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Literature summary for 2.4.1.7 extracted from
- Sucrose phosphorylase: A powerful transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals (2010), Biocatal. Biotransform., 28, 10-21.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations | Leuconostoc mesenteroides |
| synthesis | the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations | Pelomonas saccharophila |
| synthesis | the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations | Streptococcus mutans |
| synthesis | the enzyme is useful as transglucosylation catalyst for synthesis of alpha-D-glucosides as industrial fine chemicals, overview. The enzyme is also used in the industrial process for production of 2-O-(alpha-D-glucopyranosyl)-sn-glycerol as active ingredient of cosmetic formulations | Bifidobacterium adolescentis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis | Bifidobacterium adolescentis |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
2 * 50000, SDS-PAGE | Pelomonas saccharophila |
| 55000 | - |
1 * 55000, SDS-PAGE | Streptococcus mutans |
| 55700 | - |
gel filtration | Streptococcus mutans |
| 56400 | 60000 | gel filtration | Leuconostoc mesenteroides |
| 58000 | - |
2 * 58000, SDS-PAGE | Bifidobacterium adolescentis |
| 78000 | 84000 | gel filtration | Pelomonas saccharophila |
| 129000 | - |
gel filtration | Bifidobacterium adolescentis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| sucrose + phosphate | Leuconostoc mesenteroides | - |
D-fructose + alpha-D-glucose 1-phosphate | - |
r |  |
| sucrose + phosphate | Pelomonas saccharophila | - |
D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
| sucrose + phosphate | Streptococcus mutans | - |
D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
| sucrose + phosphate | Bifidobacterium adolescentis | - |
D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
| sucrose + phosphate | Leuconostoc mesenteroides B-1149 | - |
D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bifidobacterium adolescentis | Q84HQ2 | - |
- |
| Leuconostoc mesenteroides | - |
- |
- |
| Leuconostoc mesenteroides B-1149 | - |
- |
- |
| Pelomonas saccharophila | - |
- |
- |
| Streptococcus mutans | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate | a two-step catalytic mechanism: Asp192 is the catalytic nucleophile, Glu232 is the catalytic acid-base, and Asp290 functions as a transition state stabilizer. By forming a strong hydrogen bond with the hydroxyl groups at C2 and C3 of the glucosyl residue being transferred, the anionic side chain of Asp290 is suggested to provide selective stabilization to oxocarbenium ion-like transition states flanking the covalent alpha-glucosyl enzyme intermediate | Bifidobacterium adolescentis | |
| sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate | sucrose phosphorylase catalyzes glucosyl transfer with retention of the alpha-anomeric configuration of the donor substrate in the resulting glucosidic product, double displacement-like catalytic mechanism | Leuconostoc mesenteroides | |
| sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate | sucrose phosphorylase catalyzes glucosyl transfer with retention of the alpha-anomeric configuration of the donor substrate in the resulting glucosidic product, double displacement-like catalytic mechanism | Pelomonas saccharophila | |
| sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate | sucrose phosphorylase catalyzes glucosyl transfer with retention of the alpha-anomeric configuration of the donor substrate in the resulting glucosidic product, double displacement-like catalytic mechanism | Streptococcus mutans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-glucose 1-fluoride + phosphate | as efficient as substrate as sucrose | Leuconostoc mesenteroides | fluoride + alpha-D-glucose 1-phosphate | - |
r | |
| alpha-D-glucose 1-fluoride + phosphate | as efficient as substrate as sucrose | Leuconostoc mesenteroides B-1149 | fluoride + alpha-D-glucose 1-phosphate | - |
r | |
| alpha-D-glucose 1-phosphate + phosphate | 5.4fold lower activity compared to sucrose | Leuconostoc mesenteroides | ? | - |
r | |
| alpha-D-glucose 1-phosphate + phosphate | 5.4fold lower activity compared to sucrose | Leuconostoc mesenteroides B-1149 | ? | - |
r | |
| additional information | sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid | Pelomonas saccharophila | ? | - |
? | |
| additional information | sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid | Streptococcus mutans | ? | - |
? | |
| additional information | sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid | Bifidobacterium adolescentis | ? | - |
? | |
| additional information | sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid. Sucrose, glucose 1-phosphate, and alpha-glucopyranosyl fl uoride are highly reactive donor substrates for the enzyme, broad range of acceptor substrates. Nitrophenyl-alpha-D-glucopyranose is a poor substrate | Leuconostoc mesenteroides | ? | - |
? | |
| additional information | sucrose phosphorylase catalyzes three types of overall reaction: glucosyl transfer to and from phosphate, hydrolysis, and transglucosylation. Arsenate can replace phosphate as glucosyl acceptor substrate, other glucosyl acceptors are caffeic acid, benzoic acid, acetic acid, and formic acid. Sucrose, glucose 1-phosphate, and alpha-glucopyranosyl fl uoride are highly reactive donor substrates for the enzyme, broad range of acceptor substrates. Nitrophenyl-alpha-D-glucopyranose is a poor substrate | Leuconostoc mesenteroides B-1149 | ? | - |
? | |
| sucrose + arsenate | - |
Leuconostoc mesenteroides | D-fructose + alpha-D-glucose 1-arsenate | because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible | ir | |
| sucrose + arsenate | - |
Pelomonas saccharophila | D-fructose + alpha-D-glucose 1-arsenate | because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible | ir | |
| sucrose + arsenate | - |
Streptococcus mutans | D-fructose + alpha-D-glucose 1-arsenate | because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible | ir | |
| sucrose + arsenate | - |
Bifidobacterium adolescentis | D-fructose + alpha-D-glucose 1-arsenate | because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible | ir | |
| sucrose + arsenate | - |
Leuconostoc mesenteroides B-1149 | D-fructose + alpha-D-glucose 1-arsenate | because alpha-glucopyranosyl arsenate decomposes hydrolytically in a non-enzymatic reaction, the overall arsenolysis of sucrose is essentially irreversible | ir | |
| sucrose + glycerol | low activity, regioselective glucosylation of glycerol, the product 2-O-(alpha-D-glucopyranosyl)-sn-glycerol itself is a very poor substrate for the enzyme | Leuconostoc mesenteroides | D-fructose + 2-O-(alpha-D-glucopyranosyl)-sn-glycerol | - |
? | |
| sucrose + phosphate | - |
Leuconostoc mesenteroides | D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
| sucrose + phosphate | - |
Pelomonas saccharophila | D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
| sucrose + phosphate | - |
Streptococcus mutans | D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
| sucrose + phosphate | - |
Bifidobacterium adolescentis | D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
| sucrose + phosphate | - |
Leuconostoc mesenteroides B-1149 | D-fructose + alpha-D-glucose 1-phosphate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 50000, SDS-PAGE | Pelomonas saccharophila |
| dimer | 2 * 58000, SDS-PAGE | Bifidobacterium adolescentis |
| monomer | 1 * 55000, SDS-PAGE | Streptococcus mutans |
| monomer | 1 * 54000-58000, SDS-PAGE | Leuconostoc mesenteroides |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family | Leuconostoc mesenteroides |
| More | sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family | Pelomonas saccharophila |
| More | sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family | Streptococcus mutans |
| More | sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family | Bifidobacterium adolescentis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
- |
Pelomonas saccharophila |
| 30 | 37 | - |
Leuconostoc mesenteroides |
| 37 | - |
- |
Streptococcus mutans |
| 48 | - |
- |
Bifidobacterium adolescentis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 6.5 | - |
Bifidobacterium adolescentis |
| 6.2 | 7.5 | - |
Leuconostoc mesenteroides |
| 6.5 | - |
- |
Streptococcus mutans |
| 6.6 | 7 | - |
Pelomonas saccharophila |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzyme activity is not dependent on cofactors or cosubstrates | Leuconostoc mesenteroides | |
| additional information | enzyme activity is not dependent on cofactors or cosubstrates | Pelomonas saccharophila | |
| additional information | enzyme activity is not dependent on cofactors or cosubstrates | Streptococcus mutans | |
| additional information | enzyme activity is not dependent on cofactors or cosubstrates | Bifidobacterium adolescentis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose | Leuconostoc mesenteroides |
| physiological function | sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose | Pelomonas saccharophila |
| physiological function | sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose | Streptococcus mutans |
| physiological function | sucrose phosphorylase is likely to serve a catabolic function in vivo, fueling the energy metabolism of the cell with Glc1P and D-fructose produced from sucrose | Bifidobacterium adolescentis |
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