Enzyme

Download
EC Tree
     5. Isomerases
        5.4 Intramolecular transferases
            5.4.2 Phosphotransferases (phosphomutases)
ID:5.4.2.10
Description:Phosphoglucosamine mutase.
Cath: 3.30.310.50; 3.40.120.10;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 5.4.2.10
BRENDA Enzyme Link: BRENDA 5.4.2.10
KEGG Enzyme Link: KEGG5.4.2.10
BioCyc Enzyme Link: BioCyc 5.4.2.10
ExPASy Enzyme Link: ExPASy5.4.2.10
EC2PDB Enzyme Link: EC2PDB 5.4.2.10
ExplorEnz Enzyme Link: ExplorEnz 5.4.2.10
PRIAM enzyme-specific profiles Link: PRIAM 5.4.2.10
IntEnz Enzyme Link: IntEnz 5.4.2.10
MEDLINE Enzyme Link: MEDLINE 5.4.2.10
MSA:

5.4.2.10;

Phylogenetic Tree:

5.4.2.10;

Uniprot:
M-CSA:
RHEA:23424 alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
RULE(radius=1) ([*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8])>>([*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1])
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Autophosphorylation of phosphoglucosamine mutase from Escherichia coli.Jolly L, Pompeo F, van Heijenoort J, Fassy F, Mengin-Lecreulx D2000 Mar10671448
Reaction mechanism of phosphoglucosamine mutase from Escherichia coli.Jolly L, Ferrari P, Blanot D, Van Heijenoort J, Fassy F, Mengin-Lecreulx D1999 May10231382