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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Rattus norvegicus
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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: Rattus norvegicus
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
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
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme present in small amounts, distribution of BB-type MB-type and MM-type iszozymes
-
capillary and artery endothelia of the brain, liver and kidney
-
enzyme present in small amounts, distribution of BB-type MB-type and MM-type iszozymes
-
in early fetal life PGAM-BB is the only isozyme present in all tissues, in myogenesis these phenotypes undergo transition to MM-type via an MB-hybrid, all isozymes are present in mature heart tissue, enzyme activity increases with administration of 3,3'-triiodo-D-thyronine to the animal
-
enzyme present in small amounts, distribution of BB-type MB-type and MM-type iszozymes
-
in mammalian skeletal muscles, PGM is organized in a regular, striated fashion within the sarcomere. In the absence of the enzyme effectors, PGM localizes mainly at the M-line, but under conditions typical for contracting muscle, the enzyme accumulates within the I-band of the sarcomere
-
enzyme present in small amounts, distribution of BB-type MB-type and MM-type iszozymes
additional information
-
in early fetal life PGAM-BB is the only isozyme present in all tissues, in myogenesis these phenotypes undergo transition to MM-type via a MB-hybrid
-
in early fetal life PGAM-BB is the only isozyme present in all tissues, in myogenesis these phenotypes undergo transition to MM-type via a MB-hybrid, only MM-type isozyme is present in mature muscle tissue, enzyme activity increases with administration of 3,3'-triiodo-D-thyronine to the animals
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
not in mitochondria, lysosomes, or other cytoplasmic organelles
-
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). PGAM1_RAT
254
0
28832
Swiss-Prot
other Location (Reliability: 2)
PGAM2_RAT
253
0
28755
Swiss-Prot
other Location (Reliability: 4)
Q7TP58_RAT
395
0
45363
TrEMBL
other Location (Reliability: 3)
Q6P6G4_RAT
258
0
30076
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
29000
-
2 * 29000, SDS-PAGE, immunologically the MM-type and BB-type subunits show cross-reactivity as shown by ELISA and immunological neutralization, evidence for common antigenic determinants
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 29000, SDS-PAGE, immunologically the MM-type and BB-type subunits show cross-reactivity as shown by ELISA and immunological neutralization, evidence for common antigenic determinants
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MM-type isozyme and M-subunit from skeletal muscle, BB-type isozyme and B-subunit from brain
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
PGAM1 may have a pathological role of vascular invasion into cancerous tissue
medicine
-
the anti-PGAM1 antibody is a marker of autoimmune hepatitis and a nonspecific marker of central nervous system autoimmune diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Esteller, M.; Urena, J.; Carreras, J.; Martelly, I.; Climent, F.
Thyroid hormone stimulates phosphoglycerate activity and isozyme transition in rat muscle tissues
Life Sci.
54
533-538
1994
Rattus norvegicus
Urena, J.M.; Egea, G.; Grana, X.; Castella, J.; Marsal, J.; Carreras, J.; Climent, F.
Location of phosphoglycerate mutase in rat skeletal muscle. An immunological and biochemical study
Eur. J. Cell Biol.
51
151-156
1990
Rattus norvegicus
Castella, J.; Urena, J.; Ludevid, D.; Carreras, J.; Climent, F.
Immunological properties of rat phosphoglycerate mutase isozymes
Biochim. Biophys. Acta
956
97-102
1988
Rattus norvegicus
Jacobowitz, D.M.; Jozwik, C.; Fukuda, T.; Pollard, H.B.
Immunohistochemical localization of phosphoglycerate mutase in capillary endothelium of the brain and periphery
Microvasc. Res.
76
89-93
2008
Rattus norvegicus
Kowalski, W.; Gizak, A.; Rakus, D.
Phosphoglycerate mutase in mammalian striated muscles: subcellular localization and binding partners
FEBS Lett.
583
1841-1845
2009
Oryctolagus cuniculus, Rattus norvegicus
Kimura, A.; Sakurai, T.; Koumura, A.; Yamada, M.; Hayashi, Y.; Tanaka, Y.; Hozumi, I.; Tanaka, R.; Takemura, M.; Seishima, M.; Inuzuka, T.
High prevalence of autoantibodies against phosphoglycerate mutase 1 in patients with autoimmune central nervous system diseases
J. Neuroimmunol.
219
105-108
2010
Rattus norvegicus
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