EC Number |
General Information |
Reference |
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3.5.1.1 | evolution |
the enzyme is a member of an increasing rhizobial-type family of L-asparaginases |
720213 |
3.5.1.1 | metabolism |
L-asparaginase is degraded by leukemic lysosomal cysteine proteases |
714599 |
3.5.1.1 | more |
a divergent sequence between the two enzymes forms a variable loop at the C-terminal of the alpha subunit, the asparaginase variable loop plays a role in the determination of substrate preference in plants. The variable loop itself spans positions 169-182 of ASPGA1 and 168-194 of ASPGB1, dynamic simulations and comparative protein structure modeling based on the crystal structure of Lupinus luteus LlA, PDB accession number 2GEZ, overview |
720793 |
3.5.1.1 | more |
ASNase3 is not the enzyme responsible for the antitumor effects of guinea pig serum |
731313 |
3.5.1.1 | more |
increased substrate accessibility through the active site loop plays a major role in determining activity, dynamic flipping of a critical Tyr residue is responsible for the activity of thermophilic L-asparaginases, molecular dynamic simulation and reaction mechanism, overview. Structure-function analysis of active site residues T53 and K274 |
719439 |
3.5.1.1 | physiological function |
amino acid starvation by asparaginase enhances phosphorylation of eukaryotic initiation factor 2, eIF2 by general control nonderepressible 2 kinase GCN2, leading to reduced global mRNA translation rates. GCN2+/+ and GCN2-/-2 mice are injected once daily with asparaginase or saline for up to 7 d. In both thymus and spleen, activation of amino acid stress response genes to asparaginase, such as asparagine synthetase and CAAT enhancer binding protein homologous protein, requires GCN2. Asparaginase reduces food intake and body weight in both genotypes, but spleen and thymus wet weights and total cell numbers in thymus, spleen, bone marrow, and mesenteric lymph nodes are less in GCN2-/- mice treated with asparaginase. In the thymus, GCN2-/- mice treated with asparaginase demonstrate enhanced apoptosis and fewer cells in all subpopulations examined compared with GCN2+/+ mice treated with asparaginase. In the spleen, GCN2 deletion magnifies asparaginase-induced reductions in CD4+ T cells, CD8+ T cells, CD19+ B cells, and CD11b+ leukocytes |
716000 |
3.5.1.1 | physiological function |
antiproliferative effect of YpA in vitro and in vivo, overview |
-, 720973 |
3.5.1.1 | physiological function |
comparison of native L-asparaginases from Aspergillus strains |
-, 752344 |
3.5.1.1 | physiological function |
Helicobacter pylori L-asparaginase is able to inhibit the cell-cycle of fibroblasts and gastric cell lines. Interference with cell-cycle in vitro depends on cell genotype and is related to the expression levels of the concurrent enzyme asparagine synthetase |
716681 |
3.5.1.1 | physiological function |
the cytotoxic activity of L-asparaginase from Yersinia pseudotuberculosis and Erwinia carotovora are investigated and compared in vitro using human T-lymphoblastic leukemia (Jurkat and Molt-4 cells) and also solid tumor cell lines MCF-7 (human breast adenocarcinoma), LnCap (human prostate carcinoma), NGUK1 (ratGasser node neurinoma). The data obtained indicate that the Yersinia pseudotuberculosis L-asparaginase significantly inhibits growth of leukemic and solid tumor cells. Comparing effectiveness of L-asparaginases from various sources one can see that L-asparaginase from Yersinia pseudotuberculosis exhibits higher activity in suppression of tumor cell growth than the enzyme from Erwinia carotovora |
711172 |