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Nitrous oxide production via enzymatic nitroxyl from the nitrifying archaeon .
Proc Natl Acad Sci U S A
January 2025
Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, NY 14853.
Ammonia oxidizing archaea (AOA) are among the most abundant microorganisms on earth and are known to be a major source of nitrous oxide (NO) emissions, although biochemical origins of this NO remain unknown. Enzymological details of AOA nitrogen metabolism are broadly unavailable. We report the recombinant expression, purification, and characterization of a multicopper oxidase, Nmar_1354, from the AOA .
View Article and Find Full Text PDFAn unusual family of bifunctional terpene synthases has been discovered in which both catalytic domains - a prenyltransferase and a cyclase - are connected by a long, flexible linker. These enzymes are unique to fungi and catalyze the first committed steps in the biosynthesis of complex terpenoid natural products: the prenyltransferase assembles 5-carbon precursors to form C geranylgeranyl diphosphate (GGPP), and the cyclase converts GGPP into a polycyclic hydrocarbon product. Weak domain-domain interactions as well as linker flexibility render these enzymes refractory to crystallization and challenge their visualization by cryo-EM.
View Article and Find Full Text PDFEffects of different concentrations of N-acetylcysteine on the sperm quality, antioxidant enzyme activity, and antioxidant gene expression of cryopreserved goat semen.
Theriogenology
March 2025
College of Animal Science/Key Laboratory of Animal Genetics, Breeding and Reproduction in the Plateau Mountainous Region, Ministry of Education/Key Laboratory of Animal Genetics, Breeding and Reproduction, Guizhou University, Guiyang, 550025, China. Electronic address:
During cryopreservation, spermatozoa produce excess reactive oxygen species (ROS), which attack the plasma membrane, disrupt the physiological structure of the sperm, and ultimately decrease semen quality. This study investigated the effects of different N-acetylcysteine (NAC) concentrations on the cryopreservation of semen from Qianbei Ma goats. Semen samples were collected from five bucks with motility rates above 80 %.
View Article and Find Full Text PDFHeterologous expression and enzymological characterization of L-glutamate oxidase from the marine actinomycete Streptomyces lydicamycinicus NBRC 110027.
Biosci Biotechnol Biochem
December 2024
Department of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University, 3-3-35 Yamate-Cho, Suita, Osaka-Fu 564-8680, Japan.
We successfully constructed a heterologous expression system for L-glutamate oxidase from the marine actinomycete Streptomyces lydicamycinicus NBRC 110027 (Sl-LGOX) in Escherichia coli BL21(DE3) as a host. This is the first example of L-glutamate oxidase from a marine microorganism. A chemically synthesized gene optimized for codon usage in E.
View Article and Find Full Text PDFEnzymatic characterization of a thermostable 6-phosphogluconate dehydrogenase from and its application for NADH regeneration.
3 Biotech
January 2025
Yantai Key Laboratory of Characteristic Agricultural Bioresource Conservation and Germplasm Innovative Utilization, School of Life Sciences, Yantai University, Yantai, 264005 Shandong People's Republic of China.
Unlabelled: 6-Phosphogluconate dehydrogenases (6PGDHs) are widely existing as reduced cofactor (NADH/NADPH) regeneration biocatalysts. Herein, a thermostable 6PGDH from (Ht6PGDH) was overexpressed in and enzymologically characterized. Ht6PGDH exhibited exceptional stability and catalytic activity under high-temperature conditions, with an optimum temperature of 85 °C and the ability to maintain high activity for prolonged periods at 70 °C, which could be purified through a one-step heat treatment.
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