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3.4.19.13: glutathione gamma-glutamate hydrolase

This is an abbreviated version!
For detailed information about glutathione gamma-glutamate hydrolase, go to the full flat file.

Word Map on EC 3.4.19.13

Reaction

a glutathione-S-conjugate
+
H2O
=
an (L-cysteinylglycine)-S-conjugate
 +
L-glutamate

Synonyms

At4g29210, BaGGT42, BaGGT469, BlGGT13, BsGGT168, gamma-glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gamma-GT, GGT, GGT-1, GGT1, GGT3, GGT4, GGT5, hp1118, More

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.13 glutathione gamma-glutamate hydrolase

Engineering

Engineering on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAY385-E398
no autocatalytic processing, no catalytic activity
DELTAY385-I387
mutant is able to autoprocess itself, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows increase in catalytic efficiency
DELTAY385-I396
mutant is able to autoprocess itself, albeit slowly, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows decrease in catalytic efficiency
DELTAY385-K394
mutant is able to autoprocess itself, albeit slowly, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows decrease in catalytic efficiency
DELTAY385-P391
mutant is able to autoprocess itself, albeit slowly, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows decrease in catalytic efficiency
DELTAY385-V388
mutant is able to autoprocess itself, leading to the formation of a small and a large subunit with masses of about 41 kDa and 22 kDa, respectively. Mutant shows increase in catalytic efficiency
T391A
T398A
mutation results in an enzyme that is fully capable of autoprocessing but is devoid of enzymatic activity
T398S
retains considerable enzymatic activity, but hydrolysis rates are reduced about 5fold relative to wild-type enzyme and overall catalyticefficiency is diminished by nearly an order of magnitude
V272A
natural variant of the human enzyme