Enzyme Commission Number
EC 2.4.1.14
Product Overview
High-quality enzyme products.
Well-established quality management system.
Reaction
UDP-α-D-glucose + D-fructose 6-phosphate = UDP + sucrose 6F-phosphate
Systematic Name
UDP-α-D-glucose:D-fructose-6-phosphate 2-α-D-glucosyltransferase (configuration-retaining)
Function
Requires Mg2+ or Mn2+ for maximal activity. The enzyme from Synechocystis sp. strain PCC 6803 is not specific for UDP-glucose as it can use ADP-glucose and, to a lesser extent, GDP-glucose as substrates. The enzyme from rice leaves is activated by glucose 6-phosphate but that from cyanobacterial species is not. While the reaction catalysed by this enzyme is reversible, the enzyme usually works in concert with EC 3.1.3.24, sucrose-phosphate phosphatase, to form sucrose, making the above reaction essentially irreversible. The F in sucrose 6F-phosphate is used to indicate that the fructose residue of sucrose carries the substituent.
Other name
UDP-glucose—fructose-phosphate glucosyltransferase; sucrosephosphate—UDP glucosyltransferase; UDP-glucose-fructose-phosphate glucosyltransferase; SPS; uridine diphosphoglucose-fructose phosphate glucosyltransferase; sucrose 6-phosphate synthase; sucrose phosphate synthetase; sucrose phosphate-uridine diphosphate glucosyltransferase; sucrose phosphate synthase; UDP-glucose:D-fructose-6-phosphate 2-α-D-glucosyltransferase
Production Methods
Fermentation
Package
on customer request
Applications
Research Use
Storage
Should be stored in a dry and cool place, avoiding high temperature.
Appearance / Form
powder or liquid
Odor
Normal microbial fermentation odour.
WARNINGS
Keep sealed after use every time to avoid microbial infections and inactivation of enzymes until its finish.
Description
Microbial enzymes have been used in a large number of fields, such as chemical, agricultural and biopharmaceutical industries. Our enzyme production services are based on bacteria, fungi, and yeast, from strain selection, optimization, and process development to scale-up production.
