PMID- 10358060
OWN - NLM
STAT- MEDLINE
DCOM- 19990706
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 24
DP  - 1999 Jun 11
TI  - Methionine adenosyltransferase S-nitrosylation is regulated by the basic and
      acidic amino acids surrounding the target thiol.
PG  - 17075-9
AB  - S-Adenosylmethionine serves as the methyl donor for many biological methylation
      reactions and provides the propylamine group for the synthesis of polyamines.
      S-Adenosylmethionine is synthesized from methionine and ATP by the enzyme
      methionine adenosyltransferase. The cellular factors regulating
      S-adenosylmethionine synthesis have not been well defined. Here we show that in
      rat hepatocytes S-nitrosoglutathione monoethyl ester, a cell-permeable nitric
      oxide donor, markedly reduces cellular S-adenosylmethionine content via
      inactivation of methionine adenosyltransferase by S-nitrosylation. Removal of the
      nitric oxide donor from the incubation medium leads to the denitrosylation and
      reactivation of methionine adenosyltransferase and to the rapid recovery of
      cellular S-adenosylmethionine levels. Nitric oxide inactivates methionine
      adenosyltransferase via S-nitrosylation of cysteine 121. Replacement of the
      acidic (aspartate 355) or basic (arginine 357 and arginine 363) amino acids
      located in the vicinity of cysteine 121 by serine leads to a marked reduction in 
      the ability of nitric oxide to S-nitrosylate and inactivate hepatic methionine
      adenosyltransferase. These results indicate that protein S-nitrosylation is
      regulated by the basic and acidic amino acids surrounding the target cysteine.
FAU - Perez-Mato, I
AU  - Perez-Mato I
AD  - Division of Hepatology and Gene Therapy, Department of Medicine, University of
      Navarra, 31008 Pamplona, Spain.
FAU - Castro, C
AU  - Castro C
FAU - Ruiz, F A
AU  - Ruiz FA
FAU - Corrales, F J
AU  - Corrales FJ
FAU - Mato, J M
AU  - Mato JM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Amino Acids)
RN  - 0 (Nitroso Compounds)
RN  - 0 (Sulfhydryl Compounds)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - 57564-91-7 (S-Nitrosoglutathione)
RN  - 7LP2MPO46S (S-Adenosylmethionine)
RN  - AE28F7PNPL (Methionine)
RN  - EC 2.5.1.6 (Methionine Adenosyltransferase)
RN  - GAN16C9B8O (Glutathione)
SB  - IM
MH  - Amino Acids/chemistry
MH  - Animals
MH  - Catalytic Domain/genetics
MH  - Gene Expression Regulation, Enzymologic
MH  - Glutathione/*analogs & derivatives/metabolism
MH  - Liver/cytology/*enzymology
MH  - Methionine/metabolism
MH  - Methionine Adenosyltransferase/genetics/*metabolism
MH  - Models, Chemical
MH  - Models, Molecular
MH  - Mutagenesis, Site-Directed
MH  - Nitric Oxide/metabolism
MH  - Nitroso Compounds/*metabolism
MH  - Rats
MH  - Rats, Wistar
MH  - S-Adenosylmethionine/metabolism
MH  - S-Nitrosoglutathione
MH  - Sulfhydryl Compounds
EDAT- 1999/06/08 00:00
MHDA- 1999/06/08 00:01
CRDT- 1999/06/08 00:00
PHST- 1999/06/08 00:00 [pubmed]
PHST- 1999/06/08 00:01 [medline]
PHST- 1999/06/08 00:00 [entrez]
AID - 10.1074/jbc.274.24.17075 [doi]
AID - S0021-9258(19)72881-6 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Jun 11;274(24):17075-9. doi: 10.1074/jbc.274.24.17075.