Literature summary for 3.1.3.21 extracted from

Xu, Y.F.; Lu, W.; Chen, J.C.; Johnson, S.A.; Gibney, P.A.; Thomas, D.G.; Brown, G.; May, A.L.; Campagna, S.R.; Yakunin, A.F.; Botstein, D.; Rabinowitz, J.D.
Discovery and functional characterization of a yeast sugar alcohol phosphatase (2018), ACS Chem. Biol., 13, 3011-3020 .

Search for more literature for 3.1.3.21

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P53981	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glycerol-3-phosphate + H2O	preferred substrate, stereospecific for L-isomer	Saccharomyces cerevisiae	glycerol + phosphate	-	?
ribitol-5-phosphate + H2O	-	Saccharomyces cerevisiae	ribitol + phosphate	-	?
sorbitol-6-phosphate + H2O	-	Saccharomyces cerevisiae	sorbitol + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
polyol phosphatase	-	Saccharomyces cerevisiae
Pyp1	-	Saccharomyces cerevisiae
YNL010W	-	Saccharomyces cerevisiae

Expression

Organism	Comment	Expression
Saccharomyces cerevisiae	Pyp1 expression is strongly positively correlated with yeast growth rate	additional information

General Information

General Information	Comment	Organism
physiological function	Pyp1 activity is important for yeast to maintain phosphoglucose isomerase activity in the presence of environmental sugar alcohols. Pyp1 expression is strongly positively correlated with yeast growth rate. Deletion of Pyp1 leads to accumulation of octulose-8-phosphate, ribitol-5-phosphate, and erythritol-4-phosphate	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)