EC Number   |
General Information |
Reference |
|---|
    2.3.2.2 | evolution |
Bacillus licheniformis gamma-glutamyltranspeptidase (BlGGT) belongs to N-terminal nucleophile hydrolase superfamily in which all inclusive members are synthetized as single-chain precursors, and then self-processed to form mature enzymes |
-, 756966 |
| 2.3.2.2 | evolution |
gamma-glutamyl transpeptidase enzyme (GGT) is a member of the N-terminal nucleophile hydrolase superfamily |
-, 754222 |
| 2.3.2.2 | 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 |
| 2.3.2.2 | evolution |
the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases |
-, 757270 |
| 2.3.2.2 | malfunction |
deletion of the ggtA (AN10444) encoding a putative gammaGT decreased the gammaGT activities below to the detection limit suggesting that GgtA is the only enzyme possessing significant gammaGT activity under carbon stressed conditions in Aspergillus nidulans |
-, 754814 |
| 2.3.2.2 | malfunction |
gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo |
-, 757270 |
| 2.3.2.2 | malfunction |
human GGT protein without the N-terminal anchor domain is expressed as a soluble enzyme and it exhibits virtually identical enzymatic character to that of wild-type human GGT with the anchor domain |
752957 |
| 2.3.2.2 | more |
active site structures of human GGT, overview |
756188 |
| 2.3.2.2 | more |
catalytic mechanism of human GGT, catalytic Thr381 within the active site, acts as a nucleophile and attacks the delta-carbon of the glutamate moiety, leading to the formation of a tetrahedral intermediate (gamma-glutamyl enzyme complex), stabilized by two conserved glycines (Gly473 and Gly474 in hGGT), overview |
757548 |
| 2.3.2.2 | more |
comparisons of the active site structures of GGT enzyme from Pseudomonas nitroreducens with those from Escherichia coli and Homo sapiens, overview. The residues around the donor substrate-binding site of PnGGT (Arg94, Asn384, Glu403, Asp406, Ser435, Ser436, Gly456, and Gly456) are conserved among the other GGTs. In the active site of PnGGT, Phe417 in the 411-421 loop and Trp385 form the side wall of the postulated acceptor-binding pocket |
-, 756223 |
