Glucose 6-phosphatase

The enzyme glucose 6-phosphatase (EC 3.1.3.9, G6Pase; systematic name D-glucose-6-phosphate phosphohydrolase) catalyzes the hydrolysis of glucose 6-phosphate, resulting in the creation of a phosphate group and free glucose:

D-glucose 6-phosphate + H2O = D-glucose + phosphate
Glucose 6-phosphatase.
Identifiers
EC no.3.1.3.9
CAS no.9001-39-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Glucose is then exported from the cell via glucose transporter membrane proteins. This catalysis completes the final step in gluconeogenesis and therefore plays a key role in the homeostatic regulation of blood glucose levels.

Glucose 6-phosphatase is a complex of multiple component proteins, including transporters for G6P, glucose, and phosphate. The main phosphatase function is performed by the glucose 6-phosphatase catalytic subunit. In humans, there are three isozymes of the catalytic subunit: glucose 6-phosphatase-α, encoded by G6PC; IGRP, encoded by G6PC2; and glucose 6-phosphatase-β, encoded by G6PC3.

Glucose 6-phosphatase-α and glucose 6-phosphatase-β are both functional phosphohydrolases, and have similar active site structure, topology, mechanism of action, and kinetic properties with respect to G6P hydrolysis. In contrast, IGRP has almost no hydrolase activity, and may play a different role in stimulating pancreatic insulin secretion.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.