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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Bos taurus

for references in articles please use BRENDA:EC5.4.2.11
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EC Tree
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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Bos taurus
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bovine
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PMGE_BOVIN
259
0
30061
Swiss-Prot
other Location (Reliability: 3)
PGAM2_BOVIN
253
0
28685
Swiss-Prot
other Location (Reliability: 3)
PGAM1_BOVIN
254
0
28852
Swiss-Prot
other Location (Reliability: 2)
E1B959_BOVIN
259
0
29995
TrEMBL
other Location (Reliability: 3)
F1MX69_BOVIN
259
0
30070
TrEMBL
other Location (Reliability: 3)
F1N2F2_BOVIN
253
0
28699
TrEMBL
other Location (Reliability: 3)
Q862Q0_BOVIN
137
0
15741
TrEMBL
other Location (Reliability: 2)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Batke, J.; Nazaryan, K.B.; Karapetian, N.H.
Complex of brain D-phosphoglycerate mutase and gamma enolase and its reactivation by D-glycerate 2,3-bisphosphate
Arch. Biochem. Biophys.
264
510-518
1988
Bos taurus
Manually annotated by BRENDA team