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The vacuolar phosphatases PAP26 and HIIA2.1 hydrolyze 5'-, 3'-, and 2'-nucleotides derived from RNA degradation.
Plant Physiol
January 2025
Leibniz Universität Hannover, Department of Molecular Nutrition and Biochemistry of Plants, Herrenhäuser Str. 2, 30419 Hannover, Germany.
The vacuole is an important site for RNA degradation. Autophagy delivers RNA to the vacuole, where the vacuolar T2 RNase Ribonuclease 2 (RNS2) plays a major role in RNA catabolism. The presumed products of RNS2 activity are 3'-nucleoside monophosphates (3'-NMPs).
View Article and Find Full Text PDFInhibition of chondroitin sulphate-degrading enzyme Chondroitinase ABC by dextran sulphate.
Glycoconj J
January 2025
School of Natural Sciences, Faculty of Science and Engineering, Macquarie University, Sydney, NSW, 2109, Australia.
Chondroitin sulphate (CS) is a sulphated glycosaminoglycan (GAG) polysaccharide found on proteoglycans (CSPGs) in extracellular and pericellular matrices. Chondroitinase ABC (CSase ABC) derived from Proteus vulgaris is an enzyme that has gained attention for the capacity to cleave chondroitin sulphate (CS) glycosaminoglycans (GAG) from various proteoglycans such as Aggrecan, Neurocan, Decorin etc. The substrate specificity of CSase ABC is well-known for targeting various structural motifs of CS chains and has gained popularity in the field of neuro-regeneration by selective degradation of CS GAG chains.
View Article and Find Full Text PDFEvolution and Functional Diversification of Serine Racemase Homologs in Bacteria.
J Mol Evol
January 2025
Department of Plant and Soil Sciences, 311 Plant Science Building, University of Kentucky, Lexington, KY, 40546-0312, USA.
Amino acid racemases catalyze the interconversion of L- and D-amino acids, maintaining intracellular levels of both D- and L-amino acids. While alanine and glutamate racemases are widespread in bacteria, serine racemase (SerR) is predominantly found in animals. Recently, homologs of animal SerR were reported in some bacterial genomes, but their evolutionary distribution and functional roles remain poorly understood.
View Article and Find Full Text PDFA unique substrate specificity of PonAAS2, an aromatic aldehyde synthase, involved in a phytohormone auxin biosynthesis in a gall-inducing sawfly Euura sp. "Pontania".
Biosci Biotechnol Biochem
January 2025
Advanced Analysis Center, National Agriculture and Food Research Organization, 2-1-2 Kannondai, Tsukuba, Japan.
The aromatic aldehyde synthase (AAS), PonAAS2, from the gall-inducing sawfly has been identified as a biosynthetic enzyme for indole-3-acetic acid (IAA), a key molecule of the plant hormone auxin, which is thought to play a role in gall induction. Unlike other insect AASs that convert Dopa, PonAAS2 uniquely converts L-tryptophan (Trp) into indole-3-acetaldehyde, a precursor of IAA. In this study, an examination of AAS enzymes from various insect species revealed that the ability to convert Trp has been acquired in only a very limited taxonomic group.
View Article and Find Full Text PDFStructure and function of a β-1,2-galactosidase from Bacteroides xylanisolvens, an intestinal bacterium.
Commun Biol
January 2025
Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan.
Galactosides are major carbohydrates that are found in plant cell walls and various prebiotic oligosaccharides. Studying the detailed biochemical functions of β-galactosidases in degrading these carbohydrates is important. In particular, identifying β-galactosidases with new substrate specificities could help in the production of potentially beneficial oligosaccharides.
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