Zobrazeno 1 - 6
of 6
pro vyhledávání: '"R N, Thorneley"'
Autor:
J N, Rodríguez-López, L G, Fenoll, P A, García-Ruiz, R, Varón, J, Tudela, R N, Thorneley, F, García-Cánovas
Publikováno v:
Biochemistry. 39(34)
The reaction of mushroom (Agaricus bisporus) tyrosinase with dioxygen in the presence of several o-diphenolic substrates has been studied by steady-state and transient-phase kinetics in order to elucidate the rate-limiting step and to provide new ins
Autor:
J N, Rodriguez-Lopez, J, Hernández-Ruiz, F, Garcia-Cánovas, R N, Thorneley, M, Acosta, M B, Arnao
Publikováno v:
The Journal of biological chemistry. 272(9)
The kinetics of the catalytic cycle and irreversible inactivation of horseradish peroxidase C (HRP-C) reacting with m-chloroperoxybenzoic acid (mCPBA) have been studied by conventional and stopped-flow spectrophotometry. mCPBA oxidized HRP-C to compo
Publikováno v:
The Journal of biological chemistry. 271(8)
The observed pseudo-first order rate constant for the reaction between a horseradish peroxidase (HRP) variant (R38L)HRPC* and hydrogen peroxide saturates at high peroxide concentrations (Km = 11. 8 mm). The data are consistent with a two-step mechani
Autor:
S, Bornemann, M K, Ramjee, S, Balasubramanian, C, Abell, J R, Coggins, D J, Lowe, R N, Thorneley
Publikováno v:
The Journal of biological chemistry. 270(39)
Chorismate synthase catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate to chorismate. It is the seventh enzyme of the shikimate pathway, which is responsible for the biosynthesis of aromatic metabolites from glucose. The chorismate syntha
Publikováno v:
The Journal of biological chemistry. 265(22)
A synthetic gene encoding horseradish peroxidase isoenzyme C (HRP C) has been synthesized and expressed in Escherichia coli. The nonglycosylated recombinant enzyme (HRP C*) was produced in inclusion bodies in an insoluble inactive form containing onl
Publikováno v:
Biochimica et biophysica acta. 403(2)
1. Sedimentation velocity analyses of mixtures of highly purified component proteins of Azotobacter chroococcum are consistent with the formation of a tight 1 : 1 complex in the absence of Na2 S2 O4. 1 : 1 complex formation between complementary prot