Human gamma-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro.

  title={Human gamma-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro.},
  author={R. Yao and E. Schneider and T. Ryan and J. Galivan},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={93 19},
  • R. Yao, E. Schneider, +1 author J. Galivan
  • Published 1996
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
A cDNA encoding human gamma-glutamyl hydrolase has been identified by searching an expressed sequence tag data base and using rat gamma-glutamyl hydrolase cDNA as the query sequence. The cDNA encodes a 318-amino acid protein of Mr 35,960. The deduced amino acid sequence of human gamma-glutamyl hydrolase shows 67% identity to that of rat gamma-glutamyl hydrolase. In both rat and human the 24 amino acids preceding the N terminus constitute a structural motif that is analogous to a leader or… Expand
Characterization of human cellular gamma-glutamyl hydrolase.
Results indicate that the identified cDNA encodes the intracellular gamma-glutamyl hydrolase found in a variety of human tumor cells and that the baculovirus-expressed enzyme is a suitable model for further structural and enzymatic studies. Expand
Cloning of mouse gamma-glutamyl hydrolase in the form of two cDNA variants with different 5' ends and encoding alternate leader peptide sequences.
Cl cloning of this mouse lysosomal cDNA enzyme from liver GH mRNA in the form of two cDNA variants differing 14-fold (Variant I versus Variant II) in relative frequency that exhibited 5'-end heterogeneity and encoded alternate leader peptides is described. Expand
Characterization of Human Cellular g-Glutamyl Hydrolase
A previously identified cDNA encoding a human g-glutamyl hydrolase was expressed in a baculovirus system. The expressed protein had molecular mass of 37 kDa. Treatment of the protein with PNGase FExpand
Structural organization of the human gamma-glutamyl hydrolase gene.
The complete organization and structure of the human GH gene was determined and studies of cDNA from different human tissue sources provided evidence that there is a single spliced cDNA species in human. Expand
Characterization of Human gamma-glutamyl hydrolase in solution demonstrates that the enzyme is a non-dissociating homodimer.
HGH has now been characterized using analytical ultracentrifugation and dynamic light scattering and the conservation of hGH monomer-monomer interface sequences in other mammalian and plant gamma-glutamyl hydrolase molecules suggests that they also exist as stable homodimers. Expand
Recombinant Zebrafish γ-Glutamyl Hydrolase Exhibits Properties and Catalytic Activities Comparable with Those of Mammalian Enzyme
This recombinant zγGH is active and exhibits comparable endopeptidase activity with folate substrate and antifolate drug methotrexate and significantly increased efficiency in folylpolyglutamate hydrolysis for folate analysis compared with current protocols. Expand
Organization and structure of the mouse gamma-glutamyl hydrolase gene and the functional identification of its promoter.
The organization and structure of the murine GH gene encoding gamma-glutamyl hydrolase were determined and a relatively GC-rich region of the genome 5' of exon 1 was distinctly promoter-like and encoded a number of putative cis-acting elements, including six Sp1 sites known to be involved in the regulation of transcription but no TATA sequence motif. Expand
gamma-Glutamyl hydrolase from human sarcoma HT-1080 cells: characterization and inhibition by glutamine antagonists.
Using the human HT-1080 sarcoma line, the secretion of GGH activity into media during culture and an acidic pH optimum for in vitro catalytic activity of the enzyme are observed, consistent with a lysosomal location for the enzyme. Expand
Three-dimensional Structure of Human γ-Glutamyl Hydrolase
The crystal structure of human γ-glutamyl hydrolase, determined at 1.6-Å resolution, reveals that the protein is a homodimer and two sequence motifs are found in common, which include the catalytically essential residues, Cys-110 and His-220. Expand
Folylpoly-gamma-glutamate carboxypeptidase from pig jejunum. Molecular characterization and relation to glutamate carboxypeptidase II.
P pig folylpoly-gamma-carboxypeptidase, rat N-acetylated alpha-linked acidic dipeptidases, and human prostate-specific membrane antigen appear to represent varied expressions of the same gene in different species and tissues. Expand