Literature summary for 2.7.1.30 extracted from

Stefuca, V.; Vostiar, I.; Sefcovicova, J.; Katrlik, J.; Mastihuba, V.; Greifova, M.; Gemeiner, P.
Development of enzyme flow calorimeter system for monitoring of microbial glycerol conversion (2006), Appl. Microbiol. Biotechnol., 72, 1170-1175.

Organism

Organism	UniProt	Comment	Textmining
Cellulomonas sp.	-	glycerol kinase from Cellulomonas sp. is used to develop a bisensor based on flow calorimetry for quantitative analysis of glycerol during bioconversion process. Thermomeric glycerol sensor employs flow calorimeter equipped with a column packed with immobilized glycerol kinase. The glycerol kinase from Escherichia coli is able to detect glycerol in samples, but the linearity range and sensitibity are rather low and the calibration line does not pass through the origin of calibration dependence. The enzyme from Cellulomonas sp. provides a similar trend but significantly better results. The immobilized enzyme stability is excellent. The immobilized enzyme column is stored at 4°C. It can do 1 month of total operation time at 30°C with no significant loss of sensitivity. No interference with 1,3-propanediol and fermentation medium is observable.	-
Escherichia coli	-	glycerol kinase from Escherichia coli is tested to develop a bisensor based on flow calorimetry for quantitative analysis of glycerol during bioconversion process. Thermomeric glycerol sensor employs flow calorimeter equipped with a column packed with immobilized glycerol kinase. The glycerol kinase from Escherichia coli is able to detect glycerol in samples, but the linearity range and sensitibity are rather low and the calibration line does not pass through the origin of calibration dependence, so that the Escherichia coli enzyme is not used.	-

Synonyms	Comment	Organism
ATP: glycerol-3-phosphotransferase	-	Escherichia coli
ATP: glycerol-3-phosphotransferase	-	Cellulomonas sp.
GK	-	Escherichia coli
GK	-	Cellulomonas sp.