Zobrazeno 1 - 7
of 7
pro vyhledávání: '"J S, Lolkema"'
Publikováno v:
Journal of applied microbiology. 107(6)
To demonstrate that the meat food strain Weissella halotolerans combines an ornithine decarboxylation pathway and an arginine deiminase (ADI) pathway and is able to produce putrescine, a biogenic amine. Evidence is shown that these two pathways produ
Publikováno v:
Journal of molecular biology. 296(1)
The V-type Na(+)-ATPase of the thermophilic, anaerobic bacterium Caloramator fervidus was purified to homogeneity. The subunit compositions of the catalytic V(1) and membrane-embedded V(0) parts were determined and the structure of the enzyme complex
Publikováno v:
The Journal of biological chemistry. 272(29)
Membrane potential generation via malate/lactate exchange catalyzed by the malate carrier (MleP) of Lactococcus lactis, together with the generation of a pH gradient via decarboxylation of malate to lactate in the cytoplasm, is a typical example of a
Publikováno v:
Antonie van Leeuwenhoek. 71(1-2)
Lactic acid bacteria play an essential role in many food fermentation processes. They are anaerobic organisms which obtain their metabolic energy by substrate phosphorylation. In addition three secondary energy transducing processes can contribute to
Autor:
J S, Lolkema, B, Poolman
Publikováno v:
The Journal of biological chemistry. 270(21)
The kinetic behavior of a H(+)-substrate symporter has been studied in which in addition to the unloaded (E) and fully loaded states (E.S.H) of the carrier also one of the binary complexes (E.S or E.H) may reorient its binding sites. This results in
Autor:
J S, Lolkema
Publikováno v:
The Journal of biological chemistry. 268(24)
An analysis of complex kinetic mechanisms is proposed that consists of two steps, (i) building of an kinetic scheme from experimental data other than steady-state kinetics and (ii) numerical simulation and analysis of the kinetics of the proposed sch
Publikováno v:
The Journal of biological chemistry. 268(24)
The kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the bacterial P-enolpyruvate-dependent phosphotransferase system are described for three different physical conditions of the enzyme, (i) embedded in the membrane of inside-out (IS