Publications by authors named "Samuel Tanoeyadi"

Article Synopsis
  • Researchers have identified the ebo cluster, a group of genes found in various bacteria and algae, which has different roles including a defense mechanism in bacterial strains against nematode grazing.
  • In cyanobacteria, the ebo cluster aids in transporting the scytonemin monomer within the cell.
  • The study reveals that EboD proteins from this cluster convert mannose 6-phosphate into a new compound, potentially serving as a signaling molecule or transporter, thus expanding the understanding of sugar phosphate cyclases.
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Sedoheptulose 7-phosphate (SH7P) cyclases are a subset of sugar phosphate cyclases that are known to catalyze the first committed step in many biosynthetic pathways in primary and secondary metabolism. Among them are 2--5--valiolone synthase (EEVS) and 2--valiolone synthase (EVS), two closely related SH7P cyclases that catalyze the conversion of SH7P to 2--5--valiolone and 2--valiolone, respectively. However, how these two homologous enzymes use a common substrate to produce stereochemically different products is unknown.

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Serine proteases are important enzymes widely used in commercial products and industry. Recently, we identified a new serine protease from the desert bacterium Bacillus subtilis ZMS-2 that showed enhanced activity in the presence of Zn, Ag, or HO. However, the molecular basis underlying this interesting property is unknown.

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Microbial alkaline proteases are dominating the global enzyme market with a share of over 65% due to their multifarious catalytic potentials. Hence, production of proteases with novel properties of commercial significance is highly desirable to meet the global enzyme demand. Here, we report the purification, characterization, and pilot-scale application of a serine protease from the desert soil bacterium Bacillus subtilis ZMS-2 with novel properties as dehairing agent in leather processing.

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Acarbose is a well-known microbial specialized metabolite used clinically to treat type 2 diabetes. This natural pseudo-oligosaccharide (PsOS) shows potent inhibitory activity toward various glycosyl hydrolases, including α-glucosidases and α-amylases. While acarbose and other PsOSs are produced by many different bacteria, their ecological or biological role in microbial communities is still an open question.

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Natural ribomimetics represent an important group of specialized metabolites with significant biological activities. Many of the activities, , inhibition of seryl-tRNA synthetases, glycosidases, or ribosomes, are manifestations of their structural resemblance to ribose or related sugars, which play roles in the structural, physiological, and/or reproductive functions of living organisms. Recent studies on the biosynthesis and biological activities of some natural ribomimetics have expanded our understanding on how they are made in nature and why they have great potential as pharmaceutically relevant products.

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