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Enzyme Nomenclature
Information on EC 5.4.2.1 - phosphoglycerate mutase
for references in articles please use BRENDA:EC5.4.2.1
Word Map on EC 5.4.2.1
- 5.4.2.1
- phosphoglucomutase
-
torrent
-
glycolytic
- gpi
-
next-generation
- starch
-
allozyme
-
mucin
-
sanger
-
machine
- yersinia
- acp
-
hardy-weinberg
- pestis
-
miseq
- diptera
-
semiconductor
-
multilocus
- 2-phosphoglycerate
-
ampliseq
- glucose-1-phosphate
- cline
- 2,3-bisphosphoglycerate
-
monomorphic
-
barcoded
-
isoenzymatic
-
rhodium
-
mutases
-
cofactor-independent
-
starch-gel
- phosphomannomutase
-
benchtop
-
zymodemes
- phlebotomus
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
5.4.2.1
transferred to EC 5.4.2.11, EC 5.4.2.12. Now recognized as two separate enzymes 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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RECOMMENDED NAME
GeneOntology No.
phosphoglycerate mutase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
-
the enzyme is involved in glycogen catabolism
metabolism
-
despite the low level of PGM present in the cell, the enzyme is not rate limiting for glycolysis in Lactococcus lactis, probably due to a high catalytic processivity
metabolism
-
despite the low level of PGM present in the cell, the enzyme is not rate limiting for glycolysis in Lactococcus lactis, probably due to a high catalytic processivity
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
-
-
-
r
3-phospho-D-glycerate
2-phospho-D-glycerate
-
-
-
-
?
3-phospho-D-glycerate
2-phospho-D-glycerate
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
2,3-bisphosphoglycerate is not required as a cofactor
-
additional information
2,3-bisphosphoglycerate is not required as a cofactor
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
metavanadate
-
less than 5% residual activity at 10 mM after 10 min incubation
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-bisphosphoglyceric acid
-
dependent on 2,3-bisphosphoglyceric acid for activity
Cysteine hydrochloride
-
phosphoglycerate mutase activity requires the reductant dithiothreitol, cysteine hydrochloride, or glutathione for full activity
dithiothreitol
-
phosphoglycerate mutase activity requires the reductant dithiothreitol, cysteine hydrochloride, or glutathione for full activity
glutathione
-
phosphoglycerate mutase activity requires the reductant dithiothreitol, cysteine hydrochloride, or glutathione for full activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
3-phospho-D-glycerate
in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C
0.58
3-phospho-D-glycerate
in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C
1.03
3-phospho-D-glycerate
-
in triethanol-HCl buffer (125 mM, pH 7.2, 5 mM MgCl2, 10 mM KCl), 0.1 mM 2,3-bisphosphoglyceric acid, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
102
3-phospho-D-glycerate
in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C
132
3-phospho-D-glycerate
in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C
3200
3-phospho-D-glycerate
-
in triethanol-HCl buffer (125 mM, pH 7.2, 5 mM MgCl2, 10 mM KCl), 0.1 mM 2,3-bisphosphoglyceric acid, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
186
3-phospho-D-glycerate
in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C
228
3-phospho-D-glycerate
in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
71
in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56000
x * 56000, calculated from amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
?
x * 56000, calculated from amino acid sequence
homotetramer
-
2 * 26000, calculated from amino acid sequence
homotetramer
-
2 * 26000, calculated from amino acid sequence
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap nickel chelating column chromatography and HiTrap Q column chromatography
HiTrap nickel chelating column chromatography and HiTrap Q column chromatography
HiTrap nickel chelating column chromatography and HiTrap Q column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C2566/T7 cells
expressed in Escherichia coli C2566/T7 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 5.4.2.1)
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