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Information on EC 6.5.1.9 - cyclic 2,3-diphosphoglycerate synthase and Organism(s) Methanothermus fervidus and UniProt Accession O93732

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IUBMB Comments
The enzyme is present in a number of methanogenic archaeal genera that accumulate cyclic 2,3-bisphosphoglycerate as a thermoprotectant. Activity is stimulated by potassium ions.
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This record set is specific for:
Methanothermus fervidus
UNIPROT: O93732
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The taxonomic range for the selected organisms is: Methanothermus fervidus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
Synonyms
cdpgs, cyclic 2,3-diphosphoglycerate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclic 2,3-diphosphoglycerate synthetase
-
cpgS
-
-
-
-
cyclic 2,3-diphosphoglycerate synthetase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
(2R)-2,3-bisphosphoglycerate ligase (cyclizing)
The enzyme is present in a number of methanogenic archaeal genera that accumulate cyclic 2,3-bisphosphoglycerate as a thermoprotectant. Activity is stimulated by potassium ions.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + cyclic 2,3-bisphosphoglycerate
ATP + 2,3-diphospho-D-glycerate
show the reaction diagram
-
-
-
r
ATP + 2,3-diphospho-D-glycerate
ADP + phosphate + cyclic 2,3-bisphosphoglycerate
show the reaction diagram
the enzyme shows a clear preference for the synthetic reaction
-
-
r
ATP + 2,3-diphospho-D-glycerate
ADP + phosphate + cyclic 2,3-bisphosphoglycerate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + cyclic 2,3-bisphosphoglycerate
ATP + 2,3-diphospho-D-glycerate
show the reaction diagram
-
-
-
r
ATP + 2,3-diphospho-D-glycerate
ADP + phosphate + cyclic 2,3-bisphosphoglycerate
show the reaction diagram
the enzyme shows a clear preference for the synthetic reaction
-
-
r
ATP + 2,3-diphospho-D-glycerate
ADP + phosphate + cyclic 2,3-bisphosphoglycerate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
875 mM used in assay conditions
K+
-
the maximally (2.4fold) activating KC1 concentration is 0.5 M
Mg2+
-
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
the enzyme is almost completely inhibited by 5 mM EDTA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.8 - 5.9
2,3-diphospho-D-glycerate
4.1 - 4.7
ADP
3
ATP
41.2 - 44.9
cyclic 2,3-bisphosphoglycerate
-
5.5
2,3-diphospho-D-glycerate
-
at pH 7.0 and 75°C
1.3
ATP
-
at pH 7.0 and 75°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13
2,3-diphospho-D-glycerate
-
at pH 7.0 and 75°C
13
ATP
-
at pH 7.0 and 75°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
native enzyme from crude extract, at pH 7.0 and 83°C
0.15
recombinant enzyme from crude extract, at pH 7.0 and 83°C
15.6
recombinant enzyme after 104fold purification, at pH 7.0 and 83°C
29
native enzyme after 1430fold purification, at pH 7.0 and 83°C
0.02
-
crude extract, at pH 7.0 and 75°C
20.6
-
after 1030fold purification, at pH 7.0 and 75°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
-
the enzyme is active between pH 5.0 and 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
key enzyme of cyclic 2,3-diphosphoglycerate metabolism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
112000
gel filtration
145000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
-
4 * 38000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
phenyl-Sepharose column chromatography, hydroxyapatite column chromatography and Reactive Green 19 agarose column chromatography
Q-Sepharose column chromatography, hydroxyapatite column chromatography, ATP-agarose column chromatography, and 2,3-diphospho-D-glycerate-agarose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL1 Blue cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lehmacher, A.; Vogt, A.B.; Hensel, R.
Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and cyclic 2,3-diphosphoglycerate synthetase from Methanothermus fervidus
FEBS Lett.
272
94-98
1990
Methanothermus fervidus, Methanothermus fervidus DSM 2088
Manually annotated by BRENDA team
Matussek, K.; Moritz, P.; Brunner, N.; Eckerskorn, C.; Hensel, R.
Cloning, sequencing, and expression of the gene encoding cyclic 2,3-diphosphoglycerate synthetase, the key enzyme of cyclic 2,3-diphosphoglycerate metabolism in Methanothermus fervidus
J. Bacteriol.
180
5997-6004
1998
Methanothermus fervidus (O93732), Methanothermus fervidus, Methanothermus fervidus DSM 2088 (O93732)
Manually annotated by BRENDA team