Acceptor substrates

Xem 1-7 trên 7 kết quả Acceptor substrates
  • The influence of substrates on the interaction of apotrans-ketolase with thiamin diphosphate was investigated in the presence of magnesium ions. It was shown that the donor substrates, but not the acceptor substrates, enhance the affinity of the coenzyme either to only one active center of transketolase or to both active centers, but to different degrees in each, resulting in a negative cooperativity for coenzyme binding. In the absence of donor substrate, neg-ative cooperativity is not observed. ...

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  • Application of polymers from renewable resources - also identified as biopolymers - has a large potential market due to the current emphasis on sustainable technology. For optimal R&D achievements and hence benefits from these market opportunities, it is essential to combine the expertise available in the vast range of different disciplines in biopolymer science and technology.

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  • Plant family 32 glycoside hydrolase enzymes include hydrolases (cell wall invertases, fructan exohydrolases, vacuolar invertases) and fructosyltrans-ferases. These enzymes are very similar at the molecular and structural levels but are functionally different. Understanding the basis of the func-tional diversity in this family is a challenging task.

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  • UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc transferases), which initiate mucin-type O-glycan biosynthesis, have broad acceptor substrate specificities, and it is still unclear how they recognize peptides with different sequences.

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  • The specificity of the aglycone-binding site ofEscherichia colia-xylosidase (YicI), which belongs to glycoside hydrolase family 31, was characterized by examining the enzyme’s transxylosylation-catalyzing property. Acceptor specificity and regioselectivity were investigated using various sugars as acceptor substrates anda-xylosyl fluoride as the donor substrate.

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  • Calmodulin (CaM) activates the constitutive isoforms of mammalian nitric oxide synthase by triggering electron transfer from the reductase domain FMN to the heme. This enables the enzymes to be regulated by Ca 2+ con-centration. CaM exerts most of its effects on the reductase domain; these include activation of electron transfer to electron acceptors, and an increase in the apparent rate of flavin reduction by the substrate NADPH.

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  • Apple flavor is characterized by combinations of ester compounds, which increase markedly during fruit ripening. The final step in ester biosynthesis is catalyzed by alcohol acyl transferases (AATs) that use coenzyme A (CoA) donors together with alcohol acceptors as substrates. The gene MpAAT1, which produces a predicted protein containing features of other plant acyl transferases, was isolated fromMalus pumila(cv. Royal Gala). TheMpAAT1gene is expressed in leaves, flowers and fruit of apple.

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