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Literature summary for 2.4.1.B34 extracted from

  • Bai, Y.; Boeger, M.; van der Kaaij, R.M.; Woortman, A.J.; Pijning, T.; van Leeuwen, S.S.; van Bueren, A.L.; Dijkhuizen, L.
    Lactobacillus reuteri strains convert starch and maltodextrins into homoexopolysaccharides using an extracellular and cell-associated 4,6-alpha-glucanotransferase (2016), J. Agric. Food Chem., 64, 2941-2952 .
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular cell-associated Limosilactobacillus reuteri
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Organism

Organism UniProt Comment Textmining
Limosilactobacillus reuteri
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Limosilactobacillus reuteri A0A0U5F702
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Limosilactobacillus reuteri 121 A0A0U5F702
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Limosilactobacillus reuteri DSM20016
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Limosilactobacillus reuteri LMG 18388 A0A0U5F702
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Limosilactobacillus reuteri ML1
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Limosilactobacillus reuteri TMW1.106
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no activity in Lactobacillus reuteri strain 180
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no activity in Lactobacillus reuteri strain ATCC55730
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Source Tissue

Source Tissue Comment Organism Textmining
culture condition:maltodextrin-grown cell
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Limosilactobacillus reuteri
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis Limosilactobacillus reuteri ?
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additional information structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri ?
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additional information structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri ?
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additional information structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri ?
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additional information structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri ML1 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri ML1 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri ML1 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri DSM20016 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri DSM20016 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri DSM20016 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis Limosilactobacillus reuteri 121 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri TMW1.106 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri TMW1.106 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis Limosilactobacillus reuteri TMW1.106 ?
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additional information structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis Limosilactobacillus reuteri LMG 18388 ?
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Synonyms

Synonyms Comment Organism
4,6-alpha-GTase
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Limosilactobacillus reuteri
Gtf106b
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Limosilactobacillus reuteri
GtfB
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Limosilactobacillus reuteri
GtfML4
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Limosilactobacillus reuteri
GtfW
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Limosilactobacillus reuteri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Limosilactobacillus reuteri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
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assay at Limosilactobacillus reuteri

General Information

General Information Comment Organism
evolution the enzyme belongs to the GH70 family Limosilactobacillus reuteri
physiological function Lactobacillus reuteri strain 121 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfB acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with these extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). NMR, SEC, and enzymatic hydrolysis of EPS synthesized by Lactobacillus reuteri srain 121 cells show that the EPS have similar linkage specificities but generally are much bigger in size than IMMP produced by the GtfB enzyme. 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo Limosilactobacillus reuteri
physiological function Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase Gtf106b acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS Fformation by Lactobacillus reuteri in vivo Limosilactobacillus reuteri
physiological function Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfML4 acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo Limosilactobacillus reuteri
physiological function Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfW acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo Limosilactobacillus reuteri