Wide sugar substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4

Chen, Min; Chen, Leilei; Zou, Yang; Xue, Mengyang; Liang, Min; Jin, Lan; Guan, Wanyi; Shen, Jie; Wang, Wenjun; Wang, Lei; Li, Jun; Wang, Peng George

doi:10.1016/j.carres.2011.08.014

Cited by 52 publications

(54 citation statements)

References 27 publications

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“…47 It is also an abundant oligosaccharide in the milk of elephant 48 and marsupials such as brushtail possum ( Trichosurus vulpecula ), 49 tammar wallaby ( Macropus eugenii ) and grey kangaroo, 50 and koala ( Phascolarctos cinereus ). 51 As shown in Scheme 2B, Galβ1–3Galβ1–4Glc ( 2 ) was synthesized from lactose and galactose (Gal) using a one-pot four-enzyme (OP4E) system containing a Streptococcus pneumoniae TIGR4 galactokinase (SpGalK), 39 a Bifidobacterium longum ATCC55813 UDP-sugar pyrophosphorylase (BLUSP), 40 PmPpA, 21 and NmLgtA. SpGalK, BLUSP, and PmPpA were used previously for high efficient (85% yield) one-pot multienzyme (OPME) synthesis of UDP-Gal.…”

Section: Resultsmentioning

confidence: 99%

“…Enzyme abbreviations: NahK, Bifidobacterium longum ATCC55813 N -acetylhexosamine 1-kinase; 37 PmGlmU, Pasteurella multocida N -acetylglucosamine-1-phosphate uridylyltransferase; 38 PmPpA, Pasteurella multocida inorganic pyrophosphatase; 21 SpGalK, Streptococcus pneumoniae TIGR4 galactokinase; 39 BLUSP, Bifidobacterium longum UDP-sugar pyrophosphorylase. 40 …”

Section: Figurementioning

confidence: 99%

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Donor substrate promiscuity of bacterial β1–3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of β1–4-galactosyltransferases

Xue

et al. 2016

Bioorganic & Medicinal Chemistry

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β1–3-N-Acetylglucosaminyltransferases (β3GlcNAcTs) and β1–4-galactosyltransferases (β4GalTs) have been broadly used in enzymatic synthesis of N-acetyllactosamine (LacNAc)-containing oligosaccharides and glycoconjugates including poly-LacNAc, and lacto-N-neotetraose (LNnT) found in the milk of human and other mammals. In order to explore oligosaccharides and derivatives that can be synthesized by the combination of β3GlcNAcTs and β4GalTs, donor substrate specificity studies of two bacterial β3GlcNAcTs from Helicobacter pylori (Hpβ3GlcNAcT) and Neisseria meningitidis (NmLgtA), respectively, using a library of 39 sugar nucleotides were carried out. The two β3GlcNAcTs have complementary donor substrate promiscuity and 13 different trisaccharides were produced. They were used to investigate the acceptor substrate specificities of three β4GalTs from Neisseria meningitidis (NmLgtB), Helicobacter pylori (Hpβ4GalT), and bovine (Bβ4GalT), respectively. Ten of the 13 trisaccharides were shown to be tolerable acceptors for at least one of these β4GalTs. The application of NmLgtA in one-pot multienzyme (OPME) synthesis of two trisaccharides including GalNAcβ1–3Galβ1–4GlcβProN3 and Galβ1–3Galβ1–4Glc was demonstrated. The study provides important information for using these glycosyltransferases as powerful catalysts in enzymatic and chemoenzymatic syntheses of oligosaccharides and derivatives which can be useful probes and reagents.

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Section: Resultsmentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

Donor substrate promiscuity of bacterial β1–3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of β1–4-galactosyltransferases

Xue

et al. 2016

Bioorganic & Medicinal Chemistry

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“…In contrast, human N-acetylgalactosamine kinase (GALK2) has broader specificity, and it will phosphorylate both N-acetylgalactosamine and other sugars that share the 2 -acetylamine modification [92,93]. Prokaryotic galactokinases have more relaxed substrate specificity, accepting a variety of galactose analogues as substrates [33,[94][95][96][97]. Far fewer data are available on the nucleotide specificity of the GHMP carbohydrate kinases.…”

Section: Ghmp Kinase Specificitymentioning

confidence: 99%

Carbohydrate Kinases: A Conserved Mechanism Across Differing Folds

2019

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Carbohydrate kinases activate a wide variety of monosaccharides by adding a phosphate group, usually from ATP. This modification is fundamental to saccharide utilization, and it is likely a very ancient reaction. Modern organisms contain carbohydrate kinases from at least five main protein families. These range from the highly specialized inositol kinases, to the ribokinases and galactokinases, which belong to families that phosphorylate a wide range of substrates. The carbohydrate kinases utilize a common strategy to drive the reaction between the sugar hydroxyl and the donor phosphate. Each sugar is held in position by a network of hydrogen bonds to the non-reactive hydroxyls (and other functional groups). The reactive hydroxyl is deprotonated, usually by an aspartic acid side chain acting as a catalytic base. The deprotonated hydroxyl then attacks the donor phosphate. The resulting pentacoordinate transition state is stabilized by an adjacent divalent cation, and sometimes by a positively charged protein side chain or the presence of an anion hole. Many carbohydrate kinases are allosterically regulated using a wide variety of strategies, due to their roles at critical control points in carbohydrate metabolism. The evolution of a similar mechanism in several folds highlights the elegance and simplicity of the catalytic scheme.

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“…The obtained Lc 3 βSph ( 4 ) was used for synthesizing nLc 4 βSph ( 3 ) using an improved OPME galactose (Gal) activation and transfer system 50 containing Streptococcus pneumoniae TIGR4 galactokinase (SpGalK), 51 Bifidobacterium longum UDP-sugar pyrophosphorylase (BLUSP), 50 PmPpA, and Neisseria meningitidis β1–4-galactosyltransferase (NmLgtB) 48, 49 in Tris-HCl buffer (100 mM, pH 8.0) at 37 °C for 30 hours. The SpGalK, BLUSP, and PmPpA allowed in situ formation of uridine 5′-diphosphate-galactose (UDP-Gal), the donor substrate of NmLgtB, from monosaccharide galactose (Gal) for the formation of LNnTβSph ( 3 ).…”

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confidence: 99%

Highly efficient chemoenzymatic synthesis and facile purification of α-Gal pentasaccharyl ceramide Galα3nLc₄βCer

Santra

et al. 2017

Chem. Commun.

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A highly efficient chemoenzymatic method for synthesizing glycosphingolipids using α-Gal pentasaccharyl ceramide as an example is reported here. Enzymatic extension of chemically synthesized lactosyl sphingosine using efficient sequential one-pot multienzyme (OPME) reactions allowed glycosylation be carried out in aqueous solution. Facile C18 cartridge-based quick (<30 minutes) purification proctols were established using minimal amounts of green solvents (CH3CN and H2O). Simple acylation in the last step led to the formation of the target glycosyl ceramide in 4 steps with an overall yield of 57%.

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Wide sugar substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4

Cited by 52 publications

References 27 publications

Donor substrate promiscuity of bacterial β1–3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of β1–4-galactosyltransferases

Donor substrate promiscuity of bacterial β1–3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of β1–4-galactosyltransferases

Carbohydrate Kinases: A Conserved Mechanism Across Differing Folds

Highly efficient chemoenzymatic synthesis and facile purification of α-Gal pentasaccharyl ceramide Galα3nLc₄βCer

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Wide sugar substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4

Cited by 52 publications

References 27 publications

Donor substrate promiscuity of bacterial β1–3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of β1–4-galactosyltransferases

Donor substrate promiscuity of bacterial β1–3-N-acetylglucosaminyltransferases and acceptor substrate flexibility of β1–4-galactosyltransferases

Carbohydrate Kinases: A Conserved Mechanism Across Differing Folds

Highly efficient chemoenzymatic synthesis and facile purification of α-Gal pentasaccharyl ceramide Galα3nLc4βCer

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Highly efficient chemoenzymatic synthesis and facile purification of α-Gal pentasaccharyl ceramide Galα3nLc₄βCer