Active-site serine phosphate and histidine residues of phosphoglucomutase: pH titration studies monitored by proton and phosphorus-31 NMR spectroscopy

Biochemistry ◽  
1985 ◽  
Vol 24 (18) ◽  
pp. 4746-4753 ◽  
Author(s):  
Gyung Ihm Rhyu ◽  
William J. Ray ◽  
John L. Markley
Keyword(s):  
Nmr Spectroscopy ◽  
Active Site ◽  
Ph Titration ◽  
Histidine Residues ◽  
Serine Phosphate

scholarly journals Alkylation and Identification of the Histidine Residues at the Active Site of Ribonuclease

1963 ◽  
Vol 238 (7) ◽  
pp. 2413-2420 ◽  
Author(s):  
Arthur M. Crestfield ◽  
William H. Stein ◽  
Stanford Moore
Keyword(s):  
Active Site ◽  
Histidine Residues

scholarly journals Properties and Conformation of the Histidine Residues at the Active Site of Ribonuclease

1963 ◽  
Vol 238 (7) ◽  
pp. 2421-2428 ◽  
Author(s):  
Arthur M. Crestfield ◽  
William H. Stein ◽  
Stanford Moore
Keyword(s):  
Active Site ◽  
Histidine Residues

Structure and activity of phosphoglycerate mutase

1981 ◽  
Vol 293 (1063) ◽  
pp. 121-130 ◽  
Keyword(s):  
Active Site ◽  
Transfer Reaction ◽  
Chemical Kinetic ◽  
Phosphoglycerate Mutase ◽  
Phosphoryl Transfer ◽  
X Ray ◽  
Histidine Residues ◽  
Ping Pong ◽  
Available Information ◽  
Structure And Activity

The structure of yeast phosphoglycerate mutase determined by X-ray crystallographic and amino acid sequence studies has been interpreted in terms of the chemical, kinetic and mechanistic observations made on this enzyme. There are two histidine residues at the active site, with imidazole groups almost parallel to each other and approximately 0.4 nm apart, positioned close to the 2 and 3 positions of the substrate. The simplest interpretation of the available information suggests that a ping-pong type mechanism operates in which at least one of these histidine residues participates in the phosphoryl transfer reaction. The flexible C-terminal region also plays an important role in the enzymic reaction.

scholarly journals Kinetic Study of CO2 Hydration by Small-Molecule Catalysts with A Second Coordination Sphere that Mimic the Effect of the Thr-199 Residue of Carbonic Anhydrase

Biomimetics ◽  
2019 ◽  
Vol 4 (4) ◽  
pp. 66
Author(s):  
Park ◽  
Lee
Keyword(s):  
Hydrogen Bonding ◽  
Carbonic Anhydrase ◽  
Coordination Sphere ◽  
Active Site ◽  
Hydration Reaction ◽  
Ph Titration ◽  
Hydration Rate ◽  
Pka Value ◽  
Secondary Coordination Sphere ◽  
Hydrogen Bonding Network

Zinc complexes were synthesized as catalysts that mimic the ability of carbonic anhydrase (CA) for the CO2 hydration reaction (H2O + CO2 → H+ + HCO3-). For these complexes, a tris(2-pyridylmethyl)amine (TPA) ligand mimicking only the active site, and a 6-((bis(pyridin-2-ylmethyl)amino)methyl)pyridin-2-ol (TPA-OH) ligand mimicking the hydrogen-bonding network of the secondary coordination sphere of CA were used. Potentiometric pH titration was used to determine the deprotonation ability of the Zn complexes, and their pKa values were found to be 8.0 and 6.8, respectively. Stopped-flow spectrophotometry was used to confirm the CO2 hydration rate. The rate constants were measured to be 648.4 and 730.6 M-1s-1, respectively. The low pKa value was attributed to the hydrogen-bonding network of the secondary coordination sphere of the catalyst that mimics the behavior of CA, and this was found to increase the CO2 hydration rate of the catalyst.

scholarly journals Investigation of human erythrocyte superoxide dismutase by 1H nuclear-magnetic-resonance spectroscopy

1980 ◽  
Vol 185 (1) ◽  
pp. 245-252 ◽  
Author(s):  
H A O Hill ◽  
W K Lee ◽  
J V Bannister ◽  
W H Bannister
Keyword(s):  
Superoxide Dismutase ◽  
Active Site ◽  
Human Erythrocyte ◽  
Superoxide Dismutases ◽  
Resonance Spectroscopy ◽  
Structural Homology ◽  
Histidine Residues ◽  
Erythrocyte Superoxide Dismutase ◽  
1H Nuclear Magnetic Resonance ◽  
Acetyl Group

The 170MHZ 1 H n.m.r. spectra of the Cu(II)/Zn(II), Cu(I)/Zn(II) and apo- forms of human erythrocyte superoxide dismutase (EC 1.15.1.1) are reported. Resonances are assigned to the C-2 and C-4 protons of histidine residues in the active site, and it is suggested that five or six histidine residues serve as ligands to the metal ions in each subunit of the enzyme. The remaining assigned resonances are associated with histidine-41, N-terminal N-acetyl group, histidine- 108 and cysteine- 109. A comparison of the n.m.r. spectra of human and bovine superoxide dismutases suggests significant structural homology.

51V Solid-State Magic Angle Spinning NMR Spectroscopy and DFT Studies of Oxovanadium(V) Complexes Mimicking the Active Site of Vanadium Haloperoxidases

2003 ◽  
Vol 42 (4) ◽  
pp. 1256-1266 ◽  
Author(s):  
Neela Pooransingh ◽  
Ekaterina Pomerantseva ◽  
Martin Ebel ◽  
Sven Jantzen ◽  
Dieter Rehder ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Active Site ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Dft Studies ◽  
Angle Spinning

Solution-State17O Quadrupole Central-Transition NMR Spectroscopy in the Active Site of Tryptophan Synthase

2015 ◽  
Vol 128 (4) ◽  
pp. 1372-1376 ◽  
Author(s):  
Robert P. Young ◽  
Bethany G. Caulkins ◽  
Dan Borchardt ◽  
Daryl N. Bulloch ◽  
Cynthia K. Larive ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Active Site ◽  
Tryptophan Synthase ◽  
Central Transition
Sign in / Sign up

Export Citation Format

Share Document