Cellulases belong to the large family of glycosyl hydrolases (GHs) and are produced by a variety of bacteria and fungi. These extracellular enzymes act as endoglucanases (EGs), cellobiohydrolases or beta-glucosidases. In this paper, we describe molecular screening for EGs from the GH family 12. Using three homologous sequence boxes deduced from five previously known members of the family, we analysed 22 cellulase-producing fungal strains obtained from a diverse area of the fungal kingdom. Polymerase chain reactions using degenerate primers designed to the homologous protein boxes were used to identify the family 12 homologues. Several fungi showed the presence of multiple versions of the gene, while amino acid sequence analysis showed diversity in 15 novel members of the family, ranging from 26% to 96% similarity. Our sequence analysis shows that the phylogenetic tree of family 12 EGs can be divided into four subfamilies: 12-1 (fungal group I), 12-2 (fungal group II), 12-3 ( Streptomyces group in which Rhodothermus marinus fits) and 12-4 ( Thermophiles group). Erwinia carotovora may form a new subgroup.
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http://dx.doi.org/10.1007/s00294-002-0290-2 | DOI Listing |
Pediatr Neurol
December 2024
Zickler Family Prenatal Pediatrics Institute, Children's National Hospital, Washington, District of Columbia; Department of Neurology, The George Washington University School of Medicine and Health Sciences, Washington, District of Columbia; Department of Pediatrics, The George Washington University School of Medicine and Health Sciences, Washington, District of Columbia. Electronic address:
Background: Congenital disorders of glycosylation (CDG) are a group of metabolic disorders related to dysfunctional glycoprotein and glycolipid biosynthesis. ALG11-related CDG is a rare member of this group, characterized by severe neurodevelopmental impairment, progressive microcephaly, sensorineural hearing loss, and epilepsy. The objective of this report is to provide an update on the phenotype and brain magnetic resonance imaging (MRI) at age seven years for a patient initially described in early infancy with fetal brain disruption sequence.
View Article and Find Full Text PDFJ Exp Bot
January 2025
Vegetable and Fruit Improvement Center and Department of Horticultural Sciences Texas A&M University, College Station, TX 77843, USA.
Complex N-glycans are asparagine (N)-linked branched sugar chains attached to secretory proteins in eukaryotes. They are produced by modification of N-linked oligosaccharide structures in the endoplasmic reticulum (ER) and Golgi apparatus. Complex N-glycans formed in the Golgi apparatus are often assigned specific roles unique to the host organism, with their roles in plants remaining largely unknown.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Landscape Architecture and Art, Northwest A & F University, Yangling, Shaanxi 712100, China; State Key Laboratory of Crop Stress Resistance and High-Efficiency Production, Northwest A & F University, Yangling, Shaanxi 712100, China. Electronic address:
Glycosylation modification of anthocyanins is important as a preceding step to acylation modification. Cyanidin-3-O-(p-coumaroyl)glucoside-5-O-malonylglucoside (Cy3pCG5MaG) is one of the major anthocyanin substances in blue-flowered grape hyacinth, but its 5-position glycosylation is unknown. Here, we identified two glycoside hydrolase family 1 genes, MaAGGT1 and MaAGGT5, which use acyl-glucose as a donor and are involved in the glycosylation modification of anthocyanins in grape hyacinth.
View Article and Find Full Text PDFPlant Physiol Biochem
January 2025
College of Agriculture & Biotechnology, Zhejiang University, Hangzhou, 310058, China; Zhejiang Key Laboratory of Horticultural Crop Quality Improvement, Zhejiang University, Hangzhou, 310058, China. Electronic address:
Flavonol glycosides are secondary metabolites important for plant development and stress defense such as UV-B irradiation. UDP-glycosyltransferase (UGT) catalyzes the last step in the biosynthesis of flavonol glycosides. Eriobotrya japonica is abundant in flavonol glycosides, but UGTs responsible for accumulation of flavonol glycosides remain unknown.
View Article and Find Full Text PDFAnimals (Basel)
December 2024
Departamento de Biología Celular e Histología, Facultad de Medicina y de Enfermería, Universidad de Murcia, 30120 Murcia, Spain.
OGP, encoded by the gene, is the major non-serum oviductal protein in most mammals. In the genome of , has been identified as a pseudogene. However, presents a functional gene.
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