Results 61 to 70 of about 8,399 (179)

Copper in cancer: friend or foe? Metabolism, dysregulation, and therapeutic opportunities

Cancer Communications, Volume 45, Issue 5, Page 577-607, May 2025.
Abstract Copper, one of the essential nutrients for the human body, acts as an electron relay in multiple pathways due to its redox properties. Both deficiencies and excesses of copper lead to cellular fragility. Therefore, it can manifest pro‐ and anti‐cancer properties in tumors. Therefore, it is crucial to clarify the copper activity within the cell.
Dan Shan, Jinling Song, Yuqing Ren, Yuyuan Zhang, Yuhao Ba, Peng Luo, Quan Cheng, Hui Xu, Siyuan Weng, Anning Zuo, Shutong Liu, Xinwei Han, Jinhai Deng, Zaoqu Liu   +13 more
wiley   +1 more source

AKR1B1 Expression in the Colorectal Tumor Microenvironment Contributes Towards Its Prognostic Significance

Cancer Medicine, Volume 14, Issue 10, May 2025.
Our data show for the first time that CRC tumors have expression of AKR1B1 in both epithelial and stromal compartments; moreover, the relationship of AKR1B1 expression and clinical outcome depends highly on the TME content. ABSTRACT Background AKR1B1, a member of the aldo‐keto reductase enzyme family involved in the polyol pathway of aldehyde ...
Seçil Demirkol Canlı, Güneş Güner, Aynur Işık, Branka Sosic‐Jurjevic, Aleksandra Djikic Rom, Esin Gülce Seza, Ömer Dizdar, Sandra Dragicevic, Aleksandra Nikolic, Aytekin Akyol, Sreeparna Banerjee   +10 more
wiley   +1 more source

NADH Driven Enzymatic Carboxylic Acid Reduction

ChemCatChem, Volume 17, Issue 9, May 8, 2025.
Run your carboxylic acid reductase (CAR) with NADH? Yes, because well‐known CARs use NADH. NADPH remains the preferred cofactor for various diverse CARs but high conversions are possible also with NADH. We show a new Type of CAR that produces alcohols from the respective acids in the presence of either NADH or NADPH. Abstract Carboxylic acid reductases
Jonathan Guyang Ling, Hannah G. Breuer, Holly Stolterfoht‐Stock, Farah Diba Abu Bakar, Margit Winkler   +4 more
wiley   +1 more source

Rules for biocatalyst and reaction engineering to implement effective, NAD(P)H-dependent, whole cell bioreductions [PDF]

, 2015
Access to chiral alcohols of high optical purity is today frequently provided by the enzymatic reduction of precursor ketones. However, bioreductions are complicated by the need for reducing equivalents in the form of NAD(P)H.
Kratzer, Regina, Nidetzky, Bernd, Woodley, John   +2 more
core   +1 more source

Aromatic aldehydes at the active site of aldehyde oxidoreductase from Desulfovibrio gigas: reactivity and molecular details of the enzyme–substrate and enzyme–product interaction

JBIC Journal of Biological Inorganic Chemistry, 2014
Desulfovibrio gigas aldehyde oxidoreductase (DgAOR) is a mononuclear molybdenum-containing enzyme from the xanthine oxidase (XO) family, a group of enzymes capable of catalyzing the oxidative hydroxylation of aldehydes and heterocyclic compounds. The kinetic studies reported in this work showed that DgAOR catalyzes the oxidative hydroxylation of ...
Correia, Hugo D., Marangon, Jacopo, Brondino, Carlos Dante, Moura, Jose J. G., Romão, Maria J., González, Pablo Javier, Santos Silva, Teresa   +6 more
openaire   +4 more sources

Enzymes involved in vinyl acetate decomposition by Pseudomonas fluorescens PCM 2123 strain [PDF]

, 2013
Esterases are widely used in food processing industry, but there is little information concerning enzymes involved in decompositions of esters contributing to pollution of environment.
Bartelmus, Grażyna, Greń, Izabela, Szczyrba, Elżbieta   +2 more
core   +1 more source

Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas

Journal of Bacteriology, 1995
Desulfovibrio gigas NCIMB 9332 cells grown in ethanol-containing medium with 0.1 microM tungstate contained a benzylviologen-linked aldehyde oxidoreductase. The enzyme was purified to electrophoretic homogeneity and found to be a homodimer with a subunit M(r) of 62,000. It contained 0.68 +/- 0.08 W, 4.8 Fe, and 3.2 +/- 0.2 labile S per subunit.
T. A. Hansen, Wilfred R. Hagen, C. M. H. Hensgens   +2 more
openaire   +5 more sources

A Short Chain NAD(H)-Dependent Alcohol Dehydrogenase (HpSCADH) from Helicobacter Pylori: a Role in Growth under Neutral and Acidic Conditions. [PDF]

, 2013
Toxic aldehydes produced by alcohol dehydrogenases have been implicated in the pathogenesis of Helicobacter pylori-related damage to the gastric mucosa. Despite this, the enzymes that might be responsible for producing such aldehydes have not been fully ...
Cornally, Denise, Henehan, Gary, Kumari, A., Ryan, Barry, Windle, Henry   +4 more
core   +1 more source

Enzymatic Study on the Microbial Degradation of Homocholine [PDF]

This research was conducted to investigate the enzymatic activities in the degradation pathway of homocholine by bacterial strains isolated from the soil.
Ahmed, I.A. Mohamed, Arima, J., Eltayeb, M.M., Nori, N.   +3 more
core  

Metabolites and dead-end products from the microbial oxidation of quaternary ammonium alcohols [PDF]

, 2018
Methyl-triethanol-ammonium originates from the hydrolysis of the parent esterquat surfactant, which is used as softener in fabric care. The initial steps of the catabolism were investigated in cell-free extracts of the bacterial strain MM 1 able to grow ...
Egli, Thomas, Hofer, Martina, Kaech, Andres, Rentsch, Daniel, Schnider, Christian   +4 more
core