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General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability.

Angewandte Chemie (International ed. in English)

Fu X, Gadi MR, Wang S, Han J, Liu D, Chen X, Yin J, Li L.
PMID: 34661966
Angew Chem Int Ed Engl. 2021 Dec 13;60(51):26555-26560. doi: 10.1002/anie.202112574. Epub 2021 Nov 09.

Accessing large numbers of structurally diverse glycans and derivatives is essential to functional glycomics. We showed a general tolerance of galactosyltransferases toward uridine-diphosphate-galactosamine (UDP-GalN), which is not a commonly used sugar nucleotide donor. The property was harnessed to develop...

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Fu X, Gadi MR, Wang S, et al. General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability. Angew Chem Int Ed Engl. 2021;60(51):26555-26560doi: 10.1002/anie.202112574.
Fu, X., Gadi, M. R., Wang, S., Han, J., Liu, D., Chen, X., Yin, J., & Li, L. (2021). General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability. Angewandte Chemie (International ed. in English), 60(51), 26555-26560. https://doi.org/10.1002/anie.202112574
Fu, Xuan, et al. "General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability." Angewandte Chemie (International ed. in English) vol. 60,51 (2021): 26555-26560. doi: https://doi.org/10.1002/anie.202112574
Fu X, Gadi MR, Wang S, Han J, Liu D, Chen X, Yin J, Li L. General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability. Angew Chem Int Ed Engl. 2021 Dec 13;60(51):26555-26560. doi: 10.1002/anie.202112574. Epub 2021 Nov 09. PMID: 34661966.
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α(1-3)-Galactosyltransferase Inhibition Based on a New Type of Disubstrate Analogue.

Angewandte Chemie (International ed. in English)

Waldscheck B, Streiff M, Notz W, Kinzy W, Schmidt RR.
PMID: 29712256
Angew Chem Int Ed Engl. 2001 Nov 05;40(21):4007-4011. doi: 10.1002/1521-3773(20011105)40:21<4007::AID-ANIE4007>3.0.CO;2-F.

How do retaining glycosyltransferases function? To answer this question, UDP-Gal and galactose were covalently linked to form disubstrate analogues 1, of which surprisingly 1β and not 1α inhibited α(1-3)-galactosyltransferases very well. An understanding of this inhibition is a key...

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Waldscheck B, Streiff M, Notz W, et al. α(1-3)-Galactosyltransferase Inhibition Based on a New Type of Disubstrate Analogue. Angew Chem Int Ed Engl. 2001;40(21):4007-4011doi: 10.1002/1521-3773(20011105)40:21<4007::AID-ANIE4007>3.0.CO;2-F.
Waldscheck, B., Streiff, M., Notz, W., Kinzy, W., & Schmidt, R. R. (2001). α(1-3)-Galactosyltransferase Inhibition Based on a New Type of Disubstrate Analogue. Angewandte Chemie (International ed. in English), 40(21), 4007-4011. https://doi.org/10.1002/1521-3773(20011105)40:21<4007::AID-ANIE4007>3.0.CO;2-F
Waldscheck, Bernhard, et al. "α(1-3)-Galactosyltransferase Inhibition Based on a New Type of Disubstrate Analogue." Angewandte Chemie (International ed. in English) vol. 40,21 (2001): 4007-4011. doi: https://doi.org/10.1002/1521-3773(20011105)40:21<4007::AID-ANIE4007>3.0.CO;2-F
Waldscheck B, Streiff M, Notz W, Kinzy W, Schmidt RR. α(1-3)-Galactosyltransferase Inhibition Based on a New Type of Disubstrate Analogue. Angew Chem Int Ed Engl. 2001 Nov 05;40(21):4007-4011. doi: 10.1002/1521-3773(20011105)40:21<4007::AID-ANIE4007>3.0.CO;2-F. PMID: 29712256.
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Glycosylation of arabinogalactan-proteins essential for development in Arabidopsis.

Communicative & integrative biology

Showalter AM, Basu D.
PMID: 27489583
Commun Integr Biol. 2016 May 05;9(3):e1177687. doi: 10.1080/19420889.2016.1177687. eCollection 2016.

Arabinogalactan-proteins (AGPs) are ubiquitous cell wall components present throughout the plant kingdom. They are extensively post translationally modified by conversion of proline to hydroxyproline (Hyp) and by addition of arabinogalactan (AG) polysaccharides to Hyp residues. Two small gene subfamilies...

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Showalter AM, Basu D. Glycosylation of arabinogalactan-proteins essential for development in Arabidopsis. Commun Integr Biol. 2016;9(3):e1177687doi: 10.1080/19420889.2016.1177687.
Showalter, A. M., & Basu, D. (2016). Glycosylation of arabinogalactan-proteins essential for development in Arabidopsis. Communicative & integrative biology, 9(3), e1177687. https://doi.org/10.1080/19420889.2016.1177687
Showalter, Allan M, and Basu, Debarati. "Glycosylation of arabinogalactan-proteins essential for development in Arabidopsis." Communicative & integrative biology vol. 9,3 (2016): e1177687. doi: https://doi.org/10.1080/19420889.2016.1177687
Showalter AM, Basu D. Glycosylation of arabinogalactan-proteins essential for development in Arabidopsis. Commun Integr Biol. 2016 May 05;9(3):e1177687. doi: 10.1080/19420889.2016.1177687. eCollection 2016. PMID: 27489583; PMCID: PMC4951162.
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A phylogenetic view and functional annotation of the animal β1,3-glycosyltransferases of the GT31 CAZy family.

Glycobiology

Petit D, Teppa RE, Harduin-Lepers A.
PMID: 32886776
Glycobiology. 2021 Apr 01;31(3):243-259. doi: 10.1093/glycob/cwaa086.

The formation of β1,3-linkages on animal glycoconjugates is catalyzed by a subset of β1,3-glycosyltransferases grouped in the Carbohydrate-Active enZYmes family glycosyltransferase-31 (GT31). This family represents an extremely diverse set of β1,3-N-acetylglucosaminyltransferases [B3GNTs and Fringe β1,3-N-acetylglucosaminyltransferases], β1,3-N-acetylgalactosaminyltransferases (B3GALNTs), β1,3-galactosyltransferases [B3GALTs...

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Petit D, Teppa RE, Harduin-Lepers A. A phylogenetic view and functional annotation of the animal β1,3-glycosyltransferases of the GT31 CAZy family. Glycobiology. 2021;31(3):243-259doi: 10.1093/glycob/cwaa086.
Petit, D., Teppa, R. E., & Harduin-Lepers, A. (2021). A phylogenetic view and functional annotation of the animal β1,3-glycosyltransferases of the GT31 CAZy family. Glycobiology, 31(3), 243-259. https://doi.org/10.1093/glycob/cwaa086
Petit, Daniel, et al. "A phylogenetic view and functional annotation of the animal β1,3-glycosyltransferases of the GT31 CAZy family." Glycobiology vol. 31,3 (2021): 243-259. doi: https://doi.org/10.1093/glycob/cwaa086
Petit D, Teppa RE, Harduin-Lepers A. A phylogenetic view and functional annotation of the animal β1,3-glycosyltransferases of the GT31 CAZy family. Glycobiology. 2021 Apr 01;31(3):243-259. doi: 10.1093/glycob/cwaa086. PMID: 32886776; PMCID: PMC8022947.
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Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis.

BMC plant biology

Kaur D, Held MA, Smith MR, Showalter AM.
PMID: 34903166
BMC Plant Biol. 2021 Dec 13;21(1):590. doi: 10.1186/s12870-021-03362-2.

BACKGROUND: Arabinogalactan-proteins (AGPs) are structurally complex hydroxyproline-rich cell wall glycoproteins ubiquitous in the plant kingdom. AGPs biosynthesis involves a series of post-translational modifications including the addition of type II arabinogalactans to non-contiguous Hyp residues. To date, eight Hyp-galactosyltransferases (Hyp-GALTs;...

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Kaur D, Held MA, Smith MR, et al. Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis. BMC Plant Biol. 2021;21(1):590doi: 10.1186/s12870-021-03362-2.
Kaur, D., Held, M. A., Smith, M. R., & Showalter, A. M. (2021). Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis. BMC plant biology, 21(1), 590. https://doi.org/10.1186/s12870-021-03362-2
Kaur, Dasmeet, et al. "Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis." BMC plant biology vol. 21,1 (2021): 590. doi: https://doi.org/10.1186/s12870-021-03362-2
Kaur D, Held MA, Smith MR, Showalter AM. Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis. BMC Plant Biol. 2021 Dec 13;21(1):590. doi: 10.1186/s12870-021-03362-2. PMID: 34903166.
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Free Fatty acids regulate two galactosyltransferases in chloroplast envelope membranes isolated from spinach leaves.

Plant physiology

Sakaki T, Kondo N, Yamada M.
PMID: 16667779
Plant Physiol. 1990 Oct;94(2):781-7. doi: 10.1104/pp.94.2.781.

Effects of MgCl(2) and free fatty acids (FFA) on galactolipid:galactolipid galactosyltransferase (GGGT) and UDP-galactose: 1,2-diacylglycerol galactosyltransferase (UDGT) in chloroplast envelope membranes isolated from spinach (Spinacia oleracea L.) leaves were examined. GGGT activity was sigmoidally stimulated by MgCl(2) with a...

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Sakaki T, Kondo N, Yamada M. Free Fatty acids regulate two galactosyltransferases in chloroplast envelope membranes isolated from spinach leaves. Plant Physiol. 1990;94(2):781-7doi: 10.1104/pp.94.2.781.
Sakaki, T., Kondo, N., & Yamada, M. (1990). Free Fatty acids regulate two galactosyltransferases in chloroplast envelope membranes isolated from spinach leaves. Plant physiology, 94(2), 781-7. https://doi.org/10.1104/pp.94.2.781
Sakaki, T, et al. "Free Fatty acids regulate two galactosyltransferases in chloroplast envelope membranes isolated from spinach leaves." Plant physiology vol. 94,2 (1990): 781-7. doi: https://doi.org/10.1104/pp.94.2.781
Sakaki T, Kondo N, Yamada M. Free Fatty acids regulate two galactosyltransferases in chloroplast envelope membranes isolated from spinach leaves. Plant Physiol. 1990 Oct;94(2):781-7. doi: 10.1104/pp.94.2.781. PMID: 16667779; PMCID: PMC1077299.
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Rat brain glycosyltransferase activities during postnatal development.

International journal of developmental neuroscience : the official journal of the International Society for Developmental Neuroscience

Broquet P, Serres-Guillaumond M, Baubichon-Cortay H, Louisot P.
PMID: 24874592
Int J Dev Neurosci. 1985;3(2):105-10. doi: 10.1016/0736-5748(85)90001-2.

Enzymatic activity of seven glycoprotein and glycolipid glycosyltransferases was studied in microsomal fractions during postnatal development of rat brain from 3 to 42 days after birth. Specific enzymatic variations were detected for some glycosyltransferases, i.d. a maxima was shown...

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Broquet P, Serres-Guillaumond M, Baubichon-Cortay H, et al. Rat brain glycosyltransferase activities during postnatal development. Int J Dev Neurosci. 1985;3(2):105-10doi: 10.1016/0736-5748(85)90001-2.
Broquet, P., Serres-Guillaumond, M., Baubichon-Cortay, H., & Louisot, P. (1985). Rat brain glycosyltransferase activities during postnatal development. International journal of developmental neuroscience : the official journal of the International Society for Developmental Neuroscience, 3(2), 105-10. https://doi.org/10.1016/0736-5748(85)90001-2
Broquet, P, et al. "Rat brain glycosyltransferase activities during postnatal development." International journal of developmental neuroscience : the official journal of the International Society for Developmental Neuroscience vol. 3,2 (1985): 105-10. doi: https://doi.org/10.1016/0736-5748(85)90001-2
Broquet P, Serres-Guillaumond M, Baubichon-Cortay H, Louisot P. Rat brain glycosyltransferase activities during postnatal development. Int J Dev Neurosci. 1985;3(2):105-10. doi: 10.1016/0736-5748(85)90001-2. PMID: 24874592.
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Do Galactolipid Synthases Play a Key Role in the Biogenesis of Chloroplast Membranes of Higher Plants?.

Frontiers in plant science

Rocha J, Nitenberg M, Girard-Egrot A, Jouhet J, Maréchal E, Block MA, Breton C.
PMID: 29472943
Front Plant Sci. 2018 Feb 08;9:126. doi: 10.3389/fpls.2018.00126. eCollection 2018.

A unique feature of chloroplasts is their high content of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), which constitute up to 80% of their lipids. These galactolipids are synthesized in the chloroplast envelope membrane through the concerted action of...

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Rocha J, Nitenberg M, Girard-Egrot A, et al. Do Galactolipid Synthases Play a Key Role in the Biogenesis of Chloroplast Membranes of Higher Plants?. Front Plant Sci. 2018;9:126doi: 10.3389/fpls.2018.00126.
Rocha, J., Nitenberg, M., Girard-Egrot, A., Jouhet, J., Maréchal, E., Block, M. A., & Breton, C. (2018). Do Galactolipid Synthases Play a Key Role in the Biogenesis of Chloroplast Membranes of Higher Plants?. Frontiers in plant science, 9126. https://doi.org/10.3389/fpls.2018.00126
Rocha, Joana, et al. "Do Galactolipid Synthases Play a Key Role in the Biogenesis of Chloroplast Membranes of Higher Plants?." Frontiers in plant science vol. 9 (2018): 126. doi: https://doi.org/10.3389/fpls.2018.00126
Rocha J, Nitenberg M, Girard-Egrot A, Jouhet J, Maréchal E, Block MA, Breton C. Do Galactolipid Synthases Play a Key Role in the Biogenesis of Chloroplast Membranes of Higher Plants?. Front Plant Sci. 2018 Feb 08;9:126. doi: 10.3389/fpls.2018.00126. eCollection 2018. PMID: 29472943; PMCID: PMC5809773.
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Control of mannose/galactose ratio during galactomannan formation in developing legume seeds.

Planta

Edwards M, Scott C, Gidley MJ, Reid JS.
PMID: 24177968
Planta. 1992 Apr;187(1):67-74. doi: 10.1007/BF00201625.

Galactomannan deposition was investigated in developing endosperms of three leguminous species representative of taxonomic groups which have galactomannans with high, medium and low galactose content. These were fenugreek (Trigonella foenum-graecum L.; mannose/galactose (Man/Gal) = 1.1), guar (Cyamopsis tetragonoloba (L.)...

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Edwards M, Scott C, Gidley MJ, et al. Control of mannose/galactose ratio during galactomannan formation in developing legume seeds. Planta. 1992;187(1):67-74doi: 10.1007/BF00201625.
Edwards, M., Scott, C., Gidley, M. J., & Reid, J. S. (1992). Control of mannose/galactose ratio during galactomannan formation in developing legume seeds. Planta, 187(1), 67-74. https://doi.org/10.1007/BF00201625
Edwards, M, et al. "Control of mannose/galactose ratio during galactomannan formation in developing legume seeds." Planta vol. 187,1 (1992): 67-74. doi: https://doi.org/10.1007/BF00201625
Edwards M, Scott C, Gidley MJ, Reid JS. Control of mannose/galactose ratio during galactomannan formation in developing legume seeds. Planta. 1992 Apr;187(1):67-74. doi: 10.1007/BF00201625. PMID: 24177968.
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Galactolipid synthesis in chromoplasts in vitro : Specificities of acyl-and galactosyltransferases.

Planta

Liedvogel B, Kleinig H.
PMID: 24407392
Planta. 1979 Jan;144(5):467-71. doi: 10.1007/BF00380124.

Isolated chromoplasts from Narcissus pseudonarcissus flowers contain: a fatty acid synthesizing system; acyl-CoA synthetase (EC 6.2.1.3); glycero-phosphate acyltransferase (EC 2.3.1.15); acylglycero-phosphate acyltransferase; phosphatidate phosphatase (EC 3.1.3.4); diacylglycerol galactosyltransferase (EC 2.4.1.46); and diacylgalactosylglycerol galactosyltransferase, i.e. all enzymatic activities necessary for...

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Liedvogel B, Kleinig H. Galactolipid synthesis in chromoplasts in vitro : Specificities of acyl-and galactosyltransferases. Planta. 1979;144(5):467-71doi: 10.1007/BF00380124.
Liedvogel, B., & Kleinig, H. (1979). Galactolipid synthesis in chromoplasts in vitro : Specificities of acyl-and galactosyltransferases. Planta, 144(5), 467-71. https://doi.org/10.1007/BF00380124
Liedvogel, B, and Kleinig, H. "Galactolipid synthesis in chromoplasts in vitro : Specificities of acyl-and galactosyltransferases." Planta vol. 144,5 (1979): 467-71. doi: https://doi.org/10.1007/BF00380124
Liedvogel B, Kleinig H. Galactolipid synthesis in chromoplasts in vitro : Specificities of acyl-and galactosyltransferases. Planta. 1979 Jan;144(5):467-71. doi: 10.1007/BF00380124. PMID: 24407392.
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Extensin and Arabinogalactan-Protein Biosynthesis: Glycosyltransferases, Research Challenges, and Biosensors.

Frontiers in plant science

Showalter AM, Basu D.
PMID: 27379116
Front Plant Sci. 2016 Jun 15;7:814. doi: 10.3389/fpls.2016.00814. eCollection 2016.

Recent research, mostly in Arabidopsis thaliana, has led to the identification and characterization of the glycosyltransferases responsible for the biosynthesis of two of the most functionally important and abundant families of plant cell wall proteins, extensins, and arabinogalactan-proteins. Extensin...

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Showalter AM, Basu D. Extensin and Arabinogalactan-Protein Biosynthesis: Glycosyltransferases, Research Challenges, and Biosensors. Front Plant Sci. 2016;7:814doi: 10.3389/fpls.2016.00814.
Showalter, A. M., & Basu, D. (2016). Extensin and Arabinogalactan-Protein Biosynthesis: Glycosyltransferases, Research Challenges, and Biosensors. Frontiers in plant science, 7814. https://doi.org/10.3389/fpls.2016.00814
Showalter, Allan M, and Basu, Debarati. "Extensin and Arabinogalactan-Protein Biosynthesis: Glycosyltransferases, Research Challenges, and Biosensors." Frontiers in plant science vol. 7 (2016): 814. doi: https://doi.org/10.3389/fpls.2016.00814
Showalter AM, Basu D. Extensin and Arabinogalactan-Protein Biosynthesis: Glycosyltransferases, Research Challenges, and Biosensors. Front Plant Sci. 2016 Jun 15;7:814. doi: 10.3389/fpls.2016.00814. eCollection 2016. PMID: 27379116; PMCID: PMC4908140.
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Raffinose Family Oligosaccharides Act As Galactose Stores in Seeds and Are Required for Rapid Germination of Arabidopsis in the Dark.

Frontiers in plant science

Gangl R, Tenhaken R.
PMID: 27507985
Front Plant Sci. 2016 Jul 26;7:1115. doi: 10.3389/fpls.2016.01115. eCollection 2016.

Raffinose synthase 5 (AtRS5, At5g40390) was characterized from Arabidopsis as a recombinant enzyme. It has a far higher affinity for the substrates galactinol and sucrose than any other raffinose synthase previously reported. In addition raffinose synthase 5 is also...

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Gangl R, Tenhaken R. Raffinose Family Oligosaccharides Act As Galactose Stores in Seeds and Are Required for Rapid Germination of Arabidopsis in the Dark. Front Plant Sci. 2016;7:1115doi: 10.3389/fpls.2016.01115.
Gangl, R., & Tenhaken, R. (2016). Raffinose Family Oligosaccharides Act As Galactose Stores in Seeds and Are Required for Rapid Germination of Arabidopsis in the Dark. Frontiers in plant science, 71115. https://doi.org/10.3389/fpls.2016.01115
Gangl, Roman, and Tenhaken, Raimund. "Raffinose Family Oligosaccharides Act As Galactose Stores in Seeds and Are Required for Rapid Germination of Arabidopsis in the Dark." Frontiers in plant science vol. 7 (2016): 1115. doi: https://doi.org/10.3389/fpls.2016.01115
Gangl R, Tenhaken R. Raffinose Family Oligosaccharides Act As Galactose Stores in Seeds and Are Required for Rapid Germination of Arabidopsis in the Dark. Front Plant Sci. 2016 Jul 26;7:1115. doi: 10.3389/fpls.2016.01115. eCollection 2016. PMID: 27507985; PMCID: PMC4960254.
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