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Active site of T. thermophilus hpaB, showing hydrogen bonding of hpaB catalytic residues to 4-hydroxyphenylacetate and to the peroxide bound to FADH 2. (Note: this structure was generated using oxidized FAD in place of FADH 2; the magenta sphere representing oxygen here is actually a water molecule believed to occupy the space oxygen does when the flavin hydroxyperoxide is present.
SCD-1 is an important metabolic control point. Inhibition of its expression may enhance the treatment of a host of metabolic diseases. [9] One of the unanswered questions is that SCD remains a highly regulated enzyme, even though oleate is readily available, as it is an abundant monounsaturated fatty acid in dietary fat.
In enzymology, a phenylalanine 2-monooxygenase (EC 1.13.12.9) is an enzyme that catalyzes the chemical reaction. L-phenylalanine + O 2 2-phenylacetamide + CO 2 + H 2 O. Thus, the two substrates of this enzyme are L-phenylalanine and O 2, whereas its 3 products are 2-phenylacetamide, CO 2, and H 2 O.
In enzymology, a selenide, water dikinase (EC 2.7.9.3) is an enzyme that catalyzes the chemical reaction. ATP + selenide + H 2 O AMP + selenophosphate + phosphate. The 3 substrates of this enzyme are ATP, selenide, and H 2 O, whereas its 3 products are AMP, selenophosphate, and phosphate.
Cas9 (CRISPR associated protein 9, formerly called Cas5, Csn1, or Csx12) is a 160 kilodalton protein which plays a vital role in the immunological defense of certain bacteria against DNA viruses and plasmids, and is heavily utilized in genetic engineering applications. Its main function is to cut DNA and thereby alter a cell's genome.
Cas9 (or "CRISPR-associated protein 9") is an enzyme that uses CRISPR sequences as a guide to recognize and open up specific strands of DNA that are complementary to the CRISPR sequence. Cas9 enzymes together with CRISPR sequences form the basis of a technology known as CRISPR-Cas9 that can be used to edit genes within living organisms.
Heme oxygenase 1 (HMOX1, commonly HO-1) is a member of the heat shock protein (HSP) family identified as HSP32.HO-1 is a 32kDa enzyme which contains 288 amino acid residues encoded by the HMOX1 gene.
The structure of sucrose phosphorylase has been identified in numerous experiments. The enzyme consists of four major domains, namely A, B, B’, and C. Domains A, B’ and C exist as dimers around the active site. [6] The size of the enzyme, as determined by sedimentation centrifugation, was found to be 55 KDa, consisting of 488 amino acids. [7]