Translation of "Catalytic site" in German

The specific inhibition of a single catalytic site is of specific interest for the development of drugs.

Angiox contains bivalirudin, a direct and specific thrombin inhibitor that binds both to the catalytic site and the anion-binding exosite of fluid-phase and clot-bound thrombin.

The primary metabolite resulting from the cleavage of Arg3-Pro4 bond of the N-terminal sequence by thrombin is not active because of the loss of affinity to the catalytic active site of thrombin.

The primary metabolite resulting from the cleavage of Arg3-Pro4 bond of the Nterminal sequence by thrombin is not active because of the loss of affinity to the catalytic active site of thrombin.

Etravirine binds directly to reverse transcriptase (RT) and blocks the RNA-dependent and DNA-dependent DNA polymerase activities by causing a disruption of the enzyme's catalytic site.

Nevirapine binds directly to reverse transcriptase and blocks the RNA-dependent and DNA-dependent DNA polymerase activities by causing a disruption of the enzyme's catalytic site.

One of those ions is crucial for the operation of the enzyme: It is located at the catalytic site and holds the hydroxyl group of the alcohol in place.

Since the monoclonal antibodies R 3-36-16 and R 3-47 inhibit human renin very efficiently (Table 1), a homology of the catalytic site of the enzymes human renin and marmoset renin is indicated.

Hence, efficiency of photosynthesis and biomass productivity, may be increased by either changing the ratio of C0 to oxygen at the catalytic site, or changing the

The catalytic site is depicted in blue, the specificity pocket in red, a surface loop in orange and a glycosylation site in green (arrow).

Zinc is essential in the catalytically active site of metalloproteinases.

However, this multi-megadalton complex still has no catalytically active site.

In the carrying out of hydrogenation reactions, hydrogen can be used in a multiple stoichiometric excess, in order to provide the catalytically active sites of the catalyst with sufficient hydrogen.

They are distinguished by their high number of catalytically active sites in conjunction with a large surface area.

The hydrophobic constituents make the penetration of electrolytes difficult and thus keep the appropriate pores free for transport of the oxygen to the catalytically active sites.

The term proteolytic enzyme or protease therefore means, in addition to the functions of the few amino acid residues of the catalytically active site, any functions as resulting from the action of the entire remaining protein or one or more parts of the remaining protein on the actually catalytically active regions.

Reversible blockage both of the storage positions for ammonia and/or nitrogen oxides and of the SCR-catalytically active sites present in the zeolite or zeolite-like compound by hydrocarbons is thus effectively avoided.

They have a large number of catalytically active sites, combined with a large surface area.

The hydrophilic constituents allow penetration of the electrolyte to the catalytically active sites and the outward transport of the hydroxide ions.

Finally, the reduction catalyst coating displays a poorer long-term stability in respect of conversion of NO x compared to conventional SCR catalysts since the more frequent active particle filter regenerations represent a considerable thermal stress on the catalytically active coating and lead to accelerated thermal deactivation of the catalytically active sites.

The approach in the technical solution here is to reduce the diameter of oversize hydrophilic pores or of cracks on the liquid side of the oxygen-consuming electrode by accumulation of fine hydrophilic particles, but at the same time still to ensure sufficient liquid transport and to provide additional catalytically active sites.

In the case of use of such catalytically active substances, the number of catalytically active sites in the gas/liquid/solid three-phase region is increased.

In a preferred embodiment, the term “variant” of a nucleic acid sequence or amino acid sequence, used hereinafter synonymously and exchangeably with the term “homologue”, as used herein, means another nucleic acid or amino acid sequence comprising or representing a sequence which, with respect to the corresponding original wild-type nucleic acid or amino acid sequence, has a homology, used here synonymously with identity, of 70, 75, 80, 85, 90, 92, 94, 96, 98, 99% or greater, wherein preferably amino acids other than the ones forming the catalytically active site or essential for the structure or folding are deleted or substituted or are merely conservatively substituted, for example a glutamate instead of an aspartate or a leucine instead of a valine.