Enzyme

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     5. Isomerases
        5.4 Intramolecular transferases
            5.4.2 Phosphotransferases (phosphomutases)
ID:5.4.2.4
Description:Bisphosphoglycerate mutase.
Alternative Name: Glycerate phosphomutase.
Diphosphoglyceromutase.
Diphosphoglycerate mutase.
BPGM.
Bisphosphoglycerate synthase.
2,3-diphosphoglycerate mutase.
2,3-bisphosphoglycerate synthase.
2,3-bisphosphoglycerate mutase.
Prosite: PDOC00158;
PDB:
PDBScop
Cath: 3.40.50.1240;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.4.2.4
BRENDA Enzyme Link: BRENDA 5.4.2.4
KEGG Enzyme Link: KEGG5.4.2.4
BioCyc Enzyme Link: BioCyc 5.4.2.4
ExPASy Enzyme Link: ExPASy5.4.2.4
EC2PDB Enzyme Link: EC2PDB 5.4.2.4
ExplorEnz Enzyme Link: ExplorEnz 5.4.2.4
PRIAM enzyme-specific profiles Link: PRIAM 5.4.2.4
IntEnz Enzyme Link: IntEnz 5.4.2.4
MEDLINE Enzyme Link: MEDLINE 5.4.2.4
MSA:

5.4.2.4;

Phylogenetic Tree:

5.4.2.4;

Uniprot:
M-CSA:
RHEA:17765 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate + H(+)
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6]-[*:7]-[OH;+0:8]>>[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:8]-[*:7]-[*:6]-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The enzymology of 2,3-bisphosphoglycerate.Rose ZB19806255773
Crystal structure of human B-type phosphoglycerate mutase bound with citrate.Wang Y, Wei Z, Liu L, Cheng Z, Lin Y, Ji F, Gong W2005 Jun 1715883004