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Information on EC 5.4.2.4 - Bisphosphoglycerate mutase and Organism(s) Drosophila melanogaster

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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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Drosophila melanogaster
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
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, 3-phospho-d-glycerate 1,2-phosphomutase, 2,3-diphosphoglycerate synthase, 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?
Q9VGB6_DROME
292
0
32963
TrEMBL
Mitochondrion (Reliability: 5)
Q8MR44_DROME
309
0
34957
TrEMBL
other Location (Reliability: 2)
A5XD89_DROME
255
0
28672
TrEMBL
other Location (Reliability: 2)
A5XD87_DROME
255
0
28583
TrEMBL
other Location (Reliability: 2)
A5XD83_DROME
255
0
28587
TrEMBL
other Location (Reliability: 2)
Q9VAN7_DROME
255
0
28573
TrEMBL
other Location (Reliability: 2)
Q8T8W6_DROME
267
0
30518
TrEMBL
Mitochondrion (Reliability: 5)
Q86BN6_DROME
262
0
29877
TrEMBL
Mitochondrion (Reliability: 5)
A5XD86_DROME
255
0
28686
TrEMBL
other Location (Reliability: 2)
Q86BN5_DROME
253
0
28786
TrEMBL
other Location (Reliability: 2)
A5XD88_DROME
255
0
28672
TrEMBL
other Location (Reliability: 2)