6-phosphogluconolactonase
Sign in to saveAlso known as 6-phospho-D-glucono-1,5-lactone lactonohydrolase, phosphogluconolactonase
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:
In the Vinony graph
Within Vinony's link graph, 6-phosphogluconolactonase is referenced by 451 other articles, and connects out to ribose-5-phosphate isomerase, human and malaria.
Vinony files it under EC 3.1.1, Genes on human chromosome 19 and Pentose phosphate pathway.
Its subject is documented across 13 Wikipedia language editions.
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
Wikidata facts
- Image
- 6-phosphogluconolactonase complexed with 6-phosphogluconic acid. PDB- 3E7F.png
Show 2 more facts
- EC enzyme number
- 3.1.1.31
- Commons category
- 6-phosphogluconolactonase
Sources (2)
via Wikidata · CC0
~5 min read
Encyclopedic overview
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.
Excerpted from Wikipedia’s “6-phosphogluconolactonase” article, available under the CC BY-SA 4.0 licence.