about
The Crystal Structures of the Open and Catalytically Competent Closed Conformation of Escherichia coli Glycogen SynthaseStructure of formaldehyde dehydrogenase fromPseudomonas aeruginosa: the binary complex with the cofactor NAD+Structural investigations on orotate phosphoribosyltransferase from Mycobacterium tuberculosis, a key enzyme of the de novo pyrimidine biosynthesis.Glutathione synthesis and turnover in the human erythrocyte: alignment of a model based on detailed enzyme kinetics with experimental data.Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides.Time-resolved mass spectrometry for monitoring millisecond time-scale solution-phase processes.Relating structure to mechanism in creatine kinase.Mechanism based inhibition of hydroxysteroid dehydrogenases.Uridine phosphorylase from Trypanosoma cruzi: kinetic and chemical mechanisms.Magnetic resonance studies of enzyme-substrate complexes with paramagnetic probes as illustrated by creatine kinase.Extracting enzyme processivity from kinetic assays.Purification and enzymic properties of Mot1 ATPase, a regulator of basal transcription in the yeast Saccharomyces cerevisiae.Biochemical analysis of the role of G118R-linked dolutegravir drug resistance substitutions in HIV-1 integrase.Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase.Kinetic and stability properties of Penicillium chrysogenum ATP sulfurylase missing the C-terminal regulatory domain.Synthesis of glycoproteins in brain: identification, purification and properties of a synaptosomal sialyl transferase utilizing endogenous and exogenous acceptors.Kinetic involvement of acetaldehyde substrate inhibition on the rate equation of yeast aldehyde dehydrogenase.A steady-state kinetic analysis of the prolyl-4-hydroxylase mechanism.Kinetic features of cotransport mechanisms under isotope exchange conditions.Role of flexibility in the specificity, control and evolutiion of enzymes.Mathematical Model for Small Size Time Series Data of Bacterial Secondary Metabolic Pathways.Elimination of substances from the brain parenchyma: efflux via perivascular pathways and via the blood-brain barrier
P2860
Q27653948-2D1D620B-0EE6-4799-9A5C-762924FCB7FDQ27679828-004EAF34-43DD-4888-81E8-CDE79FD65E4CQ30850632-CB383611-8B3C-4F55-98F3-E70F8CEE7DE5Q33586003-ECCAE4A7-EC85-400C-8192-755E7A05293BQ34050556-F511951C-0E86-4A6F-9B4E-FF93A08A543FQ34277795-EEFDA4CC-2DE7-4005-9319-D32CD92541BFQ36086062-8A79BE22-DB69-48AF-8533-FFCB97719D16Q36476346-57E9F34B-1594-4C65-BB1D-C7B992B92996Q38942581-B98BDC2D-E078-40B2-9A12-3D9FA9302E7DQ39892198-8D9AA128-21A3-4396-95FB-4DB728E4364EQ40208295-A4FD5AA4-E47C-4811-A603-ECDE3129926FQ41745903-7DE5162B-E2FB-4F35-AA04-81EFDD1661F8Q42265700-DAE7C1A6-0E5D-4B2F-82B3-C0C59FD53EDFQ43560031-08C60168-63FA-4A63-9183-9EC5E208D053Q44653228-528CB000-A8D3-4ACF-ACCE-80DD219ECD5EQ48667982-02972C5C-4714-4044-A62B-0A7D4E51FCF4Q51330529-2773C3B3-D307-47AA-9A57-D5BA8D8DC1E1Q52435741-8EBAA324-6682-4A6F-8587-7EB830B18FD7Q52747960-6CA0C247-E7E3-40DA-91E3-FA012A88249EQ52858350-FC4A6D84-FBFF-4C99-A071-C23BF58EC76CQ54966067-1BDD48EC-4144-430F-AA2E-62518A6EEDC7Q57810063-4361FD48-3770-4E84-8A60-F424901B8838
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1967
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Enzyme kinetics.
@en
Enzyme kinetics.
@nl
type
label
Enzyme kinetics.
@en
Enzyme kinetics.
@nl
prefLabel
Enzyme kinetics.
@en
Enzyme kinetics.
@nl
P1476
Enzyme kinetics.
@en
P2093
Cleland WW
P304
P356
10.1146/ANNUREV.BI.36.070167.000453
P577
1967-01-01T00:00:00Z