The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions
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Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug designStructural basis for the insensitivity of a serine enzyme (palmitoyl-protein thioesterase) to phenylmethylsulfonyl fluorideVariation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulationsIdentification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papainConsequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bondSubstrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bondingDes-, syn- and anti-oxyimino-delta 3-cephalosporins. Intrinsic reactivity and reaction with RTEM-2 serine beta-lactamase and D-alanyl-D-alanine-cleaving serine and Zn2+-containing peptidasesInactivation of delta 5-3-oxo steroid isomerase with active-site-directed acetylenic steroidsDiffusion-Controlled Reactions of EnzymesProbing the active site of Tritrichomonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase using covalent modification of cysteine residues.Looking at the proteases from a simple perspective.Evidence that binding to the s2-subsite of papain may be coupled with catalytically relevant structural change involving the cysteine-25-histidine-159 diad. Kinetics of the reaction of papain with a two-protonic-state reactivity probe containing a hReactivities of neutral and cationic forms of 2,2'-dipyridyl disulphide towards thiolate anions. Detection of differences between the active centres of actinidin, papain and ficin by a three-protonic-state reactivity probe.Kinetics of protein modification reactions.Inactivation of the rabbit parotid Na/K/Cl cotransporter by N-ethylmaleimide.Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion.Isomerization of the uncomplexed actinidin molecule: kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation.Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sitComputer simulations of the kinetics of irreversible enzyme inhibition by an unstable inhibitor.Appendix: Analysis of pH-dependent kinetics in up to four reactive hydronic states.Modification of human placental alkaline phosphatase by periodate-oxidized 1,N6-ethenoadenosine monophosphateDifferences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe stuEvidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin.Dependence of the P2-S2 stereochemical selectivity of papain on the nature of the catalytic-site chemistry. Quantification of selectivity in the catalysed hydrolysis of the enantiomeric N-acetylphenylalanylglycine 4-nitroanilides.Experimental approach to the kinetic study of unstable site-directed irreversible inhibitors: kinetic origin of the apparent positive co-operativity arising from inactivation of trypsin by p-amidinophenylmethanesulphonyl fluoride.Kinetic analysis of regeneration by dilution of a covalently modified protein.Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics.Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probSome classical errors in the kinetic analysis of enzyme reactionsFluorescence labelling of NADPH-cytochrome P-450 reductase with the monobromomethyl derivative of syn-9,10-dioxabimane.Delta 2- and delta 3-cephalosporins, penicillinate and 6-unsubstituted penems. Intrinsic reactivity and interaction with beta-lactamases and D-alanyl-D-alanine-cleaving serine peptidases.Evidence for association-activation effects in reactions of papain from studies on its reactivity towards isomeric two-protonic-state reactivity probes.Evidence that the lack of high catalytic activity of thiolsubtilisin towards specific substrates may be due to an inappropriately located proton-distribution system. Demonstration of highly nucleophilic character of the thiol group of thiolsubtilisiMethylphenidate analogs with behavioral differences interact differently with arginine residues on the dopamine transporter in rat striatum.Affinity labelling of tryptophanyl-tRNA synthetase with mesitoyl-AMP
P2860
Q24616801-FC672656-76E0-4778-B69E-8B80B2C9486EQ27622463-A05E29BE-96AF-422E-B40C-F3A6AACF177DQ28343571-6AC0E0A1-2E98-4108-B15B-C2B1724F86C1Q28357343-98CB8F42-05BB-4146-B853-D785A4B7DB5FQ28359830-903CBD96-2698-49FA-8891-C9DD84DB9A6DQ28361928-2BF35E3D-3A1D-4651-8783-ED240193C11FQ28366914-C3544F5F-D8E7-4A7F-8826-D79F2E7EDB25Q28366964-33A9E326-E2A0-455E-AA5E-7FDE4E21632AQ30052649-766EC624-8285-452A-A30D-70383BD9C854Q30424912-A64D05B9-3A23-48C0-BD9E-784A1E1AC593Q37848282-13BBAF3C-E8C6-4408-A49A-B44425A7E127Q39296088-3B3ADAFA-C581-4B54-8C16-8954754399A1Q39296096-DE10B71B-E1CF-4F2D-9600-3D9F60FDEC5DQ40169910-9E5E6658-932C-40F6-BAC9-C8993C52176FQ41282749-A86F078C-C0A5-4EA1-9F08-47635DFAC107Q41767232-E4D5E29C-AA88-4AB5-8F31-3EB288EF2B34Q41825451-37A23185-EA99-4B4A-8CA0-8DFE4F2D5AFDQ41881996-B54B894B-913C-4E05-ADD6-C4A0C5386FA7Q41906645-D91F49FA-7364-4605-A98D-98F4AD14678AQ41962323-EC477B8A-BF0A-4771-9E5C-1C470797004BQ41968422-70EE6A4E-6DF5-4DA0-B42B-C4C9CA6020B5Q41990162-B69FC8BF-AF88-4F9B-AF81-BFF0C5AD7185Q42000549-97D7BF6B-C72F-424A-B1C8-B4452B51A4CAQ42031211-BC3E00C8-5A40-4FD1-A177-51DA7061091FQ42744661-4B352E08-9B7F-4BE8-BDE8-E0967D93BB95Q42794460-3EBB4D58-E4F7-4F3D-A8BD-C5127CFE7F3BQ42795151-4A612D31-81CC-4DC3-A3D7-B13F778CF6BDQ42796852-6E00CE5E-9E7B-47B4-A1EA-FB319CC7D43CQ42813164-FDB93135-4A45-4E23-A687-8EF6383480EAQ42865493-EA619689-1E67-4066-B277-97BFD5C0CB75Q42874670-C72E6D05-1754-4A79-A852-D49E91A439F3Q42880136-B522A7D5-9C73-403A-A334-463F9A633D72Q42883037-5A425D1F-67B1-47C9-829C-7F363F3109AFQ46536075-290F34EA-CCD7-4F6F-8279-25361E473BFAQ57417494-0F31D5EC-1126-4B1D-AFAA-C6932AA6E01C
P2860
The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions
description
1979 nî lūn-bûn
@nan
1979年の論文
@ja
1979年論文
@yue
1979年論文
@zh-hant
1979年論文
@zh-hk
1979年論文
@zh-mo
1979年論文
@zh-tw
1979年论文
@wuu
1979年论文
@zh
1979年论文
@zh-cn
name
The equilibrium assumption is ...... protein-modification reactions
@en
The equilibrium assumption is ...... protein-modification reactions
@nl
type
label
The equilibrium assumption is ...... protein-modification reactions
@en
The equilibrium assumption is ...... protein-modification reactions
@nl
prefLabel
The equilibrium assumption is ...... protein-modification reactions
@en
The equilibrium assumption is ...... protein-modification reactions
@nl
P2860
P356
P1433
P1476
The equilibrium assumption is ...... protein-modification reactions
@en
P2093
Brocklehurst K
P2860
P304
P356
10.1042/BJ1810775
P407
P577
1979-09-01T00:00:00Z