A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant
about
Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase IElucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate HydrolysisCrystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding siteCrystal structure and amino acid sequence of Wolinella succinogenes L-asparaginaseRecombinant L-asparaginase 1 from Saccharomyces cerevisiae: an allosteric enzyme with antineoplastic activityEngineering of Helicobacter pylori L-asparaginase: characterization of two functionally distinct groups of mutantsExperimental Data in Support of a Direct Displacement Mechanism for Type I/II L-Asparaginases.The glutaminase activity of L-asparaginase is not required for anticancer activity against ASNS-negative cells.From one amino acid to another: tRNA-dependent amino acid biosynthesisIdentification and structural analysis of an L-asparaginase enzyme from guinea pig with putative tumor cell killing propertiesTrapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine.Asparagine deprivation mediated by Salmonella asparaginase causes suppression of activation-induced T cell metabolic reprogramming.The differential ability of asparagine and glutamine in promoting the closed/active enzyme conformation rationalizes the Wolinella succinogenes L-asparaginase substrate specificityL-Asparaginase as potent anti-leukemic agent and its significance of having reduced glutaminase side activity for better treatment of acute lymphoblastic leukaemia.A novel alpha-glucosidase from the acidophilic archaeon Ferroplasma acidiphilum strain Y with high transglycosylation activity and an unusual catalytic nucleophile.Echinococcus granulosus antigen 5 is closely related to proteases of the trypsin family.Therapeutic l-asparaginase: upstream, downstream and beyond.Identification of functional regions in the Rhodospirillum rubrum L-asparaginase by site-directed mutagenesis.Tackling Critical Catalytic Residues in Helicobacter pylori L-Asparaginase.Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains.Engineering the substrate specificity of Escherichia coli asparaginase. II. Selective reduction of glutaminase activity by amino acid replacements at position 248.Beta-aspartylpeptides as substrates of L-asparaginases from Escherichia coli and Erwinia chrysanthemi.Gln-tRNAGln formation from Glu-tRNAGln requires cooperation of an asparaginase and a Glu-tRNAGln kinase.
P2860
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P2860
A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant
description
1996 nî lūn-bûn
@nan
1996 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@ast
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@en
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@nl
type
label
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@ast
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@en
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@nl
prefLabel
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@ast
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@en
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@nl
P2093
P2860
P3181
P1433
P1476
A covalently bound catalytic i ...... ructure of a Thr-89-Val mutant
@en
P2093
P2860
P3181
P356
10.1016/0014-5793(96)00660-6
P407
P577
1996-07-22T00:00:00Z