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Publikováno v:
The Journal of Biological Chemistry, 288(33), 23751-23764. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Leroux, A E, Haanstra, J R, Bakker, B M & Krauth-Siegel, R L 2013, ' Dissecting the catalytic mechanism of Trypanosoma brucei trypanothione synthetase by kinetic analysis and computational modelling. ', Journal of Biological Chemistry, vol. 288, pp. 23751-23764 . https://doi.org/10.1074/jbc.M113.483289
Journal of Biological Chemistry, 288, 23751-23764. American Society for Biochemistry and Molecular Biology Inc.
The Journal of Biological Chemistry
Leroux, A E, Haanstra, J R, Bakker, B M & Krauth-Siegel, R L 2013, ' Dissecting the catalytic mechanism of Trypanosoma brucei trypanothione synthetase by kinetic analysis and computational modelling. ', Journal of Biological Chemistry, vol. 288, pp. 23751-23764 . https://doi.org/10.1074/jbc.M113.483289
Journal of Biological Chemistry, 288, 23751-23764. American Society for Biochemistry and Molecular Biology Inc.
The Journal of Biological Chemistry
Background: Trypanothione synthetase catalyzes the conjugation of spermidine with two GSH molecules to form trypanothione. Results: The kinetic parameters were measured under in vivo-like conditions. A mathematical model was developed describing the
Autor:
Timothy D. H. Bugg, Nicola Brookbank, Christine Fox, Andrew J. Thompson, Martin J. Sergeant, Dean Rea, Jian-Jun Li
Publikováno v:
The Journal of Biological Chemistry
Members of the carotenoid cleavage dioxygenase family catalyze the oxidative cleavage of carotenoids at various chain positions, leading to the formation of a wide range of apocarotenoid signaling molecules. To explore the functions of this diverse e
Autor:
Kirsty J. McLean, Andy Lawrence, Ross M. Graham, Evelyne Deery, Martin J. Warren, Rebekka Biedendieck, Stephen E. J. Rigby, Susanne Schroeder, Ruth Sarah Rose, Andrew W. Munro
Publikováno v:
Journal of Biological Chemistry. 284:4796-4805
The ring contraction process that occurs during cobalamin (vitamin B(12)) biosynthesis is mediated via the action of two enzymes, CobG and CobJ. The first of these generates a tertiary alcohol at the C-20 position of precorrin-3A by functioning as a
Publikováno v:
Journal of Biological Chemistry. 277:49735-49742
The 1.6-A crystal structure of the covalent ketimine complex of apple 1-aminocyclopropane-1-carboxylate (ACC) synthase with the potent inhibitor l-aminoethoxyvinylglycine (AVG) is described. ACC synthase catalyzes the committed step in the biosynthes
Publikováno v:
Journal of Biological Chemistry. 276:37922-37928
CTP:glycerol-3-phosphate cytidylyltransferase (GCT) catalyzes the synthesis of CDP-glycerol for teichoic acid biosynthesis in certain Gram-positive bacteria. This enzyme is a model for a cytidylyltransferase family that includes the enzymes that synt
Publikováno v:
Journal of Biological Chemistry. 275:37317-37323
The homodimeric flavoenzyme glutathione reductase (GR) maintains high intracellular concentrations of the antioxidant glutathione (GSSG + NADPH + H+ ↔ 2 GSH + NADP+). Due to its central function in cellular redox metabolism, inhibition of GR from t
Publikováno v:
Journal of Biological Chemistry. 272:2252-2258
R67 dihydrofolate reductase (DHFR) is encoded by an R-plasmid, and expression of this enzyme in bacteria confers resistance to the antibacterial drug, trimethoprim. This DHFR variant is not homologous in either sequence or structure with chromosomal
Publikováno v:
Journal of Biological Chemistry. 268:9071-9078
While searching for an enzyme capable of breaking epsilon-(gamma-Glu)-Lys isopeptide bonds cross-linking protein chains, we purified a metallo-proteinase which mimics the action of an isopeptidase on the gamma-chain dimers of cross-linked fibrin. The
Publikováno v:
Journal of Biological Chemistry. 268:3342-3347
Incubation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides with 4-hydroxy-2-nonenal (HNE) results in a pseudo first-order loss of enzyme activity. The pH dependence of the inactivation rate exhibits an inflection around pH 10, and
Publikováno v:
Journal of Biological Chemistry. 266:5087-5093
Deacetoxycephalosporin C hydroxylase from cell-free extracts of Streptomyces clavuligerus was stabilized partially and purified to near homogeneity by three anion-exchange chromatographies, ammonium sulfate fractionation, and two gel filtrations. The