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Literature summary extracted from

  • Goedl, C.; Sawangwan, T.; Wildberger, P.; Nidetzky, B.
    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

EC Number Application Comment Organism
2.4.1.7 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
2.4.1.7 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
2.4.1.7 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
2.4.1.7 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)

EC Number Crystallization (Comment) Organism
2.4.1.7 crystal structure analysis Bifidobacterium adolescentis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.7 50000
-
 2 * 50000, SDS-PAGE Pelomonas saccharophila
2.4.1.7 55000
-
 1 * 55000, SDS-PAGE Streptococcus mutans
2.4.1.7 55700
-
 gel filtration Streptococcus mutans
2.4.1.7 56400 60000 gel filtration Leuconostoc mesenteroides
2.4.1.7 58000
-
 2 * 58000, SDS-PAGE Bifidobacterium adolescentis
2.4.1.7 78000 84000 gel filtration Pelomonas saccharophila
2.4.1.7 129000
-
 gel filtration Bifidobacterium adolescentis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.7 sucrose + phosphate Leuconostoc mesenteroides
-
 D-fructose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 sucrose + phosphate Pelomonas saccharophila
-
 D-fructose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 sucrose + phosphate Streptococcus mutans
-
 D-fructose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 sucrose + phosphate Bifidobacterium adolescentis
-
 D-fructose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 sucrose + phosphate Leuconostoc mesenteroides B-1149
-
 D-fructose + alpha-D-glucose 1-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.7 Bifidobacterium adolescentis Q84HQ2
-
-
2.4.1.7 Leuconostoc mesenteroides
-
-
-
2.4.1.7 Leuconostoc mesenteroides B-1149
-
-
-
2.4.1.7 Pelomonas saccharophila
-
-
-
2.4.1.7 Streptococcus mutans
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.1.7 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
a
2.4.1.7 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
a
2.4.1.7 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
a
2.4.1.7 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.7 alpha-D-glucose 1-fluoride + phosphate as efficient as substrate as sucrose Leuconostoc mesenteroides fluoride + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 alpha-D-glucose 1-fluoride + phosphate as efficient as substrate as sucrose Leuconostoc mesenteroides B-1149 fluoride + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 alpha-D-glucose 1-phosphate + phosphate 5.4fold lower activity compared to sucrose Leuconostoc mesenteroides ?
-
 r
2.4.1.7 alpha-D-glucose 1-phosphate + phosphate 5.4fold lower activity compared to sucrose Leuconostoc mesenteroides B-1149 ?
-
 r
2.4.1.7 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 ?
-
 ?
2.4.1.7 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 ?
-
 ?
2.4.1.7 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 ?
-
 ?
2.4.1.7 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 ?
-
 ?
2.4.1.7 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 ?
-
 ?
2.4.1.7 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
2.4.1.7 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
2.4.1.7 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
2.4.1.7 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
2.4.1.7 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
2.4.1.7 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
-
 ?
2.4.1.7 sucrose + phosphate
-
 Leuconostoc mesenteroides D-fructose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 sucrose + phosphate
-
 Pelomonas saccharophila D-fructose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 sucrose + phosphate
-
 Streptococcus mutans D-fructose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 sucrose + phosphate
-
 Bifidobacterium adolescentis D-fructose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.7 sucrose + phosphate
-
 Leuconostoc mesenteroides B-1149 D-fructose + alpha-D-glucose 1-phosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.4.1.7 dimer 2 * 50000, SDS-PAGE Pelomonas saccharophila
2.4.1.7 dimer 2 * 58000, SDS-PAGE Bifidobacterium adolescentis
2.4.1.7 monomer 1 * 55000, SDS-PAGE Streptococcus mutans
2.4.1.7 monomer 1 * 54000-58000, SDS-PAGE Leuconostoc mesenteroides

Synonyms

EC Number Synonyms Comment Organism
2.4.1.7 More sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family Leuconostoc mesenteroides
2.4.1.7 More sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family Pelomonas saccharophila
2.4.1.7 More sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family Streptococcus mutans
2.4.1.7 More sucrose phosphorylase is a member of family GH13, also known as the alpha-amylase family Bifidobacterium adolescentis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.7 30
-
-
 Pelomonas saccharophila
2.4.1.7 30 37
-
 Leuconostoc mesenteroides
2.4.1.7 37
-
-
 Streptococcus mutans
2.4.1.7 48
-
-
 Bifidobacterium adolescentis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.7 6 6.5
-
 Bifidobacterium adolescentis
2.4.1.7 6.2 7.5
-
 Leuconostoc mesenteroides
2.4.1.7 6.5
-
-
 Streptococcus mutans
2.4.1.7 6.6 7
-
 Pelomonas saccharophila

Cofactor

EC Number Cofactor Comment Organism Structure
2.4.1.7 additional information enzyme activity is not dependent on cofactors or cosubstrates Leuconostoc mesenteroides
2.4.1.7 additional information enzyme activity is not dependent on cofactors or cosubstrates Pelomonas saccharophila
2.4.1.7 additional information enzyme activity is not dependent on cofactors or cosubstrates Streptococcus mutans
2.4.1.7 additional information enzyme activity is not dependent on cofactors or cosubstrates Bifidobacterium adolescentis

General Information

EC Number General Information Comment Organism
2.4.1.7 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
2.4.1.7 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
2.4.1.7 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
2.4.1.7 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