The effect of amino acid modifying reagents on the activity of a (1→3)-β-glucan synthase from Italian ryegrass (Lolium multiflorum) endosperm

Bulone, Vincent; Lam, Bach-Tuyet; Stone, Bruce

doi:10.1016/s0031-9422(98)00494-4

Cited by 8 publications

(2 citation statements)

References 24 publications

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“…Although the HAS from P. multocida is currently a member of this family, it appears to be structurally distinct from other HAS (46). Experimental evidence for the role of carboxyl residues in ␤-glycan synthases comes from site-directed mutagenesis of chitin synthase 2 from Saccharomyces cerevisiae (47) and of the AcsAB cellulose synthase from Acetobacter xylinum (44) as well as from the use of amino acid-modifying reagents on a ␤-(1,3)-glucan synthase from ryegrass (48). Based on these and other results it was assumed that Asp residues are involved in the acid-base catalytic mechanism of this kind of glycosyltransferases (49).…”

Section: Resultsmentioning

confidence: 99%

Tts, a Processive β-Glucosyltransferase of Streptococcus pneumoniae, Directs the Synthesis of the Branched Type 37 Capsular Polysaccharide in Pneumococcus and Other Gram-positive Species

Llull¹,

Garcı́a

López

2001

Journal of Biological Chemistry

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Transformation experiments using either a recombinant plasmid containing the whole transcriptional unit of tts or chromosomal DNA from a type 37 pneumococcus showed that tts is the only gene required to drive the biosynthesis of a type 37 capsule in S. pneumoniae and other Gram-positive bacteria, namely Streptococcus oralis, Streptococcus gordonii, and Bacillus subtilis. The Tts synthase was overproduced in S. pneumoniae and purified as a membrane-associated enzyme. These membrane preparations used UDP-Glc as substrate to catalyze the synthesis of a high molecular weight polysaccharide immunologically identical to the type 37 capsule. In addition, UDP-Gal was also a substrate to produce type 37 polysaccharide since a strong UDP-Glc-4-epimerase activity is associated to the membrane fraction of S. pneumoniae. These results indicated that Tts has a dual biochemical activity that leads to the synthesis of the branched type 37 polysaccharide.

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Section: Resultsmentioning

confidence: 99%

Tts, a Processive β-Glucosyltransferase of Streptococcus pneumoniae, Directs the Synthesis of the Branched Type 37 Capsular Polysaccharide in Pneumococcus and Other Gram-positive Species

Llull¹,

Garcı́a

López

2001

Journal of Biological Chemistry

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“…The suggestion that the enzymes operate through a general acid -base catalytic mechanism is supported by the essential role of acidic amino acids, as shown by the kinetics of carbodiimide inhibition of the (1,3) -β -d -glucan synthase from Lolium multifl orum (Bulone et al 1998 ). Further support for the role of acidic amino acids in catalysis is given by site -directed mutagenesis studies.…”

Section: Catalytic M Echanismsmentioning

confidence: 96%

Biosynthesis of Plant Cell Wall and Related Polysaccharides by Enzymes of the GT2 and GT48 Families

Stone

Jacobs

Hrmová

et al. 2010

Annual Plant Reviews

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In this chapter we outline the evolution of our understanding of the biological functions, genetics and regulation of enzymes of the GT2 and GT48 families of glycosyl transferases. The GT2 family is very large and includes enzymes encoded by the cellulose synthase gene superfamily, together with many other transferases with diverse substrate specifi cities that are distributed from the Archaea to humans. On the other hand, there are relatively few known members of the GT48 family, in which activities are limited to putative (1,3) -β -d -glucan synthases of embryophytes, fungi and yeasts. The review is focused on a number of individual case studies, which have been chosen on the basis of their biological and economical importance in plant biology. The history of our knowledge of (1,4) -β -d -glucan (cellulose) synthases and (1,3;1,4) -β -d -glucan synthases in plants will be reviewed as representatives of the GT2 family, while the (1,3) -β -d -glucan (or callose) synthases will be compared with these, as representatives of the GT48 family. These synthases have been extensively studied using biochemical techniques, but they are associated with membranes and are not easily purifi ed. Emerging functional genomics technologies have been used to identify the genes encoding the cellulose synthases of the GT2 family, while new proteomics

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Biosynthesis of Plant Cell Wall and Related Polysaccharides by Enzymes of theGT2andGT48Families

Stone

Jacobs

Hrmová

et al. 2018

Annual Plant Reviews Online

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In this chapter we outline the evolution of our understanding of the biological functions, genetics and regulation of enzymes of the GT2 and GT48 families of glycosyl transferases. The GT2 family is very large and includes enzymes encoded by the cellulose synthase gene superfamily, together with many other transferases with diverse substrate specificities that are distributed from the Archaea to humans. On the other hand, there are relatively few known members of the GT48 family, in which activities are limited to putative (1,3)‐β‐d‐glucan synthases of embryophytes, fungi and yeasts. The review is focused on a number of individual case studies, which have been chosen on the basis of their biological and economical importance in plant biology. The history of our knowledge of (1,4)‐β‐d‐glucan (cellulose) synthases and (1,3;1,4)‐β‐d‐glucan synthases in plants will be reviewed as representatives of the GT2 family, while the (1,3)‐β‐d‐glucan (or callose) synthases will be compared with these, as representatives of the GT48 family. These synthases have been extensively studied using biochemical techniques, but they are associated with membranes and are not easily purified. Emerging functional genomics technologies have been used to identify the genes encoding the cellulose synthases of the GT2 family, while new proteomics procedures have provided amino acid sequence that has in turn been applied to the identification of the GT48 (1,3)‐β‐d‐glucan synthases of plants. The enzymes are involved in the synthesis of structurally similar polysaccharides, but appear to have evolved independently.

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The effect of amino acid modifying reagents on the activity of a (1→3)-β-glucan synthase from Italian ryegrass (Lolium multiflorum) endosperm

Cited by 8 publications

References 24 publications

Tts, a Processive β-Glucosyltransferase of Streptococcus pneumoniae, Directs the Synthesis of the Branched Type 37 Capsular Polysaccharide in Pneumococcus and Other Gram-positive Species

Tts, a Processive β-Glucosyltransferase of Streptococcus pneumoniae, Directs the Synthesis of the Branched Type 37 Capsular Polysaccharide in Pneumococcus and Other Gram-positive Species

Biosynthesis of Plant Cell Wall and Related Polysaccharides by Enzymes of the GT2 and GT48 Families

Biosynthesis of Plant Cell Wall and Related Polysaccharides by Enzymes of theGT2andGT48Families

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