{PDOC50404}
{PS50404; GST_NTER}
{PS50405; GST_CTER}
{BEGIN}
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* Soluble glutathione S-transferase N- and C-terminal domain profiles *
***********************************************************************

Glutathione S-transferases (GSTs) (EC 2.5.1.18) are involved in detoxification
of  xenobiotic compounds and in the biosynthesis of important metabolites. Two
distinct  superfamilies  of  GST  isoenzymes  exist.  The  larger  superfamily
comprises cytosolic, or soluble, dimeric enzymes that are principally, but not
exclusively,   involved   in   biotransformation   of  toxic  xenobiotics  and
endobiotics.   The  other  superfamily  is  composed  of  microsomal  proteins
primarily  involved  in  arachidonic  acid  metabolism.  The  microsomal GSTs,
grouped  together  as  a  separate  entity,  are  collectively  called  MAPEG,
designating   membrane-associated   proteins  in  eicosanoid  and  glutathione
metabolism (see <PDOC00999>) [1,2,3,4].

Soluble  GSTs  activate  glutathione  (GSH)  to  GS-.  In  many  GSTs, this is
accomplished  by  a  Tyr  at  H-bonding distance from the sulfur of GSH. These
enzymes  catalyze nucleophilic attack by reduced glutathione (GSH) on nonpolar
compounds that contain an electrophilic carbon, nitrogen, or sulphur atom [3].

Soluble  glutathione  S-transferases  are mostly homodimers, with each monomer
folding into two distinct domains, an N-terminal thioredoxin-like domain and a
C-terminal  domain  (see <PDB:1GSS>) [5]. The N-terminal domain participate in
binding  the  glutathione  moiety  via  its  thioredoxin-like domain while the
C-terminal domain contains several hydrophobic alpha-helices that specifically
bind hydrophobic substrates.

To  recognize soluble glutathione S-transferase we developed two profiles, one
that  covers  the  whole  N-terminal  domain  and  one  that  spans the entire
C-terminal domain.

-Sequences known to belong to this class detected by the first profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the second profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2007 / First entry.

[ 1] Mannervik B., Danielson U.H.
     "Glutathione transferases--structure and catalytic activity."
     CRC Crit. Rev. Biochem. 23:283-337(1988).
     PubMed=3069329
[ 2] Coles B., Ketterer B.
     "The role of glutathione and glutathione transferases in chemical
     carcinogenesis."
     Crit. Rev. Biochem. Mol. Biol. 25:47-70(1990).
     PubMed=2182291
[ 3] Mannervik B., Board P.G., Hayes J.D., Listowsky I., Pearson W.R.
     "Nomenclature for mammalian soluble glutathione transferases."
     Methods Enzymol. 401:1-8(2005).
     PubMed=16399376; DOI=10.1016/S0076-6879(05)01001-3
[ 4] Pettersson P.L., Thoren S., Jakobsson P.J.
     "Human microsomal prostaglandin E synthase 1: a member of the MAPEG
     protein superfamily."
     Methods Enzymol. 401:147-161(2005).
     PubMed=16399384; DOI=10.1016/S0076-6879(05)01009-8
[ 5] Le Trong I., Stenkamp R.E., Ibarra C., Atkins W.M., Adman E.T.
     "1.3-A resolution structure of human glutathione S-transferase with
     S-hexyl glutathione bound reveals possible extended ligandin binding
     site."
     Proteins 48:618-627(2002).
     PubMed=12211029; DOI=10.1002/prot.10162

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{END}