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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Homo sapiens
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5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)IUBMB Comments
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
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Word Map
- 5.4.2.11
- enolase
- aldolase
- isozyme
- 2-phosphoglycerate
- glyceraldehyde-3-phosphate
- glycogen
- creatine
- mutases
-
triosephosphate
-
phosphofructokinase
-
muscle-specific
-
cofactor-independent
- cramp
- myoglobinuria
- triose
- bb
- fructose-2,6-bisphosphatase
-
phosphohistidine
- tpi
-
warburg
- phosphoenzyme
-
fructose-bisphosphate
- aldoa
-
brugia
- malayi
- medicine
- biofuel production
- drug development
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
+
=
+
[enzyme]-L-histidine
+
=
[enzyme]-Ntau-phospho-L-histidine
+
Synonyms
phosphoglycerate mutase, pgam1, phosphoglycerate mutase 1, sts-1, pgam2, cofactor-dependent phosphoglycerate mutase, dpgm-b, bisphosphoglycerate phosphatase, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, rv3214, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-phospho-D-glycerate = 3-phospho-D-glycerate
ping-pong or phosphoenzyme mechanism
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent)
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
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
-
-
-
?
additional information
?
-
-
enzyme possesses some 2,3-bisphosphoglycerate phosphatase activity
-
-
?
additional information
?
-
Mdm2 is a direct binding partner and ubiquitin ligase for the enzyme in cultured cells and in vitro
-
-
?
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-benzyl 4-[(3R,4R,6R)-6-[1-(hex-5-ynoyloxy)-1-methylethyl]-1-oxaspiro[2.5]oct-4-yl] (2R)-2-(2,3-dihydro-1H-indol-3-ylmethyl)butanedioate
i.e. MJE3, spiroepoxide with anti-proliferative effects in human breast cancer cells. MJE3 covalently inactiviates enzyme at K100
2,5-bis(trifluoromethyl)-N-(1,2,8-trihydroxy-9-oxo-9Hxanthen-3-yl)benzenesulfonamide
-
3-(trifluoromethoxy)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
-
3-chloro-N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-2-fluorobenzenesulfonamide
-
3-cyano-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzene-1-sulfonamide
less than 10% inhibition at 0.02 mM
4-(piperidin-1-yl)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
-
4-(pyrrolidin-1-yl)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
-
4-(tert-butyl)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
-
4-(tert-butyl)-N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
-
4-(tert-butyl)-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
4-(trifluoromethyl)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
-
4-bromo-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
4-chloro-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
4-cyano-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzene-1-sulfonamide
less than 10% inhibition at 0.02 mM
4-cyclohexyl-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
-
4-cyclohexyl-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
4-fluoro-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
6-([1,1'-biphenyl]-4-sulfonamido)-8-hydroxy-9-oxo-9H-xanthen-2-yl acetate
-
N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)-[1,10-biphenyl]-4-sulfonamide
-
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-1-phenylmethanesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-2,5-bis(trifluoromethyl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-3-(trifluoromethoxy)benzenesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-(piperidin-1-yl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-(pyrrolidin-1-yl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-(trifluoromethyl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-iodobenzenesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-methylbenzenesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-[1,10-biphenyl]-4-sulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)naphthalene-1-sulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)naphthalene-2-sulfonamide
less than 10% inhibition at 0.02 mM
N-(1-hydroxy-5-methoxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
-
N-(1-hydroxy-5-methyl-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
-
N-(1-hydroxy-7-methoxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
-
N-(1-hydroxy-7-methyl-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
-
N-(1-hydroxy-7-nitro-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
-
N-(7-chloro-1-hydroxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
-
N-(7-fluoro-1-hydroxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
1-phenyl-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)methanesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0063
2,5-bis(trifluoromethyl)-N-(1,2,8-trihydroxy-9-oxo-9Hxanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0102
2,6-dichloro-N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0058
3-(trifluoromethoxy)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0064
3-chloro-N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-2-fluorobenzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0021
3-cyano-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
3-cyano-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzene-1-sulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.001
4-(piperidin-1-yl)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0027
4-(pyrrolidin-1-yl)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0026
4-(tert-butyl)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0084
4-(tert-butyl)-N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
4-(tert-butyl)-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.0035
4-(trifluoromethyl)-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0029
4-bromo-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
4-bromo-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.0036
4-chloro-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
4-chloro-N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
IC50 value above 0.02 mM, at pH 8.0 and 25°C
0.02
4-chloro-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.0042
4-cyano-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
4-cyano-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzene-1-sulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.0005
4-cyclohexyl-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0059
4-cyclohexyl-N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
4-cyclohexyl-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.0055
4-fluoro-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
4-fluoro-N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.0019
4-iodo-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0072
4-methyl-N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0027
6-([1,1'-biphenyl]-4-sulfonamido)-8-hydroxy-9-oxo-9H-xanthen-2-yl acetate
Homo sapiens
at pH 8.0 and 25°C
0.0012
N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)-[1,10-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0028
N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0017
N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)naphthalene-1-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0016
N-(1,2,8-trihydroxy-9-oxo-9H-xanthen-3-yl)naphthalene-2-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0064
N-(1,7-dihydroxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-1-phenylmethanesulfonamide
Homo sapiens
IC50 value above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-2-fluorobenzenesulfonamide
Homo sapiens
IC50 value above 0.02 mM, at pH 8.0 and 25°C
0.0132
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-3,5-difluorobenzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-4-fluorobenzenesulfonamide
Homo sapiens
IC50 value above 0.02 mM, at pH 8.0 and 25°C
0.0101
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-4-iodobenzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-4-methylbenzenesulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0055
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
IC50 value above 0.02 mM, at pH 8.0 and 25°C
0.006
N-(1,8-dihydroxy-9-oxo-9H-xanthen-3-yl)naphthalene-1-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-1-phenylmethanesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-2,5-bis(trifluoromethyl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-3-(trifluoromethoxy)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-(piperidin-1-yl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-(pyrrolidin-1-yl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-(trifluoromethyl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-iodobenzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-4-methylbenzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)-[1,10-biphenyl]-4-sulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)benzenesulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)naphthalene-1-sulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.02
N-(1-hydroxy-2,8-dimethoxy-9-oxo-9H-xanthen-3-yl)naphthalene-2-sulfonamide
Homo sapiens
IC50 value far above 0.02 mM, at pH 8.0 and 25°C
0.0065
N-(1-hydroxy-5-methoxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0086
N-(1-hydroxy-5-methyl-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0046
N-(1-hydroxy-7-methoxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.008
N-(1-hydroxy-7-methyl-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0021
N-(1-hydroxy-7-nitro-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0143
N-(1-hydroxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0035
N-(7-chloro-1-hydroxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
0.0137
N-(7-fluoro-1-hydroxy-9-oxo-9H-xanthen-3-yl)-[1,1'-biphenyl]-4-sulfonamide
Homo sapiens
at pH 8.0 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
patient with hereditary sperocytosis and 50% deficiency of enzyme activity in red blood cells
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the serum of healthy persons contains BB-type isozyme, whereas in patients with Duchenne muscular dystrophy it contains MM-type isozyme
-
enzyme present in small amounts, distribution of BB-type MB-type and MM-type iszozymes
-
distribution in normal brain, astrocytomas, anaplastic astrocytomas, glioblastomas, meningiomas, no difference in subunit-type in normal and tumor brain cells
-
in tumor cells the amount of EC 5.4.2.1 is decreased compared to normal cells
-
enzyme present in small amounts, distribution of BB-type MB-type and MM-type iszozymes
-
adenocarcinoma, in tumor cells EC 5.4.2.1 is found in increased amounts compared to normal cells, in contrast to this a decrease occurs in brain tumor cells
-
enzyme present in small amounts, distribution of BB-type MB-type and MM-type iszozymes
-
enzyme present in small amounts, distribution of BB-type MB-type and MM-type iszozymes
-
adenocarcinoma, squamous cell carcinoma, carcinoid, in tumor cells EC 5.4.2.1 is found in increased amounts compared to normal cells, in contrast to this a decrease occurs in brain tumor cells
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme knockdown significantly inhibits glioma cell proliferation, promotes glioma cell apoptosis, induces S phase cell cycle arrest and inhibits glioma cell migration and invasion in vitro
physiological function
the enzyme is associated with the grade of glioma and is involved in the biological behavior of glioma cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PMGE_HUMAN
259
0
30005
Swiss-Prot
other Location (Reliability: 3)
PGAM1_HUMAN
254
0
28804
Swiss-Prot
other Location (Reliability: 2)
PGAM2_HUMAN
253
0
28766
Swiss-Prot
other Location (Reliability: 3)
PGAM4_HUMAN
254
0
28777
Swiss-Prot
other Location (Reliability: 2)
Q6P6D7_HUMAN
254
0
28820
TrEMBL
other Location (Reliability: 2)
Q6FHK8_HUMAN
254
0
28835
TrEMBL
other Location (Reliability: 2)
Q6FHU2_HUMAN
254
0
28804
TrEMBL
other Location (Reliability: 2)
Q59GR5_HUMAN
147
0
17326
TrEMBL
other Location (Reliability: 4)
C9JH23_HUMAN
78
0
9220
TrEMBL
other Location (Reliability: 3)
A4D2J6_HUMAN
252
0
28220
TrEMBL
other Location (Reliability: 3)
Q0D2Q6_HUMAN
254
0
28792
TrEMBL
other Location (Reliability: 2)
A0A024R782_HUMAN
259
0
30005
TrEMBL
other Location (Reliability: 3)
O00228_HUMAN
75
0
8573
TrEMBL
other Location (Reliability: 2)
Q53G35_HUMAN
254
0
28832
TrEMBL
other Location (Reliability: 2)
PGAM1_HUMAN
254
0
28804
Swiss-Prot
other Location (Reliability: 2)
PMGE_HUMAN
259
0
30005
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
heterodimer structure of phosphoglycerate mutase/bisphosphoglycerate mutase crystallization data
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
Pak1-mediated phosphorylation of phosphoglycerate mutase predisposes the enzyme to ubiquitin-mediated degradation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with citrate, heterodimer structure of phosphoglycerate mutase/bisphosphoglycerate mutase
-
modeling study of enzyme in complex with inhibitor 1-benzyl 4-[(3R,4R,6R)-6-[1-(hex-5-ynoyloxy)-1-methylethyl]-1-oxaspiro[2.5]oct-4-yl] (2R)-2-(2,3-dihydro-1H-indol-3-ylmethyl)butanedioate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K100A
no covalent modification by inhibitor 1-benzyl 4-[(3R,4R,6R)-6-[1-(hex-5-ynoyloxy)-1-methylethyl]-1-oxaspiro[2.5]oct-4-yl] (2R)-2-(2,3-dihydro-1H-indol-3-ylmethyl)butanedioate
M230I
M230I
-
mutation identified in a patient with hereditary sperocytosis and 50% deficiency of enzyme activity in red blood cells. Enzyme shows abnormal behaviour on ion-exchange chromatography and is more thermo-labile than wild-type
M230I
-
mutation identified in a patient with non-spherocytic anemia. 50% reduction of enzyme activity, with normal levels of enzyme protein. Mutation results in decrease of glycolytic metabolites, with the exception of hexose phosphates. In contrast, lactate levels are increased
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
wild-type, 1 h, 10% loss of activity, mutant M230I, 20 min, 50% loss of activity, 1 h, 90% loss of activity. In presence of 2,3-bisphosphoglycerate, both forms remain stable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
erythrocytes, enzyme has activities of bisphosphoglyceromutase and bisphosphoglycerate phosphatase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
stress-induced down-regulation of the enzyme protein is observed in human primary fibroblasts but not in cancer cell lines
the mRNA and protein expression of the enzyme is significantly greater in glioma than normal brain tissues
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
mutation M230I identified in a patient with non-spherocytic anemia. Enzyme activity is reduced by 50%, with normal levels of enzyme protein. Mutation results in decrease of glycolytic metabolites, with the exception of hexose phosphates. In contrast, lactate levels are increased
medicine
-
mutation M230I is identified in a patient with hereditary sperocytosis and 50% deficiency of enzyme activity in red blood cells. Enzyme shows abnormal behaviour on ion-exchange chromatography and is more thermo-labile than wild-type
medicine
PGAM1 plays an important role in hepatocarcinogenesis, is a potential diagnostic biomarker as well as an attractive therapeutic target for hepatocellular carcinoma
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rose, Z.B.
The enzymology of 2,3-bisphosphoglycerate
Adv. Enzymol. Relat. Areas Mol. Biol.
51
211-253
1980
Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, Homo sapiens, Sus scrofa
Durany, N.; Joseph, J.; Cruz-Sanchez, F.F.; Carreras, J.
Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and creatine kinase activity and isoenzymes in human brain tumors
Br. J. Cancer
76
1139-1149
1997
Homo sapiens
Durany, N.; Joseph, J.; Campo, E.; Molina, R.; Carreras, J.
Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas
Br. J. Cancer
75
969-977
1997
Homo sapiens
Durany, N.; Carreras, J.
Distribution of phosphoglycerate mutase isozymes in rat, rabbit and human tissues
Comp. Biochem. Physiol. B
114
217-223
1996
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Grana, X.; Perez de la Ossa, P.; Broceno, C.; Stoecker, M.; Garriga, J.; Puigdomenech, P.; Climent, F.
2,3-Bisphosphoglycerate-independent phosphoglycerate mutase is conserved among different phylogenic kingdoms
Comp. Biochem. Physiol. B
112
287-293
1995
Homo sapiens
Edwards, R.J.; Carter, N.D.; Jeffery, S.; Yates, S.
Purification of human muscle phosphoglycerate mutase by fast protein liquid chromatography based on hydrophobic interactions
J. Chromatogr.
490
424-431
1989
Homo sapiens
Rosa, R.; Calvin, M.C.; Prehu, M.O.; Arous, N.
Purification of human erythrocyte phosphoglyceromutase
J. Chromatogr.
285
203-209
1984
Homo sapiens
Ikura, K.; Narita, H.; Sasaki, R.; Chiba, H.
Immunochemical and enzymatic properties of bisphosphoglyceromutase/phosphatase and phosphoglyceromutase from human erythrocytes
Eur. J. Biochem.
89
23-31
1978
Homo sapiens
Sheibley, R.H.; Hass, L.F.
Isolation and partial characterization of monophosphoglycerate mutase from human erythrocytes
J. Biol. Chem.
251
6699-6704
1976
Homo sapiens
Hass, L.F.; Sheibley, R.H.; Kappel, W.K.; Miller, K.B.
A comparison of some of the physical and chemical properties of the phosphoglycerate mutases from human erythrocytes
Biochem. Biophys. Res. Commun.
72
976-983
1976
Homo sapiens
Sakoda, S.; Shanske, D.; DiMauro, S.; Schon, E.A.
Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family
J. Biol. Chem.
263
16899-16905
1988
Homo sapiens
Shanske, S.; Sakoda, S.; Hermodson, M.A.; DiMauro, S.; Schon, E.A.
Isolation of cDNA encoding the muscle-specific subunit of human phosphoglycerate mutase
J. Biol. Chem.
262
14612-14617
1987
Homo sapiens
Wang, Y.; Wei, Z.; Liu, L.; Cheng, Z.; Lin, Y.; Ji, F.; Gong, W.
Crystal structure of human B-type phosphoglycerate mutase bound with citrate
Biochem. Biophys. Res. Commun.
331
1207-1215
2005
Homo sapiens
de Atauri, P.; Repiso, A.; Oliva, B.; Vives-Corrons, J.L.; Climent, F.; Carreras, J.
Characterization of the first described mutation of human red blood cell phosphoglycerate mutase
Biochim. Biophys. Acta
1740
403-410
2005
Homo sapiens
Repiso, A.; Ramirez Bajo, M.J.; Corrons, J.L.; Carreras, J.; Climent, F.
Phosphoglycerate mutase BB isoenzyme deficiency in a patient with non-spherocytic anemia: familial and metabolic studies
Haematologica
90
257-259
2005
Homo sapiens
Evans, M.J.; Morris, G.M.; Wu, J.; Olson, A.J.; Sorensen, E.J.; Cravatt, B.F.
Mechanistic and structural requirements for active site labeling of phosphoglycerate mutase by spiroepoxides
Mol. Biosyst.
3
495-506
2007
Homo sapiens (P18669), Homo sapiens
Ren, F.; Wu, H.; Lei, Y.; Zhang, H.; Liu, R.; Zhao, Y.; Chen, X.; Zeng, D.; Tong, A.; Chen, L.; Wei, Y.; Huang, C.
Quantitative proteomics identification of phosphoglycerate mutase 1 as a novel therapeutic target in hepatocellular carcinoma
Mol. Cancer
9
81
2010
Homo sapiens (P18669), Homo sapiens
Hakobyan, D.; Nazaryan, K.
Molecular dynamics study of interaction and substrate channeling between neuron-specific enolase and B-type phosphoglycerate mutase
Proteins
78
1691-1704
2010
Homo sapiens
Wang, P.; Jiang, L.; Cao, Y.; Zhang, X.; Chen, B.; Zhang, S.; Huang, K.; Ye, D.; Zhou, L.
Xanthone derivatives as phosphoglycerate mutase 1 inhibitors Design, synthesis, and biological evaluation
Bioorg. Med. Chem.
26
1961-1970
2018
Homo sapiens (P18669)
Mikawa, T.; Maruyama, T.; Okamoto, K.; Nakagama, H.; Lleonart, M.E.; Tsusaka, T.; Hori, K.; Murakami, I.; Izumi, T.; Takaori-Kondo, A.; Yokode, M.; Peters, G.; Beach, D.; Kondoh, H.
Senescence-inducing stress promotes proteolysis of phosphoglycerate mutase via ubiquitin ligase Mdm2
J. Cell Biol.
204
729-745
2014
Mus musculus (O70250), Homo sapiens (P15259)
Wang, P.; Jiang, L.; Cao, Y.; Ye, D.; Zhou, L.
The design and synthesis of n-xanthone benzenesulfonamides as novel phosphoglycerate mutase 1 (PGAM1) inhibitors
Molecules
23
E1396
2018
Homo sapiens (P18669)
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