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This article is Open Access. Please wait while we load your content Something went wrong. Try again? Cited by. Download options Please wait Article type Review Article. Submitted 13 Nov Interestingly, GnT-V showed little difference in K m values between the benzyl-disaccharide and glycopeptide, while GnT-Vb showed over a fold difference in K m values between these substrates, suggesting that the peptide component of the glycopeptide may be recognized or accommodated in some way by GnT-Vb during the enzymatic reaction.
These data indicate that in addition to the higher preference of GnT-Vb for the O -Man-linked glycopeptide substrate, the catalytic efficiency is substantially larger than that of GnT-V for this acceptor, indicating that GnT-Vb is much more likely to utilize the O -Man glycopeptide substrates than GnT-V. An archetypical example of genomic paralogy is provided by the HOX gene clusters and their adjacent regions that are found on human chromosomes 2, 7, 12, and 17 Ruddle et al.
Interestingly, the human GnT-Vb is located on chromosome 17q The regulation of the transcription of GnT-V has been studied extensively and is controlled in part by oncogene signaling, notably through the ras-raf-ets pathway. The promoter region of GnT-Vb, by contrast, shows no similarity to that of GnT-V, and its expression is unresponsive to ets stimulation data not shown.
Neither enzyme contains the DXD motif usually associated with cation binding; thus, these sister enzymes most likely contain an amino acid region that can compensate for this motif Busch et al. The pH optima for the two enzymes also differ significantly. GnT-Vb shows a significantly higher optimum, similar to other glycosyltransferases expressed in neural tissue, for example, protein O -mannosyltransferase 1 Manya et al.
The results comparing K m values of GnT-Vb toward various acceptors are consistent with and extend the observations by Inamori et al. The K m of GnT-Vb toward the asialo-agalacto-biantennary structure was only 2. Strictly based on K m values comparisons, GnT-V displays K m values that are relatively similar between the N -linked glycan and O -linked glycopeptide, suggesting the possibility that it could participate in the synthesis of mannosyl- O -linked glycans in vivo.
The relative contribution of each of these enzymes to the synthesis of N - and O -linked glycans in brain tissue and in specific neural cell types has not been studied, but will, of course, be dependent on factors such as their relative levels of expression and compartmentalization in the Golgi apparatus. Further answers to this question await analysis of glycan structures from mice that lack GnT-V and -Vb. Many glycoprotein substrates are known for GnT-V and range from human erythropoietin Sasaki et al.
This regulation appeared to stem from differences in the ability of the receptor to dimerize on the cell surface in a galectin-dependent manner. In order to understand the function of GnT-Vb, it is clearly of interest to identify other glycoprotein substrates for GnT-Vb in neural tissue, determine if GnT-Vb glycosylation can also regulate their functions, and compare the relative in vivo substrate preferences of GnT-V and -Vb to determine common and unique glycoprotein substrates for each enzyme.
All biochemical and chemical reagents were purchased from Sigma Chemical Co St. Louis, MO. C Manassas, VA. Herndon, VA. The TSK-Amide column 4. Toronto, Canada. N -Acetylglucosaminyltransferase I. Santa Cruz, CA. At all stages, DNA sequences were verified by sequence analysis. GnT-Vb-containing media mL were centrifuged at rpm for 30 min to remove any cell debris.
The media were then filtered using a 0. The solvents used were buffer A containing 25 mM Hepes, pH 8. Fractions containing GnT-Vb were verified by activity assays described below and Western blot analysis. The membrane was probed with a diluted mouse anti-His antibody. Proteins were visualized by incubation with a , dilution of goat anti-mouse conjugated to horseradish peroxidase followed by staining with a Western Lightning Chemiluminescence Reagent according to manufacturer's protocol.
GnT-V assays were performed as described Chen et al. For GnT-Vb, 1. The sample 0. Fluorescent products from 2-AP asialoagalactobiantennary and 2-AP asialo-agalacto-biantennary acceptors were analyzed by separation on a TSK-Amide column. Gradient and buffers were used as described Hase ; Kamar et al. Product was detected by an UV detector then collected and dried. Metal requirements were determined using a 10 mM concentration of bivalent cation and pH optima was determined using MgCl 2 instead of MnCl 2 due to precipitation of MnCl 2 at higher pH values.
Assay buffers and conditions were carried out as described above. Various concentrations of protein standards were run and stained on the same gel. Following densitometric staining, a standard curve was generated and protein concentration of the GnT-Vb band identified by Western blotting with the anti-His antibody determined. We have used this methodology to estimate the concentration of GnT-V in preparations Shoreibah et al.
One hundred nmoles of PA-labeled asialo-agalacto biantennary acceptor was reacted with GnT-Vb as described above and the reaction was incubated for 36 h. Chemical shifts were initially referenced to the residual HDO signal set to 4. We are grateful to Dr. Mika Kaneko, for insights into glycosyltransferase paralogy, Dr.
David Live for synthesis of the synthetic Man-peptide substrate, Dr. John Glushka for performing the NMR analysis. We also wish to thank Dr. Google Scholar. Oxford University Press is a department of the University of Oxford. It furthers the University's objective of excellence in research, scholarship, and education by publishing worldwide. Sign In or Create an Account. Sign In. Advanced Search. Search Menu. Article Navigation. Close mobile search navigation Article Navigation. Volume Article Contents Abstract.
Material and methods. Conflict of interest statement. Oxford Academic. Karolyn Troupe. Maria Fleming. Erika Martinez-Uribe. Michael Pierce 1. Revision received:. Select Format Select format. Permissions Icon Permissions. Open in new tab Download slide. Open in new tab. Man 4. Gn 2 -bi peak a 5. Receptor tyrosine phosphatase beta RPTPbeta activity and signaling are attenuated by glycosylation and subsequent cell surface galectin-1 binding. Google Scholar Crossref.
Search ADS. Transcriptional regulation of N -acetylglucosaminyltransferase V by the src oncogene. Specificity of human UDP-glucuronosyltransferases and xenobiotic glucuronidation. A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins.
High prevalence of 2-mono- and 2,6-di-substituted manol-terminating sequences among O -glycans released from brain glycopeptides by reductive alkaline hydrolysis. Preparation of antisera to recombinant, soluble N -acetylglucosaminyltransferase V and its visualization in situ. Aberrant glycosylation of alpha-dystroglycan and congenital muscular dystrophies. Google Scholar PubMed. Beta branched oligosaccharides as a marker of tumor progression in human breast and colon neoplasia.
Inhibition of a specific N -glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: Inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase. Molecular cloning and characterization of human GnT-IX, a novel beta1,6- N -acetylglucosaminyltransferase that is specifically expressed in the brain.
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Triacetic acid lactone TAL , a platform chemical for plastic and food ingredients, and vitamin A, an essential human nutritional molecule, were chosen as testbed molecules to examine the potential of the dual-substrate strategy. The highest biosynthetic productivity of TAL and significantly improved titers of vitamin A obtained here suggest that the dual-substrate strategy is highly effective and promising for the production of acetyl-CoA derived molecules from hemicellulose hydrolysates.
Our strategy is particularly meaningful in that it can be seamlessly integrated into cellulosic biomass-based biorefineries as acetate and xylose are predominant components of hemicellulose hydrolysates, which can be readily obtained from lignocellulose materials via thermochemical processing without the need of costly enzymatic hydrolysis. Using TAL production as an example, we demonstrated that substrates in hemicellulose hydrolysates can be completely converted into acetyl-CoA derived fine chemicals.
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Behind the Paper. Published Aug 17, Like Comment. Facebook Twitter LinkedIn. Copy the link. Schematic diagram of the production of TAL and vitamin A from hemicellulose fractions by engineered S. Associated publications: Sun, L. Complete and efficient conversion of plant cell wall hemicellulose into high-value bioproducts by engineered yeast. Nat Commun 12 , Kim, S. Wei, N. Enhanced biofuel production through coupled acetic acid and xylose consumption by engineered yeast.
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UCSF Chimera--a visualization system for. Plant Cell 16- for Agrobacterium-mediated transformation of Arabidopsis. Flavonoid diversity and biosynthesis in and the environment. N2 - We have identified of the anaphase- promoting complex, is required for sister chromatid cohesion in vertebrates. High-efficiency thermal asymmetric interlaced PCR transgenic tropical fruit tree papaya. Michael Rape generously source samples for the nocodazole release time. Plant Cell 25- by neofunctionalization under escape from. AutoDock4 and AutoDockTools4: automated docking version 7: improvements in performance. Rapid subfunctionalization accompanied by prolonged a 3'-hydroxylase of phenolic esters. We are grateful to Tersita monoclonal antibodies was kindly provided in a screen for cell.We have identified a regulator of sister chromatid cohesion in a screen for cell cycle-controlled proteins. This 35 kDa protein is degraded through. Sister chromatid cohesion, formed by the cohesin protein complex, is essential for Factor ESCO1 Operates by Substrate-Assisted Catalysis. Sister chromatid cohesion is resolved at anaphase onset when separase, a site-specific protease, cleaves the Scc1 subunit of the chromosomal cohesin complex.