly, NAT enzymes have been 
      shown as potential targets of clinical interest.
CI  - Copyright (c) 2020 Elsevier Inc. All rights reserved.
FAU - Xu, Ximing
AU  - Xu X
AD  - Universite de Paris, BFA, UMR 8251, CNRS, 75013, Paris, France; Key Laboratory of 
      Marine Drugs, Chinese Ministry of Education, School of Medicine and Pharmacy, 
      Ocean University of China, Qingdao, 266003, China.
FAU - Zhang, Wenchao
AU  - Zhang W
AD  - Universite de Paris, BFA, UMR 8251, CNRS, 75013, Paris, France.
FAU - Berthelet, Jeremy
AU  - Berthelet J
AD  - Universite de Paris, BFA, UMR 8251, CNRS, 75013, Paris, France.
FAU - Liu, Rongxing
AU  - Liu R
AD  - Universite de Paris, BFA, UMR 8251, CNRS, 75013, Paris, France.
FAU - Michail, Christina
AU  - Michail C
AD  - Universite de Paris, BFA, UMR 8251, CNRS, 75013, Paris, France.
FAU - Chaffotte, Alain F
AU  - Chaffotte AF
AD  - Institut Pasteur, Unite de Resonance Magnetique Nucleaire des Biomolecules, 
      75015, Paris, France.
FAU - Dupret, Jean-Marie
AU  - Dupret JM
AD  - Universite de Paris, BFA, UMR 8251, CNRS, 75013, Paris, France.
FAU - Rodrigues-Lima, Fernando
AU  - Rodrigues-Lima F
AD  - Universite de Paris, BFA, UMR 8251, CNRS, 75013, Paris, France. Electronic 
      address: fernando.rodrigues-lima@u-paris.fr.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20200220
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Amino Acids, Aromatic)
RN  - EC 2.3.1.5 (Arylamine N-Acetyltransferase)
RN  - EC 2.3.2.13 (Transglutaminases)
SB  - IM
MH  - *Amino Acid Sequence
MH  - Amino Acids, Aromatic
MH  - Animals
MH  - Arylamine N-Acetyltransferase/*chemistry
MH  - Biocatalysis
MH  - Catalytic Domain
MH  - *Conserved Sequence
MH  - Humans
MH  - Transglutaminases/*chemistry/genetics
OTO - NOTNLM
OT  - Active site
OT  - Arylamine N-Acetyltransferases
OT  - Catalytic mechanism
OT  - Transglutaminases
OT  - Transition state
COIS- Declaration of competing interest The authors declare that they have no conflict 
      of interest.
EDAT- 2020/02/25 06:00
MHDA- 2020/11/11 06:00
CRDT- 2020/02/25 06:00
PHST- 2020/02/10 00:00 [received]
PHST- 2020/02/12 00:00 [accepted]
PHST- 2020/02/25 06:00 [pubmed]
PHST- 2020/11/11 06:00 [medline]
PHST- 2020/02/25 06:00 [entrez]
AID - S0006-291X(20)30356-9 [pii]
AID - 10.1016/j.bbrc.2020.02.082 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2020 Apr 30;525(2):308-312. doi: 
      10.1016/j.bbrc.2020.02.082. Epub 2020 Feb 20.