[NMR paper] Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Nucleic Acids Res. 2013 Aug 27;
Authors: Barabás O, Németh V, Bodor A, Perczel A, Rosta E, Kele Z, Zagyva I, Szabadka Z, Grolmusz VI, Wilmanns M, Vértessy BG
Abstract
Enzymatic synthesis...
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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[NMR paper] The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic
The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis.
Related Articles The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis.
Biochemistry. 2004 Apr 13;43(14):4082-91
Authors: Azurmendi HF, Wang SC, Massiah MA, Poelarends GJ, Whitman CP, Mildvan AS
trans-3-Chloroacrylic acid dehalogenase (CaaD) converts trans-3-chloroacrylic acid to malonate semialdehyde by the...
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[NMR paper] NMR observation of substrate in the binding site of an active sugar-H+ symport protei
NMR observation of substrate in the binding site of an active sugar-H+ symport protein in native membranes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR observation of substrate in the binding site of an active sugar-H+ symport protein in native membranes.
Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3877-81
Authors: Spooner PJ, Rutherford NG, Watts A, Henderson PJ
NMR methods have been adopted to observe directly the characteristics of substrate...
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[NMR paper] NMR observation of substrate in the binding site of an active sugar-H+ symport protei
NMR observation of substrate in the binding site of an active sugar-H+ symport protein in native membranes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR observation of substrate in the binding site of an active sugar-H+ symport protein in native membranes.
Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3877-81
Authors: Spooner PJ, Rutherford NG, Watts A, Henderson PJ
NMR methods have been adopted to observe directly the characteristics of substrate...
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08-22-2010 03:33 AM
[NMR paper] Involvement of various amino- and carboxyl-terminal residues in the active site of th
Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins.
Related Articles Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with...
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[NMR paper] The roles of Glu-327 and His-446 in the bisphosphatase reaction of rat liver 6-phosph
The roles of Glu-327 and His-446 in the bisphosphatase reaction of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase probed by NMR spectroscopic and mutational analyses of the enzyme in the transient phosphohistidine intermediate complex.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The roles of Glu-327 and His-446 in the bisphosphatase reaction of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase probed by NMR spectroscopic and mutational analyses of the enzyme in the transient phosphohistidine...
Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
Linear Mode
