Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Endo-N-acetyl-beta-D-glucosaminidase (ENGase, EC 3.2.1.96) and peptide-N4-(N-acetyl-beta-D-glucosaminyl) asparagine amidase (PNGase, EC 3.5.1.52) activities were monitored during germination and postgerminative development in Raphanus sativus. The PNGase activity was found in dry seeds and its level was constant during germination and postgermination. The ENGase activity was first detected about 18 hr after the start of imbibition (HAI) and displayed a maximum level at 36 HAI. After 36 HAI the production of both enzymes was constant until days 4-5. Both enzymes displayed substrate specificities corresponding to the potential glycoprotein substrates found in plants. They are in agreement (i) with the hypothesis that ENGase and PNGase are at the origin of the production of 'unconjugated N-glycans' and (ii) with the possibility that protein activity could be regulated by the removal of N-glycans.
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PMID:Endo-N-acetyl-beta-D-glucosaminidase and peptide-N4-(N-acetyl-glucosaminyl) asparagine amidase activities during germination of Raphanus sativus. 757 49

The asparagine-linked oligosaccharides from an adult female mouse submandibular gland mucin were released by treatment with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F or endo-beta-N-acetylglucosaminidase H. Endo-beta-N-acetylglucosaminidase H appeared to be more effective at releasing the asparagine-linked oligosaccharides from this mucin than was peptide-N4-(N-acetyl-beta-glucosaminyl)-asparagine amidase F. After quantitative reductive labelling with the fluorophore, 8-aminonaphthalene-1,3,6-sulphonic acid, the oligosaccharides were separated by polyacrylamide gel electrophoresis and isolated. The individual oligosaccharides were sequenced by a battery of recombinant exoglycosidases. Approximately 50% of the oligosaccharides were of the high-mannose type. The five-mannose member of this family was the most prevalent. The second group of oligosaccharides were of the non-bisected hybrid type. No complex asparagine-linked oligosaccharides were detected. The hybrids exhibited both biantennary and triantennary branching patterns. The triantennary hybrid was the most common hybrid at > 30% of all oligosaccharides. With approximately 98% of the hybrid oligosaccharides sialylated and all lacking a bisecting N-acetylglucosamine, these oligosaccharides as a group have been only rarely observed in other glycoproteins. The fully sialylated triantennary hybrid may be unique.
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PMID:Characterization of asparagine-linked oligosaccharides on a mouse submandibular mucin. 856 46

The occurrence of two enzymes performing de-N-glycosylation of glycoproteins, namely, endo-N-acetyl-beta-D-glucosaminidase (ENGase, EC 3.2.1.96) and peptide-N(4)-(N-acetyl-beta-D-glucosaminyl) asparagine amidase (PNGase, EC 3.5.1.52) was investigated in barley, cv. Plaisant (a winter six rowed variety). The dry grain showed both activities according to the HPLC detection of the hydrolysis of fluorescent resorufin-labelled substrates. However, PNGase activity was 16-fold higher than ENGase activity. During germination, both activities increased, PNGase by only 1.5-fold compared to nearly 4.8-fold for ENGase over the 4 d following imbibition. The localization of these activities within the grain showed that the major contribution of PNGase was due to the endosperm, typically representing over 90% of the whole grain activity. In contrast, ENGase activity was especially high in the embryo and, later, in the developing plantlet (10-fold higher than in the endosperm), particularly in the rootlets and scutellum. In developing spikes, PNGase activity was 5.6-fold higher than in the leaves, but similar ENGase activity was measured in both organs. During grain formation, PNGase activity followed dry matter increase together with endosperm development. In contrast, ENGase activity dropped by 66% at the beginning of grain filling before stabilizing until harvest. The occurrence of de-N-glycosylation-performing enzymes throughout the development of barley raises the question of the nature of their natural substrates. Moreover, the prevalence of one of these enzymes over the other depending on the organ and the developmental stage, could represent the first evidence of specific functions for each enzyme.
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PMID:Evidence of two enzymes performing the de-N-glycosylation of proteins in barley: expression during germination, localization within the grain and set-up during grain formation. 1094 9

The activities of the de-N-glycosylation enzymes endo-N-acetyl- [beta]-D-glucosaminidase (ENGase; EC 3.2.1.96) and peptide-N4- (N-acetyl-[beta]-D-glucosaminyl) asparagine amidase (PNGase; EC 3.5.1.52) were monitored during germination and postgerminative development in radish (Raphanus sativus L. cv Flamboyant). The ENGase activity was detected only during postgermination, whereas the PNGase activity was present at high levels in both stages. When germination was inhibited with abscisic acid or cycloheximide, PNGase activity was detected at a basic level and ENGase activity was not detected at all. PNGase is present as an active protein in dry seeds and is apparently synthesized during seed formation. Conversely, the absence of ENGase in dry seeds suggests that its activity is dependent on the protein synthesis that occurs during and after germination. Treatment with gibberellic acid confirmed the production of both de-N-glycosylation enzymes after germination, and demonstrated a temporal delay between the production of the two enzymes during this period. Our results suggest that the two de-N-glycosylation enzymes are differentially regulated during plant development.
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PMID:Regulation of De-N-Glycosylation Enzymes in Germinating Radish Seeds. 1222 89