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The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction
Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization of high-energy states along the reaction coordinate is the crux of the catalytic power ofExpand
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In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis.
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor (Dol-PP-GlcNAc(2)Man(9)Glc(3)), which is assembled by the series of membrane-boundExpand
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Analysis of the substrate specificity loop of the HAD superfamily cap domain.
The haloacid dehalogenase (HAD) superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All members possessExpand
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The Phosphonopyruvate Decarboxylase from Bacteroides fragilis*
The Bacteroides fragilis capsular polysaccharide complex is the major virulence factor for abscess formation in human hosts. Polysaccharide B of this complex contains a 2-aminoethylphosphonateExpand
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X-ray Crystallographic and Site-directed Mutagenesis Analysis of the Mechanism of Schiff-base Formation in Phosphonoacetaldehyde Hydrolase Catalysis*
Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolytic P–C bond cleavage of phosphonoacetaldehyde (Pald) to form orthophosphate and acetaldehyde. The reaction proceeds via aExpand
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Long-Range Inhibitor-Induced Conformational Regulation of Human IRE1α Endoribonuclease Activity
Activation of the inositol-requiring enzyme-1 alpha (IRE1α) protein caused by endoplasmic reticulum stress results in the homodimerization of the N-terminal endoplasmic reticulum luminal domains,Expand
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The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily.
Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor. The reaction proceeds via a novel bicovalentExpand
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Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis.
Phosphoglucomutases catalyze the interconversion of D-glucose 1-phosphate and D-glucose 6-phosphate, a reaction central to energy metabolism in all cells and to the synthesis of cell wallExpand
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Catalytic cycling in beta-phosphoglucomutase: a kinetic and structural analysis.
Lactococcus lactis beta-phosphoglucomutase (beta-PGM) catalyzes the interconversion of beta-d-glucose 1-phosphate (beta-G1P) and beta-d-glucose 6-phosphate (G6P), forming beta-d-glucoseExpand
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C-terminal region of USP7/HAUSP is critical for deubiquitination activity and contains a second mdm2/p53 binding site.
  • J. Ma, J. Martin, +8 authors Z. Lai
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 15 November 2010
USP7, also known as the hepes simplex virus associated ubiquitin-specific protease (HAUSP), deubiquitinates both mdm2 and p53, and plays an important role in regulating the level and activity of p53.Expand
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