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Information on EC 5.4.2.4 - Bisphosphoglycerate mutase and Organism(s) Gallus gallus

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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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Gallus gallus
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The taxonomic range for the selected organisms is: Gallus gallus
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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-
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2,3-bisphosphoglycerate mutase, erythrocyte
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-
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2,3-bisphosphoglycerate synthase
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-
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2,3-Diphosphoglycerate mutase
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-
-
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2,3-Diphosphoglycerate synthase
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-
-
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2,3-Diphosphoglyceromutase
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-
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Biphosphoglycerate synthase
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-
-
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Bisphosphoglyceromutase
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-
-
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BPG-dependent PGAM
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-
-
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BPGM
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-
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Diphosphoglycerate mutase
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-
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Diphosphoglyceric mutase
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-
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Diphosphoglyceromutase
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-
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DPGM
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-
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Glycerate phosphomutase
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-
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Phosphomutase, glycerate (phosphoglycerate cofactor)
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-
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-Diphosphoglycerate
2,3-Diphosphoglycerate
show the reaction diagram
-
the enzyme has additional activities of EC 5.4.2.1(phosphoglycerate mutase) and EC 3.1.3.13 (bisphosphoglycerate phosphatase)
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na2S2O4
-
stimulation
NaHSO3
-
stimulation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-phosphoglycerate
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-
3-phosphoglycerate
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diphosphate
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phytic acid
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i.e. inositol hexaphosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Phosphoglycolate
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0.02 mM activates
phosphoenolpyruvate
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stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0024 - 0.0028
2,3-diphosphoglycerate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.56
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
embryonic
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGAM1_CHICK
254
0
28898
Swiss-Prot
other Location (Reliability: 3)
Q5ZHV4_CHICK
259
0
29736
TrEMBL
other Location (Reliability: 3)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of EC 5.4.2.1 (phosphoglycerate mutase) and EC 3.1.3.13 (bisphosphoglycerate phosphatase), three activities in one enzyme protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Harkness, D.R.; Isaacks, R.E.; Roth, S.C.
Purification and properties of 2,3-bisphosphoglycerate phosphatase-mutase from erythrocytes of day-old chicks
Eur. J. Biochem.
78
343-351
1977
Gallus gallus
Manually annotated by BRENDA team