Results 11 to 20 of about 2,535 (131)

UDP-glucuronate carboxy-lyase in cultured chondrocytes.

Journal of Biological Chemistry, 1977
UDP-glucuronate carboxy-lyase has been demonstrated in chick chondrocytes in tissue culture. It occurs in the particulate fraction, and its activity is stimulated by exogenous NAD. The enzyme is allosterically activated by UDP-glucuronate and inhibited by UDP-xylose, n Values of 2.8 indicate positive cooperativity of at least three interacting sites on
K. V. John, Nancy B. Schwartz, Helmut Ankel   +2 more
openalex   +4 more sources

Functional and structural characterization of Stenotrophomonas maltophilia EntB, an unusual form of isochorismatase for siderophore synthesis. [PDF]

Acta Crystallogr F Struct Biol Commun
The crystal structure of S. maltophilia EntB revealed an unusual form of isochorismate lyase that is involved in siderophore biosynthesis.Clinical and environmental isolates of Stenotrophomonas maltophilia produce an enterobactin‐like siderophore that promotes bacterial growth under low‐iron conditions.
Nas MY, Gabell J, Inniss N, Minasov G, Shuvalova L, Satchell KJF, Cianciotto NP.   +6 more
europepmc   +2 more sources

α/β Hydrolases: Toward Unraveling Entangled Classification. [PDF]

Proteins
ABSTRACT α/β Hydrolase‐like enzymes form a large and functionally diverse superfamily of proteins. Despite retaining a conserved structural core consisting of an eight‐stranded, central β‐sheet flanked with six α‐helices, they display a modular architecture allowing them to perform a variety of functions, like esterases, lipases, peptidases, epoxidases,
Ozhelvaci F, Steczkiewicz K.
europepmc   +2 more sources

Intricate Regulation of Sphingolipid Biosynthesis: An In‐Depth Look Into ORMDL‐Mediated Regulation of Serine Palmitoyltransferase

BioEssays, EarlyView.
Multiple enzymes play a crucial role in regulating the biosynthesis of de novo sphingolipids. This regulation starts with the rate‐limiting enzyme, serine palmitoyltransferase (SPT), which catalyzes the first step of the pathway. Disruptions in this regulatory process can lead to serious diseases.
Usha Mahawar, Binks Wattenberg
wiley   +1 more source

Identification of a l‐Threonine‐Utilizing Hydrazine Synthetase for Thrazarine Biosynthesis in Streptomyces coerulescens MH802‐fF5

ChemBioChem, EarlyView.
A putative thrazarine biosynthetic gene cluster is discovered in the genome sequence of Streptomyces coerulescens MH802‐fF5. In vivo and in vitro analyses of ThzN, a hydrazine synthetase with cupin and methionyl‐tRNA synthetase‐like domains encoded in the cluster, showed that it synthesizes a key intermediate of thrazarine by catalyzing condensation ...
Yusuke Shikai, Hideyuki Muramatsu, Masayuki Igarashi, Yohei Katsuyama, Yasuo Ohnishi   +4 more
wiley   +1 more source

In Hyphomicrobium denitrificans Two Related Sulfane‐Sulfur Responsive Transcriptional Repressors Regulate Thiosulfate Oxidation and Have a Deep Impact on Nitrate Respiration and Anaerobic Biosyntheses

Molecular Microbiology, EarlyView.
In Hyphomicrobium denitrificans, the use of thiosulfate as a supplemental electron donor is regulated by two homologous sulfane‐sulfur responsive ArsR‐type transcriptional repressors, sHdrR and SoxR, that act cooperatively. Remarkably, the regulation by sHdrR/SoxR extends far beyond sulfur oxidation and deeply affects anaerobic metabolism, particularly
Jingjing Li, Nora E. Schmitte, Kaya Törkel, Christiane Dahl   +3 more
wiley   +1 more source

Re‐evaluation of neotame (E 961) as food additive

EFSA Journal, Volume 23, Issue 7, July 2025.
Abstract The present opinion deals with the re‐evaluation of neotame (E 961) as a food additive. Neotame is the chemically manufactured compound N‐[N‐(3,3‐dimethylbutyl)‐l‐α‐aspartyl]‐l‐phenylalanine 1‐methyl ester. The main impurity of neotame (E 961) is also a degradation product (de‐esterified form), N‐[N‐(3,3‐dimethylbutyl)‐l‐α‐aspartyl]‐L ...
EFSA Panel on Food Additives and Flavourings (FAF), Laurence Castle, Monica Andreassen, Gabriele Aquilina, Maria Lourdes Bastos, Polly Boon, Biagio Fallico, Reginald FitzGerald, Maria Jose Frutos Fernandez, Bettina Grasl‐Kraupp, Ursula Gundert‐Remy, Rainer Gürtler, Eric Houdeau, Marcin Kurek, Henriqueta Louro, Patricia Morales, Sabina Passamonti, Monika Batke, Ellen Bruzell, James Chipman, Riccardo Crebelli, Cristina Fortes, Peter Fürst, Eric Gaffet, Cheyns Karlien, Thorhallur Halldorsson, Jean‐Charles Leblanc, Oliver Lindtner, Katrin Loeschner, Jan Mast, Manuela Mirat, Alicja Mortensen, Anna Undas, Matthew Wright, Stefania Barmaz, Consuelo Civitella, Jose Cortiñas Abrahantes, Pauline Le Gall, Elena Mazzoli, Agnieszka Mech, Josef Daniel Rasinger, Ana Rincon, Francesca Riolo, Camilla Smeraldi, Alexandra Tard, Panagiota Zakidou, Federica Lodi   +46 more
wiley   +1 more source

Purine Chemistry in the Early RNA World at the Origins of Life: From RNA and Nucleobases Lesions to Current Key Metabolic Routes

ChemBioChem, Volume 26, Issue 11, June 3, 2025.
In the nascent processes of the beginnings and evolution of life, nucleobases and especially purines, ribonucleos(t)ides and primitive RNAs have been continuously modified. A RNA‐peptide world and key metabolic pathways probably have emerged from the corresponding chemical modifications resulting from adenine deamination, purine alkylation and ...
Jean‐Luc Décout, Marie‐Christine Maurel   +1 more
wiley   +1 more source

New glycoside hydrolase families of β‐1,2‐glucanases

Protein Science, Volume 34, Issue 6, June 2025.
Abstract β‐1,2‐Glucans are natural glucose polymers produced by bacteria and play important physiological roles, including as symbiotic or pathogenic factors and in osmoregulation. Glycoside hydrolase (GH) families related to β‐1,2‐glucan metabolism (GH144, GH162, and GH189) have recently been created by identification of two β‐1,2‐glucanases and a β‐1,
Masahiro Nakajima, Nobukiyo Tanaka, Sei Motouchi, Kaito Kobayashi, Hisaka Shimizu, Koichi Abe, Naoya Hosoyamada, Naoya Abara, Naoko Morimoto, Narumi Hiramoto, Ryosuke Nakata, Akira Takashima, Marie Hosoki, Soichiro Suzuki, Kako Shikano, Takahiro Fujimaru, Shiho Imagawa, Yukiya Kawadai, Ziyu Wang, Yoshinao Kitano, Takanori Nihira, Hiroyuki Nakai, Hayao Taguchi   +22 more
wiley   +1 more source

Elucidating the Mechanism of Temporal Adaptation to Hydrogen Peroxide‐Induced Oxidative Stress in Corynebacterium glutamicum

Microbial Biotechnology, Volume 18, Issue 6, June 2025.
In this study, RNA‐seq was employed to investigate the temporal transcriptional response of C. glutamicum ATCC 13032 to external H2O2 at 720 mM (2.45% w/w). The results reveal significant changes in gene expression across multiple pathways, including peroxide scavenging, central metabolism, sulphur and iron metabolism, amino acid biosynthesis, and DNA ...
Chang Yu, Wenjing Hu, Xiaoyu Li, Yu Lei, Dandan Gao, Meng Wang, Ping Zheng, Yan Zhu, Jibin Sun   +8 more
wiley   +1 more source