Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II
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Thermostable Carbonic Anhydrases in Biotechnological ApplicationsApo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of a Metal in Protein Structure, Stability, and Solvent Network ,Role of Hydrophilic Residues in Proton Transfer during Catalysis by Human Carbonic Anhydrase II † ‡High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug designA Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase IINeutron Structure of Human Carbonic Anhydrase II: Implications for Proton TransferStructural and Kinetic Study of the Extended Active Site for Proton Transfer in Human Carbonic Anhydrase IIComparison of solution and crystal properties of Co(II)–substituted human carbonic anhydrase IIKinetic and crystallographic studies of the role of tyrosine 7 in the active site of human carbonic anhydrase IINeutron Structure of Human Carbonic Anhydrase II: A Hydrogen-Bonded Water Network “Switch” Is Observed between pH 7.8 and 10.0Structure and catalysis by carbonic anhydrase II: Role of active-site tryptophan 5Water Networks in Fast Proton Transfer during Catalysis by Human Carbonic Anhydrase IIStructural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bondStructural, catalytic and stabilizing consequences of aromatic cluster variants in human carbonic anhydrase IIKinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase IIThe Structure of Carbonic Anhydrase IX Is Adapted for Low-pH CatalysisStructural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestrationJoint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer.Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.Proton transport in carbonic anhydrase: Insights from molecular simulation.Transport activity of the sodium bicarbonate cotransporter NBCe1 is enhanced by different isoforms of carbonic anhydraseEnzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.Intramolecular proton shuttle supports not only catalytic but also noncatalytic function of carbonic anhydrase II.Catalysis and pH control by membrane-associated carbonic anhydrase IX in MDA-MB-231 breast cancer cellsRole of Trp19 and Tyr200 in catalysis by the γ-class carbonic anhydrase from Methanosarcina thermophila.Effects of cryoprotectants on the structure and thermostability of the human carbonic anhydrase II-acetazolamide complexTracking solvent and protein movement during CO2 release in carbonic anhydrase II crystals.Origins of enhanced proton transport in the Y7F mutant of human carbonic anhydrase II.Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Preliminary joint neutron and X-ray crystallographic study of human carbonic anhydrase II.Carbonic anhydrase immobilized on hollow fiber membranes using glutaraldehyde activated chitosan for artificial lung applications.Effect of active-site mutation at Asn67 on the proton transfer mechanism of human carbonic anhydrase II.Elucidation of the proton transport mechanism in human carbonic anhydrase II.Sequestration of carbon dioxide by the hydrophobic pocket of the carbonic anhydrases.Carbonic anhydrases and their biotechnological applications.Membrane inlet for mass spectrometric measurement of catalysis by enzymatic decarboxylases.Human carbonic anhydrase II-cyanate inhibitor complex: putting the debate to rest.Structural and kinetic effects on changes in the CO(2) binding pocket of human carbonic anhydrase II.Proton transfer in catalysis and the role of proton shuttles in carbonic anhydrase.Active-site solvent replenishment observed during human carbonic anhydrase II catalysis.
P2860
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P2860
Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II
description
2007 nî lūn-bûn
@nan
2007 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մարտին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Speeding up proton transfer in ...... of human carbonic anhydrase II
@ast
Speeding up proton transfer in ...... of human carbonic anhydrase II
@en
Speeding up proton transfer in ...... of human carbonic anhydrase II
@nl
type
label
Speeding up proton transfer in ...... of human carbonic anhydrase II
@ast
Speeding up proton transfer in ...... of human carbonic anhydrase II
@en
Speeding up proton transfer in ...... of human carbonic anhydrase II
@nl
prefLabel
Speeding up proton transfer in ...... of human carbonic anhydrase II
@ast
Speeding up proton transfer in ...... of human carbonic anhydrase II
@en
Speeding up proton transfer in ...... of human carbonic anhydrase II
@nl
P2093
P50
P356
P1433
P1476
Speeding up proton transfer in ...... of human carbonic anhydrase II
@en
P2093
Chingkuang Tu
David N Silverman
Deepa Bhatt
S Zoë Fisher
P304
P356
10.1021/BI602620K
P407
P577
2007-03-27T00:00:00Z