Results 61 to 70 of about 4,201 (187)

Extending Cofactor‐Tethered Nanomachines to Complex Multienzyme Redox Cascades in Continuous Flow

open access: yesChemSusChem, Volume 19, Issue 15, 14 August 2026.
Engineered enzyme fusions bearing covalently tethered PEG–nicotinamide cofactors enable intramolecular cofactor retention and recycling within self‐sufficient biocatalytic nanomachines. These nanomachines support cofactor‐autonomous operation of complex redox multienzyme cascades under continuous‐flow conditions, as demonstrated in a 10‐step glucose‐to‐
Zinnia Dsouza   +4 more
wiley   +1 more source

Enzymatic Synthesis of NAD+

open access: yesCurrent Protocols, Volume 6, Issue 6, June 2026.
Abstract Nicotinamide adenine dinucleotide (NAD+) is an essential metabolite involved in numerous biological processes, functioning both as a redox cofactor in cellular energy metabolism and as a co‐substrate for NAD+‐utilizing enzymes, including sirtuins and poly(ADP‐ribose) polymerases.
Emily Boyle, Olivia Zhang, Yana Cen
wiley   +1 more source

The return of metabolism: biochemistry and physiology of glycolysis

open access: yesBiological Reviews, Volume 101, Issue 2, Page 751-803, April 2026.
ABSTRACT Glycolysis is a fundamental metabolic pathway central to the bioenergetics and physiology of virtually all living organisms. In this comprehensive review, we explore the intricate biochemical principles and evolutionary origins of glycolytic pathways, from the classical Embden–Meyerhof–Parnas (EMP) pathway in humans to various prokaryotic and ...
Nana‐Maria Grüning   +19 more
wiley   +1 more source

Biochemical Characterisation of the Lon Protease from Thermoplasma acidophilum [PDF]

open access: yes, 2007
Die Lon-Protease aus dem Archaebakterium Thermoplasma acidophilum (TaLon) besteht aus einer N-terminalen AAA+-Domäne und einer C-terminalen Lon-Protease-Domäne. Die AAA+-Domäne wird von einer Transmembrandomäne unterbrochen.
Besche, Henrike Christine
core  

The thermoplasma acidophilum rpl15 gene encodes a homologue of eukaryotic ribosomal proteins l15/yl10

open access: yes, 1995
A gene has been cloned from the archaebacterium, Thermoplasma acidophilum, which, on the basis of the deduced amino acid sequence, encodes a homologue of the eukaryotic large subunit ribosomal proteins, L15/YL10.
Zwickl, P.   +3 more
core   +1 more source

Enzyme Technology in the Food Industry: Molecular Mechanisms, Applications, and Sustainable Innovations

open access: yesFood Science &Nutrition, Volume 13, Issue 9, September 2025.
This review explores the role of microbial and plant enzymes in food processing, highlighting advancements in molecular engineering and sustainable production from underutilized agro‐industrial waste. It focuses on key enzymes such as amylase, lipase, protease, and lactase, discussing their applications, advantages, and challenges in enhancing product ...
Fahima Siddikey   +8 more
wiley   +1 more source

The thermosome - alternating alpha and beta-subunits within the chaperonin of the archaeon thermoplasma acidophilum

open access: yes, 1997
The thermosome of the archaeon Thermoplasma acidophilum is composed of two subunits, alpha and beta, which are arranged in two stacked, eight-membered rings.
Nitsch, M.   +5 more
core   +1 more source

Bioleaching as an Eco‐Friendly Nano‐Factory for Sustainable Inorganic Waste Management: Current Advancements, Challenges, and Opportunities

open access: yesChemistryOpen, Volume 14, Issue 9, September 2025.
The review explores the latest updates and information about the global trends and hazards of e‐waste and also discusses the bioleaching of metals and nanoparticles from various inorganic wastes. It also focuses on the mechanistic pathway of the bioleaching process and computational aspects. Inorganic waste management and metal recovery technology pose
Adhish Jaiswal   +7 more
wiley   +1 more source

Identification, characterization and classification of prokaryotic nucleoid‐associated proteins

open access: yesMolecular Microbiology, Volume 123, Issue 3, Page 206-217, March 2025.
Nucleoid‐associated proteins (NAPs) structure DNA by either bending, wrapping, bridging, or forming protein filaments on the DNA. We review newly identified NAPs and provide a list of simple biochemical assays to study the DNA‐structuring properties of novel NAPs. Abstract Common throughout life is the need to compact and organize the genome.
Samuel Schwab, Remus T. Dame
wiley   +1 more source

Chromatin and gene regulation in archaea

open access: yesMolecular Microbiology, Volume 123, Issue 3, Page 218-231, March 2025.
Recent data from diverse archaea with different repertoires of nucleoid‐associated proteins show a common genome‐wide chromatin organisation where chromatin maintains access to gene promoters independently of transcription activity. Abstract The chromatinisation of DNA by nucleoid‐associated proteins (NAPs) in archaea ‘formats’ the genome structure in ...
Fabian Blombach, Finn Werner
wiley   +1 more source

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