Catalysis by enzyme conformational change as illustrated by orotidine 5'-monophosphate decarboxylase.
about
Formation and stability of a vinyl carbanion at the active site of orotidine 5'-monophosphate decarboxylase: pKa of the C-6 proton of enzyme-bound UMPComputer aided enzyme design and catalytic conceptsTesting Geometrical Discrimination within an Enzyme Active Site: Constrained Hydrogen Bonding in the Ketosteroid Isomerase Oxyanion HoleMechanism of the Orotidine 5′-Monophosphate Decarboxylase-Catalyzed Reaction: Evidence for Substrate Destabilization ,Atomic Resolution Structure of the Orotidine 5'-Monophosphate Decarboxylase Product Complex Combined with Surface Plasmon Resonance Analysis: IMPLICATIONS FOR THE CATALYTIC MECHANISMSubstrate Distortion Contributes to the Catalysis of Orotidine 5′-Monophosphate DecarboxylaseProton transfer from C-6 of uridine 5'-monophosphate catalyzed by orotidine 5'-monophosphate decarboxylase: formation and stability of a vinyl carbanion intermediate and the effect of a 5-fluoro substituentMechanism of OMP decarboxylation in orotidine 5'-monophosphate decarboxylase.Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.Kinetic isotope effects of L-Dopa decarboxylase.OMP decarboxylase: phosphodianion binding energy is used to stabilize a vinyl carbanion intermediate.Mechanisms and free energies of enzymatic reactions.Orotidine 5'-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions.Computation of kinetic isotope effects for enzymatic reactions.Quantum mechanical/molecular mechanical simulation study of the mechanism of hairpin ribozyme catalysisMolecular dynamics simulations of biotin carboxylase.Molecular dynamics simulations of the intramolecular proton transfer and carbanion stabilization in the pyridoxal 5'-phosphate dependent enzymes L-dopa decarboxylase and alanine racemase.Development and application of ab initio QM/MM methods for mechanistic simulation of reactions in solution and in enzymes.On unjustifiably misrepresenting the EVB approach while simultaneously adopting itCritical role of substrate conformational change in the proton transfer process catalyzed by 4-oxalocrotonate tautomerase.Enzyme architecture: the activating oxydianion binding domain for orotidine 5'-monophophate decarboxylase.Specificity in transition state binding: the Pauling model revisited.Probing protein multidimensional conformational fluctuations by single-molecule multiparameter photon stamping spectroscopy.Enzyme Architecture: Erection of Active Orotidine 5'-Monophosphate Decarboxylase by Substrate-Induced Conformational Changes.Glycosyltransfer in mutants of putative catalytic residue Glu303 of the human ABO(H) A and B blood group glycosyltransferases GTA and GTB proceeds through a labile active site.Quantum mechanics/molecular mechanics minimum free-energy path for accurate reaction energetics in solution and enzymes: sequential sampling and optimization on the potential of mean force surface.
P2860
Q24643971-A701E5FF-77BA-49FB-B9B3-D44B45EE31A4Q26866557-E80005F4-9655-4B7B-BAB7-3115AB32269DQ27652268-E04F98DD-FC35-43A1-A48D-69CEEB795445Q27655450-14A27147-63A3-4F60-A668-E3ACE9FB3A34Q27676270-559F9F41-25FC-4C25-8157-AF4266AC655AQ27680432-28A8AF9E-244A-4084-80C0-AC28FED0CF77Q28728056-C5E5CE04-8F12-4D20-9D21-699E37AFBEF1Q30539734-E7272050-C758-4171-B9BD-27E0F9699321Q33998251-D588B98F-5014-4C0F-B931-B788C7D8AD58Q34764634-0D7A2F9E-8B2F-4EDB-9A7A-4D9CAED29128Q34996638-F90A47B7-898A-4DCB-9262-FED901F7D5C0Q35768462-1B211A3D-5D3F-47BA-92F5-C0ED8C7F7E0AQ36201065-F2CC35E5-2ADC-4985-B699-693E71E38388Q37112024-45B7798C-33C3-4F7B-B559-066390621438Q37127249-BB238A7F-AEA1-4E6A-9DDD-584F84F46091Q37127253-6FBE6551-1ABB-42C5-AA76-F7AD2E609391Q37191277-E7F68141-57D7-447B-A4EE-0A3867DB3A6DQ37238383-D75C001E-B3E9-4C9C-B6BA-87CFAA9CB53DQ37329360-F634EF02-FD83-4CBE-802B-593BA5AE6912Q37353149-B01F307F-B534-4FB9-A036-183F23B134BAQ37503752-9B2F6CC0-FD11-4B4C-9409-5E9B33865B9DQ38074690-2913FC2E-A41E-4FCD-BB04-4C32E0F781E8Q41772321-2560F2FC-B735-4192-9CC0-528B0EDA5581Q48145721-984B929F-5A2C-4162-A5EE-5CA43670324EQ52677329-54E49118-0958-43CA-A304-C00A9DD1DC9BQ53551886-A755B1B8-712A-48DD-9FA8-3D51313EF970
P2860
Catalysis by enzyme conformational change as illustrated by orotidine 5'-monophosphate decarboxylase.
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Catalysis by enzyme conformati ...... '-monophosphate decarboxylase.
@ast
Catalysis by enzyme conformati ...... '-monophosphate decarboxylase.
@en
type
label
Catalysis by enzyme conformati ...... '-monophosphate decarboxylase.
@ast
Catalysis by enzyme conformati ...... '-monophosphate decarboxylase.
@en
prefLabel
Catalysis by enzyme conformati ...... '-monophosphate decarboxylase.
@ast
Catalysis by enzyme conformati ...... '-monophosphate decarboxylase.
@en
P1476
Catalysis by enzyme conformati ...... '-monophosphate decarboxylase.
@en
P2093
P304
P356
10.1016/S0959-440X(03)00041-1
P577
2003-04-01T00:00:00Z