Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad.
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Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzymeThe human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activityAnalysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissueCrystal Structure of Acivicin-Inhibited γ-Glutamyltranspeptidase Reveals Critical Roles for Its C-Terminus in Autoprocessing and Catalysis † ‡Crystal Structure of Bacillus anthracis Transpeptidase Enzyme CapDCrystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocketAutoproteolytic Activation of ThnT Results in Structural Reorganization Necessary for Substrate Binding and CatalysisEvidence for conserved function of γ-glutamyltranspeptidase in Helicobacter genusRole of Campylobacter jejuni gamma-glutamyl transpeptidase on epithelial cell apoptosis and lymphocyte proliferation.γ-Glutamyl transpeptidase is a heavily N-glycosylated heterodimer in HepG2 cellsA hydrolytic γ-glutamyl transpeptidase from thermo-acidophilic archaeon Picrophilus torridus: binding pocket mutagenesis and transpeptidation.Functional genomics of novel secondary metabolites from diverse cyanobacteria using untargeted metabolomics.Unfolding analysis of the mature and unprocessed forms of Bacillus licheniformis γ-glutamyltranspeptidaseHuman γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.Emerging regulatory paradigms in glutathione metabolism.Heterogeneous nucleation helps the search for initial crystallization conditions of γ-glutamyl transpeptidase from Bacillus licheniformis.Experimental evidence for the involvement of amino acid residue Glu398 in the autocatalytic processing of Bacillus licheniformis γ-glutamyltranspeptidaseBiochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathwayA novel, species-specific class of uncompetitive inhibitors of gamma-glutamyl transpeptidase.γ-Glutamyltranspeptidases: sequence, structure, biochemical properties, and biotechnological applications.High Resolution X-ray Diffraction Dataset for Bacillus licheniformis Gamma Glutamyl Transpeptidase-acivicin complex: SUMO-Tag Renders High Expression and Solubility.Gastric epithelial cell death caused by Helicobacter suis and Helicobacter pylori γ-glutamyl transpeptidase is mainly glutathione degradation-dependent.Structure of Bacillus subtilis γ-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue"Phylogenetic and evolutionary analysis of functional divergence among Gamma glutamyl transpeptidase (GGT) subfamilies"Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: comparison of molecular and structural properties with mesophilic counterparts.Garlic γ-glutamyl transpeptidases that catalyze deglutamylation of biosynthetic intermediate of alliin.Histoplasma capsulatum secreted gamma-glutamyltransferase reduces iron by generating an efficient ferric reductant.Effect of pH on the hydrolytic kinetics of gamma-glutamyl transferase from Bacillus subtilis.
P2860
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P2860
Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad.
description
2006 nî lūn-bûn
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2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
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2006年學術文章
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name
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@ast
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@en
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@nl
type
label
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@ast
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@en
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@nl
prefLabel
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@ast
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@en
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@nl
P2093
P2860
P356
P1476
Autoprocessing of Helicobacter ...... nine-threonine catalytic dyad.
@en
P2093
Aaron Sand
Gina Boanca
Hidehiko Kumagai
Hideyuki Suzuki
Joseph J Barycki
Keiichi Fukuyama
Toshihiro Okada
P2860
P304
P356
10.1074/JBC.M607694200
P407
P577
2006-11-15T00:00:00Z