Fritz G

References (3)

Title : Seek and you shall find-news on the quest for novel PET-degrading enzymes - Faber_2023_Febs.j__
Author(s) : Faber A , Fritz G
Ref : Febs J , : , 2023
Abstract : Plastic-degrading enzymes hold immense potential for eco-friendly recycling methods. However, the catalytic rates of current enzymes do not stack up against the mammoth task of degrading millions of tons of plastic waste per year. In the quest for more efficient polyethylene terephthalate (PET)-degrading enzymes, Zhang et al. report the discovery and characterization of PET40, a versatile PET-hydrolyzing esterase that is divergent from most characterized PETases. While PET40 has comparably low hydrolytic activity on PET, Zhang et al. demonstrate its broad activity on an expanded substrate pool. This sheds light on the potential ecological role of these esterases and suggests that PET might be only a recent addition to their substrate spectrum.
ESTHER : Faber_2023_Febs.j__
PubMedSearch : Faber_2023_Febs.j__
PubMedID: 37731192

Title : Perception of butenolides by Bacillus subtilis via the alpha\/beta hydrolase RsbQ - Melville_2023_Curr.Biol__
Author(s) : Melville KT , Kamran M , Yao J , Costa M , Holland M , Taylor NL , Fritz G , Flematti GR , Waters MT
Ref : Current Biology , : , 2023
Abstract : The regulation of behavioral and developmental decisions by small molecules is common to all domains of life. In plants, strigolactones and karrikins are butenolide growth regulators that influence several aspects of plant growth and development, as well as interactions with symbiotic fungi.(1)(,)(2)(,)(3) DWARF14 (D14) and KARRIKIN INSENSITIVE2 (KAI2) are homologous enzyme-receptors that perceive strigolactones and karrikins, respectively, and that require hydrolase activity to effect signal transduction.(4)(,)(5)(,)(6)(,)(7) RsbQ, a homolog of D14 and KAI2 from the gram-positive bacterium Bacillus subtilis, regulates growth responses to nutritional stress via the alternative transcription factor SigmaB (sigma(B)).(8)(,)(9) However, the molecular function of RsbQ is unknown. Here, we show that RsbQ perceives butenolide compounds that are bioactive in plants. RsbQ is thermally destabilized by the synthetic strigolactone GR24 and its desmethyl butenolide equivalent dGR24. We show that, like D14 and KAI2, RsbQ is a functional butenolide hydrolase that undergoes covalent modification of the catalytic histidine residue. Exogenous application of both GR24 and dGR24 inhibited the endogenous signaling function of RsbQ in vivo, with dGR24 being 10-fold more potent. Application of dGR24 to B. subtilis phenocopied loss-of-function rsbQ mutations and led to a significant downregulation of sigma(B)-regulated transcripts. We also discovered that exogenous butenolides promoted the transition from planktonic to biofilm growth. Our results suggest that butenolides may serve as inter-kingdom signaling compounds between plants and bacteria to help shape rhizosphere communities.
ESTHER : Melville_2023_Curr.Biol__
PubMedSearch : Melville_2023_Curr.Biol__
PubMedID: 38183985
Gene_locus related to this paper: bacsu-RsbQ

Title : Dependence of lipoprotein-lipase-catalyzed triacylglycerol hydrolysis on droplet size of synthetic monodisperse emulsions measured with static light scattering - Fritz_2004_J.Colloid.Interface.Sci_275_642
Author(s) : Fritz G , Wagner EM , Lindner H , Hofmann W , Zechner R , Glatter O
Ref : J Colloid Interface Sci , 275 :642 , 2004
Abstract : Well-defined triolein emulsions of low polydispersity were prepared by shearing a crude emulsion in a modified Couette cell, resulting in radii in the range of 300 to 900 nm. These emulsions were used as synthetic substrates for lipoprotein lipase, a key enzyme for the hydrolysis of serum triacylglycerols. The change in radius with time was studied with on-line static light scattering at 37 degrees C. An optimum radius of about 750 nm was found for this reaction.
ESTHER : Fritz_2004_J.Colloid.Interface.Sci_275_642
PubMedSearch : Fritz_2004_J.Colloid.Interface.Sci_275_642
PubMedID: 15178298