-
methionine (SAM), also
known under the
commercial names of SAMe, SAM-e, or
AdoMet, is a
common cosubstrate involved in
methyl group transfers, transsulfuration...
-
regulated by
effectors such as the
ubiquitous cofactor S-adenosyl-L-methionine (
adoMet). This
enzyme belongs to the
family of lyases, to be specific, the hydro-lyases...
-
methylation status of the
target DNA. The
cofactors S-Adenosyl
methionine (
AdoMet),
hydrolyzed adenosine triphosphate (ATP), and
magnesium (Mg2+) ions, are...
- (August 1993). "A new
function of S-adenosylmethionine: the
ribosyl moiety of
AdoMet is the
precursor of the
cyclopentenediol moiety of the tRNA
wobble base...
- S-adenosylmethionine-dependent
methyltransferase (SAM-MTase or
AdoMet-MTase) is a
conserved protein domain and
protein superfamily. SAM-MTase proteins...
-
revealed the
location of the
AdoMet or
AdoHcy cofactor, the SET
domain bears no
similarity at all to the canonical/
AdoMet-dependent
methyltransferase fold...
- S-adenosylmethionine (also
known as
AdoMet, SAM or SAMe) by
reacting methionine (a non-polar
amino acid) and ATP (the
basic currency of energy).
AdoMet is a
methyl donor...
-
using the
prefix "meth-" to
indicate the
presence of a
single carbon.
AdoMet Methylation March,
Jerry (1992).
Advanced organic chemistry: reactions,...
- last
positions of the β2
strand to bind the
AdoMet.
Motif III is also
implicated in the
binding of
Adomet.
Motif IV is
especially important and well known...
-
including DNA, RNA and
protein synthesis. S-adenosylmethionine
decarboxylase (
AdoMetDC)
plays an
essential regulatory role in the
polyamine biosynthetic pathway...
