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Information on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent) and Organism(s) Thermoplasma acidophilum and UniProt Accession Q9HL27

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EC Tree
IUBMB Comments
The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.
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Thermoplasma acidophilum
UNIPROT: Q9HL27
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Word Map
The taxonomic range for the selected organisms is: Thermoplasma acidophilum
The enzyme appears in selected viruses and cellular organisms
Synonyms
ipgam, cofactor-independent phosphoglycerate mutase, 3-phosphoglycerate mutase, independent pgm, independent pgam, 2,3-biphosphoglycerate-independent phosphoglycerate mutase, co-factor-independent phosphoglycerate mutase, cofactor independent phosphoglycerate mutase, sso0417, ph0037, more
SYSTEMATIC NAME
IUBMB Comments
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-independent)
The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
-
-
-
r
3-phospho-D-glycerate
2-phospho-D-glycerate
show the reaction diagram
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
vanadate
up to 0.1 mM, 90% maximal inhibition. Inhibition may be partially reversed by EDTA
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
strictly required, Km value 0.017 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
2-phospho-D-glycerate
pH 7.0, 50°C
3.3
3-phospho-D-glycerate
pH 7.0, 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cofactor-dependent isoform
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23800
2 * 23800, calculated, 2 * 24000, SDS-PAGE
24000
2 * 23800, calculated, 2 * 24000, SDS-PAGE
46000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 23800, calculated, 2 * 24000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H23A
no enzymic activity. Like wild-type, mutant forms a dimer
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inhibition of enzyme by vanadate may be partially reversed by EDTA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnsen, U.; Schoenheit, P.
Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea
Extremophiles
11
647-657
2007
Archaeoglobus fulgidus, Thermoplasma acidophilum (Q9HL27)
Manually annotated by BRENDA team