Cofactor designing in functional analysis of thiamin diphosphate enzymes.

Methods Enzymol

Fachbereich Biochemie/Biotechnologie, Institue of Biochemistry, University of Halle-Wittenberg, Germany.

Published: August 1997

Download full-text PDF

Source
http://dx.doi.org/10.1016/s0076-6879(97)79017-7DOI Listing

Publication Analysis

Top Keywords

cofactor designing
4
designing functional
4
functional analysis
4
analysis thiamin
4
thiamin diphosphate
4
diphosphate enzymes
4
cofactor
1
functional
1
analysis
1
thiamin
1

Similar Publications

Redox enzymes, mostly equipped with metal or organic cofactors, can vary their reactivity with oxygen by orders of magnitudes. Understanding how oxygen reactivity is controlled by the protein milieu remains an open issue with broad implications for mechanistic enzymology and enzyme design. Here, we address this problem by focusing on a widespread group of flavoenzymes that oxidize phenolic compounds derived from microbial lignin degradation, using either oxygen or a cytochrome c as electron acceptors.

View Article and Find Full Text PDF

Objectives: This study aims (1) to assess the prevalence of severe fatigue among the general population of Geneva, 2 years into the COVID-19 pandemic and (2) to identify pandemic and non-pandemic factors associated with severe fatigue.

Design: Cross-sectional population-based survey conducted in Spring 2022.

Setting: General adult population of Geneva, Switzerland.

View Article and Find Full Text PDF

Purification and Electron Transfer from Soluble c-Type Cytochrome TorC to TorA for Trimethylamine N-Oxide Reduction.

Int J Mol Sci

December 2024

Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht Str. 24-25, 14476 Potsdam, Germany.

The enterobacterium present in the human gut can reduce trimethylamine N-oxide (TMAO) to trimethylamine during anaerobic respiration. The TMAO reductase TorA is a monomeric, bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor-containing enzyme that belongs to the dimethyl sulfoxide reductase family of molybdoenzymes. TorA is anchored to the membrane via TorC, a pentahemic -type cytochrome which receives the electrons from the menaquinol pool.

View Article and Find Full Text PDF

Purpose: The development of endocrine resistance remains a significant challenge in the clinical management of estrogen receptor-positive () breast cancer. Metabolic reprogramming is a prominent component of endocrine resistance and a potential therapeutic intervention point. However, a limited understanding of which metabolic changes are conserved across the heterogeneous landscape of ER+ breast cancer or how metabolic changes factor into ER DNA binding patterns hinder our ability to target metabolic adaptation as a treatment strategy.

View Article and Find Full Text PDF

Proteomics Analysis of Five Potential Plasma-derived Exosomal Biomarkers for Acute Myocardial Infarction.

Curr Med Chem

January 2025

Department of Cardiology, Taizhou Hospital of Zhejiang Province, affiliated to Wenzhou Medical University, Linhai, Zhejiang Province, China.

Aims: This study was to explore the relationship between plasma exosomes and Acute myocardial infarction (AMI).

Background: Acute myocardial infarction (AMI) is one of the most common cardiovascular complications. Recent studies have shown that exosomes play a crucial role in the development and progression of cardiovascular diseases.

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!