about
Impaired Acid Catalysis by Mutation of a Protein Loop Hinge Residue in a YopH Mutant Revealed by Crystal StructuresConservative tryptophan mutants of the protein tyrosine phosphatase YopH exhibit impaired WPD-loop function and crystallize with divanadate esters in their active sitesProbing potential medium effects on phosphate ester bonds using 18O isotope shifts on 31P NMR.Transition state differences in hydrolysis reactions of alkyl versus aryl phosphate monoester monoanions.Enzymatic mechanisms of phosphate and sulfate transfer.Mechanistic study of protein phosphatase-1 (PP1), a catalytically promiscuous enzymeNew functional aspects of the atypical protein tyrosine phosphatase VHZ.Mechanism and transition state structure of aryl methylphosphonate esters doubly coordinated to a dinuclear cobalt(III) center.Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis.Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases.Structural and Kinetic Properties of the Aldehyde Dehydrogenase NahF, a Broad Substrate Specificity Enzyme for Aldehyde Oxidation.Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases.The divalent metal ion in the active site of uteroferrin modulates substrate binding and catalysisMechanistic studies of protein tyrosine phosphatases YopH and Cdc25A with m-nitrobenzyl phosphate.A comparison of phosphonothioic acids with phosphonic acids as phosphatase inhibitors.The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: a computational and isotope effect study.Probing the origin of the compromised catalysis of E. coli alkaline phosphatase in its promiscuous sulfatase reaction.Metavanadate at the active site of the phosphatase VHZChemistry and mechanism of phosphatases, diesterases and triesterases.The effects of sulfur substitution for the nucleophile and bridging oxygen atoms in reactions of hydroxyalkyl phosphate esters.Altered transition state for the reaction of an RNA model catalyzed by a dinuclear zinc(II) catalyst.Thermodynamic origin of the increased rate of hydrolysis of phosphate and phosphorothioate esters in DMSO/water mixtures.NMR data do not implicate a phosphorane in the T4 DNA ligase reaction.Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase.Isotope effects and medium effects on sulfuryl transfer reactions.The catalytic mechanism of Cdc25A phosphatase.An altered mechanism of hydrolysis for a metal-complexed phosphate diester.Metal ion catalyzed hydrolysis of ethyl p-nitrophenyl phosphate.Comparisons of phosphorothioate with phosphate transfer reactions for a monoester, diester, and triester: isotope effect studies.Role of protein conformational mobility in enzyme catalysis: acylation of alpha-chymotrypsin by specific peptide substrates.Probing the transition-state structure of dual-specificity protein phosphatases using a physiological substrate mimic.Altered mechanisms of reactions of phosphate esters bridging a dinuclear metal center.A mechanistic study of the alkaline hydrolysis of diaryl sulfate diesters.A concerted mechanism for the transfer of the thiophosphinoyl group from aryl dimethylphosphinothioate esters to oxyanionic nucleophiles in aqueous solution.Examination of P-OR bridging bond orders in phosphate monoesters using (18)O isotope shifts in 31P NMR.The thermodynamics of phosphate versus phosphorothioate ester hydrolysis.Transition States and Control of Substrate Preference in the Promiscuous Phosphatase PP1.Comparison of the reaction progress of calcineurin with Mn2+ and Mg2+.Isotope effect studies on the calcineurin phosphoryl-transfer reaction: transition state structure and effect of calmodulin and Mn2+.Mechanistic Aspects of Phosphate Diester Cleavage Assisted by Imidazole. A Template Reaction for Obtaining Aryl Phosphoimidazoles.
P50
Q27653412-34D9C045-56EF-41E3-A208-F7AE409F6BBFQ28829658-D2B11386-C463-460C-A3AA-E4001865042CQ31009921-BAE3115A-488F-447C-9A88-9B21A380AA52Q33194110-08E8947E-3E3A-4807-A8ED-5BE01CA18F1BQ36559640-DB7129B2-BA0B-4CB6-9595-3D9F06A44A5FQ37066048-1C262D36-9E42-4EA1-9E18-77F98C677D2FQ37377130-203C1018-A417-44C2-BDB6-F4419C47F7E5Q37410994-301D09FC-18C1-4D91-A2B0-736D90878769Q38373982-CDF8C159-BA46-4923-A360-6BC2CB2EEE66Q38404139-3B665D86-5DCC-4837-9F2C-7D58FEC3F27BQ38825944-A638CF43-FD01-449A-8C90-CF28EFFDB6A5Q41394107-FF5C2BA7-7F3D-4388-AB71-C578F75A5C87Q41459135-AD4AB710-899A-4446-9F4E-905F1CBF4D2EQ41462245-645816B4-C29A-42A4-8AF0-42991FDF360CQ41466001-2E01C63E-8434-473A-BAEB-BEFF2C1E55BDQ41475729-DF88F6BE-1CD0-43D0-A19D-782A0FCEB267Q41834608-0D8131CC-C15F-489C-B6FD-B2F99529DD4CQ41898134-A992FAED-91E1-4237-B4DC-F3C2B4B7B8CCQ42076938-2278E201-3ADE-40F4-86DC-05510D7497C9Q42081384-18B2243D-D195-4837-8996-7B6FAF724619Q42199277-CDD305A8-BAA4-47E1-A5FF-6EA6507720D8Q42406949-DF75A161-7934-4126-8CF1-F97A93A34C50Q43241776-3BB70552-9FC2-4861-B861-8C6339803B99Q43563708-6716498C-32C4-4208-A621-FD263F5FE4DFQ43741176-B7F7C92E-0095-4318-8B30-673BF4A24C83Q43862884-461B7BC3-8009-424F-AC0E-F8ECC0679FFCQ44244371-0E93A895-E575-43BE-AB25-96AE346493C6Q44284959-B1E6EAF6-407F-4926-9A5D-CEC965E3831BQ44481774-D99EDDE9-3A6A-42E5-8456-3866497C941FQ44733828-55E3050F-9212-4B1B-BC2D-E3CFDB4D66E5Q44965726-9A10D583-0E56-43C3-8402-B8903C4659A1Q45070605-912A6AC7-DE85-4909-9810-6C0377388E42Q45194663-89F53181-CD71-4E64-90A5-BB4BE81B13AEQ46447958-40C26F5F-75AC-4603-8480-0536E9186490Q46524552-AF669EF7-BA5A-4133-A5D3-88DE5171C1F3Q46739374-70E7DAAC-0DC8-49ED-A782-79196D2A5DBAQ48174982-9210488A-21A9-4C54-A646-C98B296B3574Q51091458-7E1B2CB5-ED4D-4A15-BFCA-63B1227D4AE3Q51101320-02E0DDF5-409F-49CA-BE3D-97F407F53B85Q52860550-0109CB1E-18E7-41AF-9247-26DB1770E08C
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Alvan C Hengge
@ast
Alvan C Hengge
@en
Alvan C Hengge
@es
Alvan C Hengge
@nl
type
label
Alvan C Hengge
@ast
Alvan C Hengge
@en
Alvan C Hengge
@es
Alvan C Hengge
@nl
prefLabel
Alvan C Hengge
@ast
Alvan C Hengge
@en
Alvan C Hengge
@es
Alvan C Hengge
@nl
P1053
C-8667-2011
P106
P21
P31
P3829
P496
0000-0002-5696-2087
P569
2000-01-01T00:00:00Z