about
Exploring the role of the active site cysteine in human muscle creatine kinaseGetting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMTThe 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complexMolecular recognition of sub-micromolar inhibitors by the epinephrine-synthesizing enzyme phenylethanolamine N-methyltransferaseMolecular recognition of physiological substrate noradrenaline by the adrenaline-synthesizing enzyme PNMT and factors influencing its methyltransferase activityFragment-based screening by X-ray crystallography, MS and isothermal titration calorimetry to identify PNMT (phenylethanolamine N-methyltransferase) inhibitorsPerturbation of the Monomer–Monomer Interfaces of the Benzoylformate Decarboxylase TetramerA bulky hydrophobic residue is not required to maintain the V-conformation of enzyme-bound thiamin diphosphateExtended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligationThe kinetic characterization and X-ray structure of a putative benzoylformate decarboxylase from M. smegmatis highlights the difficulties in the functional annotation of ThDP-dependent enzymesCharacterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae.Identification of initiation sites for T4 lysozyme folding using CD and NMR spectroscopy of peptide fragments.Phenylethanolamine N-methyltransferase inhibition: re-evaluation of kinetic data.Inhibitors of phenylethanolamine N-methyltransferase that are predicted to penetrate the blood-brain barrier: design, synthesis, and evaluation of 3-fluoromethyl-7-(N-substituted aminosulfonyl)-1,2,3,4-tetrahydroisoquinolines that possess low affiniIsolation and characterization of a benzoylformate decarboxylase and a NAD+/NADP+-dependent benzaldehyde dehydrogenase involved in D-phenylglycine metabolism in Pseudomonas stutzeri ST-201.Using directed evolution to probe the substrate specificity of mandelamide hydrolase.Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633.Saturation mutagenesis of putative catalytic residues of benzoylformate decarboxylase provides a challenge to the accepted mechanismKinetic and pH studies on human phenylethanolamine N-methyltransferase.The reaction mechanism of phenylethanolamine N-methyltransferase: a density functional theory study.Substrate specificity in thiamin diphosphate-dependent decarboxylases.Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes.Identification of charge transfer transitions related to thiamin-bound intermediates on enzymes provides a plethora of signatures useful in mechanistic studies.Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity.Phosphonodifluoropyruvate is a mechanism-based inhibitor of phosphonopyruvate decarboxylase from Bacteroides fragilis.Time-dependent inactivation of human phenylethanolamine N-methyltransferase by 7-isothiocyanatotetrahydroisoquinolineSpecific inhibitors of Plasmodium falciparum thioredoxin reductase as potential antimalarial agents.Phenylethanolamine N-methyltransferase kinetics: bovine versus recombinant human enzyme.Expression of Torpedo californica creatine kinase in Escherichia coli and purification from inclusion bodies.Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase signature family.Isoleucine 69 and valine 325 form a specificity pocket in human muscle creatine kinase.Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida.Physical, kinetic and spectrophotometric studies of a NAD(P)-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633.Loop movement and catalysis in creatine kinase.Chemical modification of PABA synthase.Heterogeneity of Escherichia coli-expressed human muscle creatine kinase.Determinants of substrate specificity in KdcA, a thiamin diphosphate-dependent decarboxylase.Specificity and mechanism of mandelamide hydrolase catalysis.Pharmacokinetics of thiopental and pentobarbital enantiomers after intravenous administration of racemic thiopental.Determination of (R)-(+)- and (S)-(-)-isomers of thiopentone in plasma by chiral high-performance liquid chromatography.
P50
Q24642138-33D99346-007F-45E4-A5F2-D4029AB9B0DEQ27635284-4BF90D62-080D-476B-817B-82576BC751BCQ27639974-622AE69C-385A-4A7F-A1FC-0CA2AA703198Q27642855-C583C1B3-36AE-4F87-871E-C746980B77C0Q27656300-C5964083-8FB2-41C8-9A8F-8B2646DBB30CQ27663569-026EED98-6133-45CF-A4F5-41EBAB8DA4EEQ27684437-D258365B-D835-4F6B-A27B-629799FCC1F6Q27684458-DE9513BF-CD59-4C73-8081-81CEC5EA8EB8Q27696160-B1877D28-BDB8-414C-B5D1-FF0B6AD4A5F4Q27700483-732E6300-FD97-4B8F-B8AF-32A77570C1B3Q27935077-9BE9EB6B-2F24-46DC-AF26-B254380713C1Q30595681-455600B9-1CBF-493E-BEF8-427381FFF287Q30945285-3CFDF6A7-7E19-4F7F-8E58-4A6C198082BEQ33206071-B6264BB7-BBE7-42F9-9AE4-09E18500B5E8Q33301603-ED739F08-D7B6-415A-AA54-36BCD3EA6E39Q33392166-43CB5171-3FFA-41C2-A020-12C8CD1D691FQ34891664-628C6984-D28B-4326-9FAD-DF3818128627Q36557922-B6F21FB7-FB3D-4395-9BE9-5C874E3FB334Q37368928-EE04999D-5C68-4FEF-B256-9C0347171B50Q37384529-B31E4AB9-10B8-4540-809B-E92B63916DB5Q37975827-F941D3CF-9DCD-442E-8FD7-CE86942C4A29Q38124949-DBB81664-7950-4D4C-8FD0-488555897FF2Q38739167-16F57915-B032-4395-BFF6-074D71101523Q38963577-1899E90D-4E28-42DB-A25B-41E9B0A0321DQ40141034-9C4BBA34-3800-4E88-B2BE-BA569A1491BBQ41463443-ECAD2CBA-6D8B-422F-80A1-16C2103E8C73Q41945917-AB9C3EE4-647D-4491-9026-B5DFDFE64AB1Q43645269-339E74E0-B84B-4D4A-B0A7-C1D4AC887F04Q44160710-9F56CF68-5E6F-4B2D-B1E8-E1010E3184C1Q44935391-27EFB3B3-01A5-4250-8EE9-809022314EF6Q45123445-2A819E20-1673-47BA-AC52-BE18B82429ADQ46522364-398276B0-EFA2-492F-B00C-FFDFE72DF783Q46579730-4707CCCC-EAC2-49B8-9DBA-D657C3C85D45Q46612700-32C54585-4B45-4EC1-A26C-63329C542C84Q46883207-6823748E-08A4-4097-B0A0-B14C40F677C0Q50478440-AF43A2FF-B6A9-48A8-9646-6B42C64269DFQ51122187-6659E839-01B9-4536-95A8-64C3A1EF6D35Q51165519-1E206F3A-D4ED-47DF-BB4E-67A71F178FAFQ51564204-5E539F28-215C-4A8D-81C3-E7950D694FDFQ51580072-7B7449B3-03FA-4393-BE04-532B2D01FADA
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Michael J McLeish
@es
Michael J McLeish
@nl
Michael J McLeish
@sl
Michael J. McLeish
@en
type
label
Michael J McLeish
@es
Michael J McLeish
@nl
Michael J McLeish
@sl
Michael J. McLeish
@en
prefLabel
Michael J McLeish
@es
Michael J McLeish
@nl
Michael J McLeish
@sl
Michael J. McLeish
@en
P106
P1153
7003298267
P21
P31
P496
0000-0002-9221-9119