Edge Rewrite
// HTMLRewriter · presentation

This page was redesigned at the edge.

Cloudflare fetched the original article and streamed it through HTMLRewriter to apply an entirely new visual system without rebuilding the source page.

// request.cf · coarse context

A page that knows where it met you.

Only coarse request metadata is shown. This demo does not display or persist visitor IP addresses.

Country
US
Cloudflare location
CMH
Connection
HTTP/2
Language
Not provided

Ray ID: a229c1f0d84b8020

Jump to content

Beta-phosphoglucomutase

From Wikipedia, the free encyclopedia
β-Phosphoglucomutase
Identifiers
EC no.5.4.2.6
CAS no.68651-99-0
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a β-phosphoglucomutase (EC 5.4.2.6) is an enzyme that catalyzes the chemical reaction

β-D-glucose 1-phosphate β-D-glucose 6-phosphate

Hence, this enzyme has one substrate, β-D-glucose 1-phosphate, and one product, β-D-glucose 6-phosphate.

This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is beta-D-glucose 1,6-phosphomutase. This enzyme participates in starch and sucrose metabolism.

Structural studies

[edit]

20 structures have been solved for this enzyme PDB. Some of the accession codes are PDB: 1LVH, PDB: 1O03, PDB: 1O08, PDB: 1Z4N, PDB: 1Z4O, and PDB: 1ZOL. Most of these structures detail metal fluoride analogue complexes which are used to mimic different states along the reaction coordinate.

References

[edit]
  • Ben-Zvi R, Schramm M (1961). "A phosphoglucomutase specific for beta-glucose 1-phosphate". J. Biol. Chem. 236 (8): 2186–2189. doi:10.1016/S0021-9258(18)64053-0.
  • Boyer PD, ed. (1972). The Enzymes. Vol. 6 (3rd ed.). pp. 407–477.