Übersetzung für 'glycosylation enzyme' von Englisch nach Deutsch

glycosylation enzyme

Glykosylierungs­enzym {n}biochem.

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glycosylation

Glycosylierung {f}biochem.

Glykosylation {f}biochem.

Glykosylierung {f}biochem.

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protein glycosylation

Proteinglykosylierung {f} [auch: Protein-Glykosylierung]biochem.

Proteinglycosylierung {f}biochem.

nonenzymatic glycosylation

nichtenzymatische Glykosylierung {f}chem.

glycosylation pattern

Glykosylierungs­muster {n}biotech.

glycosylation reaction

Glycosylierungs­reaktion {f}biochem.

non-enzymatic glycosylation

nichtenzymatische Glykosylierung {f}chem.

enzyme

Enzym {n}biochem.

endogenous enzyme

endogenes Enzym {n}biochem.

membrane enzyme

Membranenzym {n}biochem.

enzyme inhibition

Enzyminhibition {f}biochem.

oxidation enzyme

Oxidationsenzym {n}biochem.

enzyme regulation

Enzymregulation {f}biochem.

enzyme histochemistry

Enzymhistochemie {f}med.

viral enzyme

virales Enzym {n}biochem.

branching enzyme

Verzweigungs­enzym {n}biochem.

debranching enzyme

Entzweigungs­enzym {n}biochem.

coagulation enzyme

Gerinnungs­enzym {n}biochem.

• The enzyme was found to be a type of hydroxylases used in the substrate formation of protein glycosylation.
• In rice, cold stress decreases N-glycosylation of the enzyme, which is thought to alter the enzyme's activity in response to cold.
• The beta 3-glucosyltransferase enzyme is responsible for glycosylation, the attachment of sugars to proteins, which through this modification allows for performance of a wider variety of functions.
• The prominence of salt bridges, disulfide bridges, hydrogen bonding, and glycosylation are thought to contribute to the enzyme’s stability, especially when the plant is under attack and experiences severe tissue damage.
• UDP-N-acetylglucosamine transferase subunit ALG13 homolog, also known as asparagine-linked glycosylation 13 homolog, is an enzyme that in humans is encoded by the "ALG13" gene.

• degree for a dissertation on the role of glycosylation in lysosomal enzyme expression with Kurt von Figura as his advisor.
• It encodes a glycosyltransferase which participates in glycosylation of alpha-dystroglycan, and may carry out the synthesis of glycoprotein and glycosphingolipid sugar chains.
• It contains 119 amino acid residues making it the shortest known human RNase and contains no "N-glycosylation" sites.
• Individual GalNAc-transferases have distinct activities, and initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases.
• Tunicamycin blocks N-linked glycosylation (N-glycans) and treatment of cultured human cells with tunicamycin causes cell cycle arrest in G1 phase.

• In addition, human GCPII has ten sites of potential glycosylation, and many of these sites (including some far from the catalytic domain) affect the ability of GCPII to hydrolyze NAAG.
• In addition, mutations in enzymes involved in the glycosylation of the CD22 ligand may also lead to the susceptibility to autoimmune diseases.
• These N-terminal regions contain several glycosylation sites and it is thought that these sites also play a role in targeting.
• The acceptor substrate can be another sugar such as the transfer of a fucose to a core GlcNAc (N-acetylglucosamine) sugar as in the case of N-linked glycosylation, or to a protein, as in the case of "O"-linked glycosylation produced by "O"-fucosyltransferase.
• CDG syndromes are genetic disorders of the glycosylation pathway.

• The resulting compound is methylated by NovO and SAM prior to glycosylation.
• A study showed that it was evident that glycosylation at the two sites in the F domain (positions 26 and 603), in addition to that in the E domain (position 144), is required for the HE molecule to be transported from the endoplasmic reticulum and that mutant HEs lacking one of these three sites failed to undergo the trimer assembly.
• The non-enzymatic glycosylation is also known as glycation or non-enzymatic glycation.
• Daphnetin is a dihydroxy coumarin and can undergo enzymatic glycosylation to yield 7-O-glucoside also called daphnin.