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Information on EC 5.4.2.4 - Bisphosphoglycerate mutase and Organism(s) Bos taurus

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.2 Phosphotransferases (phosphomutases)
                5.4.2.4 Bisphosphoglycerate mutase
IUBMB Comments
In the direction shown, this enzyme is phosphorylated by 3-phosphoglyceroyl phosphate, to give phosphoenzyme and 3-phosphoglycerate. The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. This enzyme also catalyses, slowly, the reaction of EC 5.4.2.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] and EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)].
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
bisphosphoglycerate mutase, 2,3-bisphosphoglycerate mutase, diphosphoglycerate mutase, bisphosphoglyceromutase, 2,3-bisphosphoglycerate synthase, 2,3-diphosphoglycerate mutase, diphosphoglyceromutase, bpg synthase, 2,3-diphosphoglyceromutase, 3-phospho-d-glycerate 1,2-phosphomutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,3-Bisphosphoglycerate mutase
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2,3-bisphosphoglycerate mutase, erythrocyte
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2,3-bisphosphoglycerate synthase
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2,3-Diphosphoglycerate mutase
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2,3-Diphosphoglycerate synthase
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2,3-Diphosphoglyceromutase
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Biphosphoglycerate synthase
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Bisphosphoglyceromutase
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BPG-dependent PGAM
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BPGM
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Diphosphoglycerate mutase
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Diphosphoglyceric mutase
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Diphosphoglyceromutase
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DPGM
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Glycerate phosphomutase
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Phosphomutase, glycerate (phosphoglycerate cofactor)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3-Phospho-D-glycerate 1,2-phosphomutase
In the direction shown, this enzyme is phosphorylated by 3-phosphoglyceroyl phosphate, to give phosphoenzyme and 3-phosphoglycerate. The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. This enzyme also catalyses, slowly, the reaction of EC 5.4.2.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] and EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)].
CAS REGISTRY NUMBER
COMMENTARY hide
37211-69-1
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PMGE_BOVIN
259
0
30061
Swiss-Prot
other Location (Reliability: 3)
PGAM2_BOVIN
253
0
28685
Swiss-Prot
other Location (Reliability: 3)
PGAM1_BOVIN
254
0
28852
Swiss-Prot
other Location (Reliability: 2)
E1B959_BOVIN
259
0
29995
TrEMBL
other Location (Reliability: 3)
F1MX69_BOVIN
259
0
30070
TrEMBL
other Location (Reliability: 3)
F1N2F2_BOVIN
253
0
28699
TrEMBL
other Location (Reliability: 3)
Q862Q0_BOVIN
137
0
15741
TrEMBL
other Location (Reliability: 2)