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Literature summary extracted from

  • Nomura, K.; Sugimoto, K.; Nishiura, H.; Ohdan, K.; Nishimura, T.; Hayashi, H.; Kuriki, T.
    Glucosylation of acetic acid by sucrose phosphorylase (2008), Biosci. Biotechnol. Biochem., 72, 82-87.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.7 expression in Escherichia coli Streptococcus mutans

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 Streptococcus mutans
-
D-fructose + alpha-D-glucose 1-phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.7 Streptococcus mutans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.7 recombinant enzyme from Escherichia coli by anion exchange and hydrophobic interaction chromatography Streptococcus mutans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.7 additional information the undissociated carboxyl group is essential to the acceptor molecule for the transglycosylation reaction of sucrose phosphorylase Streptococcus mutans ?
-
?
2.4.1.7 sucrose + acetate substrate and product structure determination, overview Streptococcus mutans D-fructose + 1-O-acetyl-alpha-D-glucopyranose
-
?
2.4.1.7 sucrose + hydroquinone
-
Streptococcus mutans D-fructose + ?
-
?
2.4.1.7 sucrose + phosphate
-
Streptococcus mutans D-fructose + alpha-D-glucose 1-phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.7 SPase
-
Streptococcus mutans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.7 37
-
assay at Streptococcus mutans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.7 3.5
-
assay at Streptococcus mutans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.7 3 6.5
-
Streptococcus mutans