Results 191 to 200 of about 7,719 (211)
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Uridine diphosphate release mechanism in O-N-acetylglucosamine (O-GlcNAc) transferase catalysis
Biochimica et Biophysica Acta (BBA) - General Subjects, 2019O-linked N-acetylglucosamine transferase (OGT) is an essential enzyme that catalyzes the covalent bonding of N-acetylglucosamine (GlcNAc) to the hydroxyl group of a serine or threonine in the target protein. It plays an important role in many important cellular physiological catalytic reactions.
Nai, She +4 more
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Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5'-diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminylphosphotransferase activity. [PDF]
Journal of Clinical Investigation, 1981 Newly synthesized acid hydrolases, destined for transport to lysosomes, acquire a phosphomannosyl targeting signal by the transfer of N-acetylglucosamine 1-phosphate from uridine 5'-diphosphate (UDP)-N-acetylglucosamine to a mannose residue of the acid hydrolase followed by removal of the outer, phosphodiester-linked N-acetylglucosamine to expose 6 ...
Marc L Reitman, Stuart Kornfeld
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Pest Management Science, 2021
AbstractBACKGROUNDUridine diphosphate‐N‐acetylglucosamine (UDP‐GlcNAc) diphosphorylase (UAP) catalyzes the formation of UDP‐GlcNAc, the precursor for the production of chitin in ectodermally derived epidermal cells and midgut, for GlcNAcylation of proteins and for generation of glycosyl‐phosphatidyl‐inositol anchors in all tissues in Drosophila ...
Lin‐Hong Jiang +4 more
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AbstractBACKGROUNDUridine diphosphate‐N‐acetylglucosamine (UDP‐GlcNAc) diphosphorylase (UAP) catalyzes the formation of UDP‐GlcNAc, the precursor for the production of chitin in ectodermally derived epidermal cells and midgut, for GlcNAcylation of proteins and for generation of glycosyl‐phosphatidyl‐inositol anchors in all tissues in Drosophila ...
Lin‐Hong Jiang +4 more
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Journal of Bacteriology, 1974
The specific activity of uridine diphosphate N -acetylglucosamine-4-epimerase increases during spherulation of Physarum polycephalum , a process that involves the synthesis of galactosamine walls. This increase is prevented by the addition of cycloheximide.
W R, Hiatt, H R, Whiteley
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The specific activity of uridine diphosphate N -acetylglucosamine-4-epimerase increases during spherulation of Physarum polycephalum , a process that involves the synthesis of galactosamine walls. This increase is prevented by the addition of cycloheximide.
W R, Hiatt, H R, Whiteley
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Canadian Journal of Microbiology, 1979
Uridine diphosphate N-acetylglucosamine pyrophosphorylase (EC. 2.7.7.23) of Neurospora crassa has been purified approximately 210-fold with dithiothreitol as the stabilizing agent by use of chromatographic techniques. The enzyme preparation appeared to be homogeneous when subjected to electrophoresis.
K, Yamamoto +3 more
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Uridine diphosphate N-acetylglucosamine pyrophosphorylase (EC. 2.7.7.23) of Neurospora crassa has been purified approximately 210-fold with dithiothreitol as the stabilizing agent by use of chromatographic techniques. The enzyme preparation appeared to be homogeneous when subjected to electrophoresis.
K, Yamamoto +3 more
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European Journal of Biochemistry, 1994
Uptake and metabolism of uridine diphosphate N‐acetylglucosamine (UDP‐GlcNAc) by rough‐endoplasmic‐reticulum (rER)‐derived vesicles was studied. Analysis of the molecular species, double‐label experiments, cis‐inhibition and trans‐stimulation experiments revealed that uptake represented entry of intact UDP‐GlcNAc into the microsomal lumen.
X, Bossuyt, N, Blanckaert
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Uptake and metabolism of uridine diphosphate N‐acetylglucosamine (UDP‐GlcNAc) by rough‐endoplasmic‐reticulum (rER)‐derived vesicles was studied. Analysis of the molecular species, double‐label experiments, cis‐inhibition and trans‐stimulation experiments revealed that uptake represented entry of intact UDP‐GlcNAc into the microsomal lumen.
X, Bossuyt, N, Blanckaert
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Journal of Mass Spectrometry, 2005
AbstractUridine 5′‐diphospho‐N‐acetylglucosamine (UDP‐GlcNAc) is the final product of hexosamine biosynthetic pathway (HSP) and the donor substrate for the modification of nucleocytoplasmic proteins at serine and threonine residues with N‐acetylglucosamine (GlcNAc) catalyzed by O‐GlcNAc transferase (OGT).
Hua-Dong, Liu +4 more
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AbstractUridine 5′‐diphospho‐N‐acetylglucosamine (UDP‐GlcNAc) is the final product of hexosamine biosynthetic pathway (HSP) and the donor substrate for the modification of nucleocytoplasmic proteins at serine and threonine residues with N‐acetylglucosamine (GlcNAc) catalyzed by O‐GlcNAc transferase (OGT).
Hua-Dong, Liu +4 more
openaire +2 more sources