{PDOC00404}
{PS00462; G_GLU_TRANSPEPTIDASE}
{BEGIN}
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* Gamma-glutamyltranspeptidase signature *
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Gamma-glutamyltranspeptidase (EC 2.3.2.2) (GGT) [1]  catalyzes the transfer of
the gamma-glutamyl moiety  of glutathione to an  acceptor that may be an amino
acid, a peptide  or water (forming glutamate).   GGT  plays a  key role in the
gamma-glutamyl  cycle,  a  pathway  for  the  synthesis   and  degradation  of
glutathione.  In prokaryotes  and eukaryotes, it is an enzyme that consists of
two polypeptide  chains,  a heavy and a light subunit, processed from a single
chain precursor.  The  active  site of GGT is known to be located in the light
subunit.

The sequences  of  mammalian  and  bacterial  GGT  show a number of regions of
high similarity  [2].  Pseudomonas  cephalosporin  acylases  (EC 3.5.1.-) that
convert 7-beta-(4-carboxybutanamido)-cephalosporanic   acid   (GL-7ACA)   into
7-aminocephalosporanic acid (7ACA) and  glutaric acid are evolutionary related
to GGT and also show some GGT activity [3].  Like GGT, these GL-7ACA acylases,
are also composed of two subunits.

One of  the  conserved  regions  correspond to the N-terminal extremity of the
mature light chains of these enzymes. We have used this region  as a signature
pattern.

-Consensus pattern: T-[STA]-H-x-[ST]-[LIVMA]-x(4)-G-[SN]-x-V-[STA]-x-T-x-T-
                    [LIVM]-[NE]-x(1,2)-[FY]-G
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 1997 / Pattern and text revised.

[ 1] Tate S.S., Meister A.
     "Gamma-glutamyl transpeptidase from kidney."
     Methods Enzymol. 113:400-419(1985).
     PubMed=2868390
[ 2] Suzuki H., Kumagai H., Echigo T., Tochikura T.
     "DNA sequence of the Escherichia coli K-12
     gamma-glutamyltranspeptidase gene, ggt."
     J. Bacteriol. 171:5169-5172(1989).
     PubMed=2570061
[ 3] Ishiye M., Niwa M.
     "Nucleotide sequence and expression in Escherichia coli of the
     cephalosporin acylase gene of a Pseudomonas strain."
     Biochim. Biophys. Acta 1132:233-239(1992).
     PubMed=1358202

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