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Creative Enzymes has been a lead company in enzyme activity assays for years. We offer the rapid activity measurement in industrial scales and deeply customized activity assays for any special request. The premier team is specialized in activity measurement of oxidoreductases, including shikimate dehydrogenase, using spectrophotometry.
Shikimate Dehydrogenase (EC 1.1.1.25) catalyzes the reversible NADPH-dependent reduction of 3-dehydroshikimate to shikimate. The enzyme reduces the carbon-oxygen double bond of a carbonyl group to a hydroxyl group, meanwhile the cofactor NADPH is oxidized to NADP+. This enzyme can be found in phenylalanine, tyrosine, and tryptophan biosynthesis, acting on one step of the shikimate pathway. This pathway essential in bacteria, plants, fungi, algae, and parasites and is responsible for the biosynthesis of aromatic amino acids, such as phenylalanine, tyrosine, and tryptophan, from the metabolism of carbohydrates. In contrast, shikimate pathway is absent in animals and humans. As a result, the three aromatic amino acids are essential amino acids that must be obtained through diet. The systematic name of this enzyme class is shikimate:NADP+ 3-oxidoreductase, and it is also known as:
Because the shikimate pathway is not present in human or animals, it is identified as a promising target for herbicides and antimicrobial agents. Studies on shikimate dehydrogenases have become an emerging topic, as more and more hebicides and antibiotics loss efficacy to the growing resistance. In addition, it is also important to maintain diversity in the blocked enzymes in one pathway to achieve higher bacteria killing rates. Given the dismal prospective of current antimicrobial treatment, the demand of potent and non-toxic inhibitors of shikimate dehydrogenase continues to grow. Even that the activity test of shikimate dehydrogenase was reported before, the assay is never easy to perform. The instability of its substrates and susceptibility to interference from other enzymes makes the task difficult. Creative Enzymes overcomes all these hurdles with the support of the scientist team and the-state-of-the-art instruments. The enzymatic activity can be accurately monitored at either reaction direction through changes in NADPH concentrations by measuring absorption intensity at 340 nm.
Creative Enzymes is excited to offer you the latest activity assays for shikimate dehydrogenase and willing to collabroate with you towards success. As you may work in the pharmaceutical, agricultural, or veterinary industry, we are always ready to deliver high-quality activity results all the same.
Figure: The crystal structure of shikimate dehydrogenase, showing the unique binding loop (green) for NADPH (yellow).
Reference: Ye, S. et. al., A. J. Bacteriol. 2003, 185 (14), 4144.
