THE ENZYMATIC ACTIVITY ASSOCIATED WITH THE PROTEIN IMMUNOLOGICALLY RELATED TO TRYPTOPHAN SYNTHETASE.

Proc Natl Acad Sci U S A

DEPARTMENT OF MICROBIOLOGY, SCHOOL OF MEDICINE, WESTERN RESERVE UNIVERSITY, CLEVELAND, OHIO.

Published: March 1958

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC335401PMC
http://dx.doi.org/10.1073/pnas.44.3.245DOI Listing

Publication Analysis

Top Keywords

enzymatic activity
4
activity associated
4
associated protein
4
protein immunologically
4
immunologically tryptophan
4
tryptophan synthetase
4
enzymatic
1
associated
1
protein
1
immunologically
1

Similar Publications

Steering acidic oxygen reduction selectivity of single-atom catalysts through the second sphere effect.

Nat Commun

December 2024

Center of Artificial Photosynthesis for Solar Fuels and Department of Chemistry, School of Science, Westlake University, Hangzhou, China.

Natural enzymes feature distinctive second spheres near their active sites, leading to exquisite catalytic reactivity. However, incumbent synthetic strategies offer limited versatility in functionalizing the second spheres of heterogeneous catalysts. Here, we prepare an enzyme-mimetic single Co-N atom catalyst with an elaborately configured pendant amine group in the second sphere via 1,3-dipolar cycloaddition, which switches the oxygen reduction reaction selectivity from the 4e to the 2e pathway under acidic conditions.

View Article and Find Full Text PDF

Cas12e orthologs evolve variable structural elements to facilitate dsDNA cleavage.

Nat Commun

December 2024

Beijing Frontier Research Center for Biological Structure, State Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.

Exceptionally diverse type V CRISPR-Cas systems provide numerous RNA-guided nucleases as powerful tools for DNA manipulation. Two known Cas12e nucleases, DpbCas12e and PlmCas12e, are both effective in genome editing. However, many differences exist in their in vitro dsDNA cleavage activities, reflecting the diversity in Cas12e's enzymatic properties.

View Article and Find Full Text PDF

The β-1,4 galactosylation catalyzed by β-1,4 galactosyltransferases (β4Gal-Ts) is not only closely associated with diverse physiological and pathological processes in humans but also widely applied in the -glycan modification of protein glycoengineering. The loop-closing process of β4Gal-Ts is an essential intermediate step intervening in the binding events of donor substrate (UDP-Gal/Mn) and acceptor substrate during its catalytic cycle, with a significant impact on the galactosylation activities. However, the molecular mechanisms in regulating loop-closing dynamics are not entirely clear.

View Article and Find Full Text PDF

The outstanding efficiency and selectivity of enzymatic reactions, such as C-H oxidation by nonheme iron oxygenases, stems from a precise control of substrate positioning inside the active site. The resulting proximity between a specific moiety (a certain C-H bond) to the reactant (a FeIV(O) active species) translates into higher rates and selectivity, that can be in part replicated also with artificial supramolecular catalysts. However, structural modification of the position and orientation of the binding site both in enzymes and in artificial catalysts often leads to significant variations in reactivity that can be difficult to rationalize due to the system's complexity.

View Article and Find Full Text PDF

Background: Intracerebral hemorrhage (ICH) is a severe condition associated with high mortality and disability rates. Oxidative stress plays a critical role in the development of secondary brain injury (SBI) following ICH. Previous research has demonstrated that Annao Pingchong decoction (ANPCD) treatment for ICH has antioxidant effects, but the exact mechanism is not yet fully understood.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!