Enzymes catalyze nearly all of the chemical reactions that occur in biological systems. Enzymes are generally proteins but also include catalytic DNA and catalytic RNA. As effective biological catalysts, enzymes work by lowering a reaction’s activation energy barrier, thereby increasing the rate of the reaction. They also improve the specificity of the reactions.

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News and Comment

  • Comments and Opinion |

    Dipeptidylpeptidase (DPP)-4 is a key regulator of the incretin system. For several years DPP-4 inhibitors in addition to GLP-1 analogues are of major importance in the clinical management of obesity and type 2 diabetes. DPP-4 is also known as CD26 and represents a membrane bound protease on the surface of several eukaryotic cell types. Of interest, DPP-4, like ACE2, has been shown to serve as a binding partner for corona-like viruses to enter host immune cells. Since metabolic diseases are major risk factors for the present COVID-19 pandemic, we examined circulating soluble DPP-4 serum concentrations in patients suffering from severe COVID-19 infection and in healthy human subjects in a case control design. In this analysis sDPP-4 levels were significantly lower in COVID-19 patients compared to controls (242.70 ± 202.12 ng/mL versus 497.70 ± 188.13 ng/mL, p = 0.02). We also examined sDPP-4 serum concentrations in patients suffering from sepsis not due to corona-like viruses. In these subjects, sDPP-4 levels were not different compared to healthy case controls (p = 0.14), which might suggest the decrease of sDPP-4 to be specific for corona-like virus infections. Currently, most data point towards membrane bound ACE2 in contrast to DPP-4 as the major binding partner for COVID-19 internalization into host immune cells. However, the finding that the circulating soluble form of DPP-4 is reduced in hospitalized patients might suggest a regulatory role for both, ACE and DPP-4, in COVID-19 infections, especially since obesity and type 2 diabetes are major risk factor for a severe course of the disease

    • Kristina Schlicht
    • , Nathalie Rohmann
    • , Corinna Geisler
    • , Tim Hollstein
    • , Carina Knappe
    • , Katharina Hartmann
    • , Jeanette Schwarz
    • , Florian Tran
    • , Domagoj Schunk
    • , Ralf Junker
    • , Thomas Bahmer
    • , Philip Rosenstiel
    • , Dominik Schulte
    • , Kathrin Türk
    • , Andre Franke
    • , Stefan Schreiber
    •  & Matthias Laudes
  • News and Views |

    It is generally believed that large protein complexes provide a catalytic advantage due to substrate channeling between enzymatic domains. However, the structure and function of the pentafunctional AROM complex suggests a noteworthy exception.

    • Martin St. Maurice
  • News and Views |

    Enzymes that methylate using S-adenosyl-l-methionine — nature’s methyliodide — are abundant and often promiscuous; however, a preference for alkylation over methylation has been neither observed in nature nor engineered. Now, carboxymethylation has been demonstrated using engineered methyltransferases.

    • Jennifer N. Andexer
    •  & Andrea Rentmeister
    Nature Chemistry 12, 791-792
  • Comments and Opinion
    | Open Access

    Glycans are ubiquitous in biology, but their complex structure and biosynthesis have challenged research of their wide-ranging roles. Here, the authors comment on current trends on the role of chemical methodologies in the field of glycobiology.

    • Mia I. Zol-Hanlon
    •  & Benjamin Schumann