6-phosphogluconolactonase
Sign in to save6-Phosphogluconolactonase (EC 3.1.1.31, 6PGL, PGLS, systematic name 6-phospho-D-glucono-1,5-lactone lactonohydrolase) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway:
Key facts
- Protein.Name
- 6-phosphogluconolactonase
- Protein.caption
- Crystallized monomer of 6-phosphogluconolactonase from Trypanosoma brucei complexed with 6-phosphogluconic acid
- Protein.image
- 6-phosphogluconolactonase_complexed_with_6-phosphogluconic_acid._PDB-_3E7F.png
- Protein.HGNCid
- 8903
- Protein.Symbol
- PGLS
- Protein.EntrezGene
- 25796
- Protein.OMIM
- 604951
- Protein.RefSeq
- NM_012088
- Protein.UniProt
- O95336
- Protein.ECnumber
- 3.1.1.31
- Protein.Chromosome
- 19
- Protein.Arm
- p
- Protein.Band
- 13.2
via Wikipedia infobox
Article
6 sectionsContents
- Enzyme Mechanism
- Enzyme Structure
- Biological Function
- Disease Relevance
- References
- External links
6-Phosphogluconolactonase (EC 3.1.1.31, 6PGL, PGLS, systematic name 6-phospho-D-glucono-1,5-lactone lactonohydrolase) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
The tertiary structure of 6PGL employs an α/β hydrolase fold, with active site residues clustered on the loops of the α-helices. Based on the crystal structure of the enzyme, the mechanism is proposed to be dependent on proton transfer by a histidine residue in the active site. 6PGL selectively catalyzes the hydrolysis of δ-6-phosphogluconolactone, and has no activity on the γ isomer.