EC Number   |
General Information |
Reference |
|---|
   3.4.19.13 | evolution |
phylogenetic analysis of gamma-glutamyltranspeptidase proteins from different organisms divides the gamma-glutamyltranspeptidases into various clades and offers several interesting insights into the evolution and relatedness of these gamma-glutamyltranspeptidases. The present study focuses on the residues that are highly specific to each gamma-glutamyltranspeptidase subfamily and underlines their importance in imparting unique functional properties to the gamma-glutamyltranspeptidase proteins of each clade. The present study highlights the clade specific variation in the GXXGG motif, where SP (XX) of bacterial gamma-glutamyltranspeptidases is substituted by VM, CA, AS in extremophilic bacteria, archaea, and eukaryotes respectively, which could explain the differences in rates of enzyme reaction in gamma-glutamyltranspeptidases of these clades as this motif is known to be involved in gamma-glutamyltranspeptidase-substrate complex intermediate formation and the rate of final product release. Many sites predicted to be contributing to type 2 functional divergence are quite often found lining the substrate binding cavity and are close to the highly conserved known functional residues. This implies that they may be affecting the biochemical environment of the binding cavity and influencing the catalytic residues, thereby contributing to the functional differences among gamma-glutamyltranspeptidase-like proteins of various clades |
-, 752897 |
| 3.4.19.13 | evolution |
the deduced amino acid sequence of Bacillus amyloliquefaciens BaGGT469 is almost identical to that of Bacillus amyloliquefaciens BaGGT42 with the exception of only two amino acid residues (Val349Ile and Ser383Ala) |
-, 757413 |
| 3.4.19.13 | metabolism |
capacity of the enzyme to cleave GSH conjugates of both aromatic and aliphatic diisocyanates, suggesting a potential role in their metabolism |
755662 |
| 3.4.19.13 | metabolism |
in the presence of 1alpha,25-dihydroxyvitamin D3, gamma-glutamyl transpeptidase activity is significantly increased in LLC-PK1 cells, with an increase in enzymic activity also found in the cell medium. While the stimulatory effect of 1-hydroxyvitamin D3 is similar to that of 1alpha,25-dihydroxyvitamin D3, vitamin D3 and 25-hydroxyvitamin D3 have no effect on activity. The increase in activity is due to prolonged turnover |
732523 |
| 3.4.19.13 | metabolism |
primary enzyme of the mercapturic acid pathway |
755662 |
| 3.4.19.13 | metabolism |
the enzyme plays a role in asthma, reperfusion injury, and cancer |
754112 |
| 3.4.19.13 | physiological function |
construction of stably transfected NIH/3T3 mouse fibroblasts that express the enzyme in its proper orientation on the outer surface of the cell. NIH/3T3 fibroblasts require cysteine for growth and are unable to use extracellular glutathione as a source of cysteine. NIH/3T3 fibroblasts expressing the enzyme are able to grow in cysteine-free medium supplemented with glutathione. Cysteine derived from the cleavage of extracellular glutathione can be used to maintain intracellular levels of glutathione, and cells are able to replenish intracellular glutathione when incubated in cysteine-free medium containing glutathione |
721575 |
| 3.4.19.13 | physiological function |
enzyme calatyzes the first step in vacuolar degradation of glutathione conjugates. In Arabidopsis thaliana, degradation of glutathione S-conjugates strictly occurs by the ordered removal of Glu first and Gly second. Hydrolysis of glutathione S-bimane is blocked in enzyme null mutants |
686731 |
| 3.4.19.13 | physiological function |
enzyme catalyzes the obligate initial step in glutathione conjugate metabolism. Enzyme disruption plants grown on soil under normal conditions until they set seed do not display visible differences compared with wild-type plants |
689627 |
| 3.4.19.13 | physiological function |
enzyme gamma-glutamyl transpeptidase and a L-Cys-Gly dipeptidase catalyse the complete hydrolysis of glutathione stored in the central vacuole of the yeast cell, prior to release of its constitutive amino acids L-glutamate, L-cysteine and glycine into the cytoplasm |
487970 |
