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1 cal polymer from UDP-N-acetylglucosamine and UDP-glucuronic acid.
2 nal UDP-glycosyltransferase UGT co-substrate UDP-glucuronic acid.
3 ), UDP-N-acetylglucosamine (UDP-GlcNAc), and UDP-glucuronic acid.
4 lyzes two oxidations of UDP-glucose to yield UDP-glucuronic acid.
5 ntermediate that is synthesized by ArnA from UDP-glucuronic acid.
6 pose a pathway for l-Ara4N biosynthesis from UDP-glucuronic acid.
9 ities for the sugar donors UDP-galactose and UDP-glucuronic acid, although UDP-glucose was always pre
10 uccessive oxidations of UDP-glucose to yield UDP-glucuronic acid, an essential precursor for matrix p
11 UDP-glucose dehydrogenase (Ugd) generates UDP-glucuronic acid, an important precursor for the prod
12 copyranosiduronic acids (glucuronides) using UDP-glucuronic acid and acceptor substrates such as drug
13 (+)-dependent oxidation of the 4''-OH of the UDP-glucuronic acid and decarboxylation of the UDP-4-ket
14 rt to its ability to sequester intracellular UDP-glucuronic acid and inhibition of hyaluronan synthas
15 showed that the resulting mutant lacked both UDP-glucuronic acid and its downstream product, UDP-xylo
16 ponsible for the oxidation of UDP-glucose to UDP-glucuronic acid and its subsequent decarboxylation t
17 y, we propose a binding model for NAD(+) and UDP-glucuronic acid and the involvement of residues T(43
19 s that synthesize the building blocks of HA, UDP-Glucuronic acid and UDP-N-Acetyl-Glucosamine, as wel
20 HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as subst
21 rategy, we used purified S. equisimilis HAS, UDP-glucuronic acid, and UDP[beta-32P]-Glc-NAc to radiol
24 .8-A resolution apo crystal structure of the UDP-glucuronic acid binding domain of human UGT isoform
25 he encoded protein is closely related to the UDP-glucuronic acid binding site consensus sequence, and
28 s at residues predicted to interact with the UDP-glucuronic acid cofactor exhibited significantly imp
29 n the content of UDP-N-acetylhexosamines and UDP-glucuronic acid, correlating with the expression lev
31 Biosynthesis of UDP-xylose is mediated by UDP-glucuronic acid decarboxylase, which converts UDP-gl
34 m adenosine diphosphate-activated platelets, UDP-glucuronic acid-dependent bilirubin conjugation was
37 d C-4" oxidation and C-6" decarboxylation of UDP-glucuronic acid, followed by the C-4" transamination
38 ion and C-6" decarboxylation of [alpha-(32)P]UDP-glucuronic acid, followed by transamination to gener
39 Extracts of the mutants completely lacked UDP-glucuronic acid:Galbeta1,3Gal-R glucuronosyltransfer
40 AS) is a membrane-bound enzyme that utilizes UDP-glucuronic acid (GlcUA) and UDP-GlcNAc to synthesize
41 ae catalyzes sugar transfer from UDP-Glc and UDP-glucuronic acid (GlcUA) to a polymer with the repeat
48 ponents may be linked to the availability of UDP-glucuronic acid; therefore UGDH is an intriguing the
49 micals by linking glucuronic acid donated by UDP-glucuronic acid to a lipophilic acceptor substrate.
51 e unprecedented oxidative decarboxylation of UDP-glucuronic acid to form uridine 5'-(beta-l-threo-pen
52 AD(+)-dependent oxidative decarboxylation of UDP-glucuronic acid to generate a UDP-4'-keto-pentose su
53 (i) the NAD(+)-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose and (ii) the
55 e C. neoformans gene catalyzed conversion of UDP-glucuronic acid to UDP-xylose, as confirmed by NMR a
57 NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid to yield the UDP-4''-ketopentose, ur
58 y the authentic sugar nucleotide precursors, UDP-glucuronic acid (UDP-GlcA) and UDP-N-acetylglucosami
59 Api) together with UDP-xylose is formed from UDP-glucuronic acid (UDP-GlcA) by UDP-Api synthase (UAS)
62 alyzing (1) the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcA) to the UDP-4' '-ketopento
65 disaccharide units from the donor molecules UDP-glucuronic acid (UDP-GlcUA) and UDP-N-acetylglucosam
66 neumoniae requires UDP-glucose (UDP-Glc) and UDP-glucuronic acid (UDP-GlcUA) for production of the [3
67 he presence of protein-mediated transport of UDP-glucuronic acid (UDP-GlcUA) in rat liver endoplasmic
68 -d-GlcUA-(1-] from UDP-glucose (UDP-Glc) and UDP-glucuronic acid (UDP-GlcUA) is catalysed by the type
69 substrate for all glucuronidation reactions, UDP-glucuronic acid (UDP-GlcUA), was determined using a
70 yces cerevisiae expressing SQV-7 transported UDP-glucuronic acid, UDP-N-acetylgalactosamine, and UDP-
71 HA synthase for UDP-N-acetylglucosamine and UDP-glucuronic acid were estimated to be approximately 7
72 y catalyzes the conversion of UDP-glucose to UDP-glucuronic acid, which is essential for the biosynth
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