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Information on EC 3.1.4.61 - cyclic 2,3-diphosphoglycerate hydrolase
for references in articles please use BRENDA:EC3.1.4.61
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.4 Phosphoric-diester hydrolases
3.1.4.61 cyclic 2,3-diphosphoglycerate hydrolase
IUBMB Comments
The enzyme degrades cyclic 2,3-bisphosphoglycerate, a thermoprotectant that is produced by certain archaeal genera. Two different enzymes that catalyse this activity, one soluble and one membrane-bound, have been characterized from the archaeon Methanothermobacter thermautotrophicus.
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
showSynonyms
cDPG hydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cDPG hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclic 2,3-bisphosphoglycerate + H2O = 2,3-diphosphoglycerate
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SYSTEMATIC NAME
IUBMB Comments
cyclic 2,3-diphosphoglycerate phosphohydrolyase
The enzyme degrades cyclic 2,3-bisphosphoglycerate, a thermoprotectant that is produced by certain archaeal genera. Two different enzymes that catalyse this activity, one soluble and one membrane-bound, have been characterized from the archaeon Methanothermobacter thermautotrophicus.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclic 2,3-bisphosphoglycerate + H2O
2,3-diphosphoglycerate
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Substrates: -
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cyclic 2,3-bisphosphoglycerate + H2O
2,3-diphosphoglycerate
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Substrates: -
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cyclic 2,3-bisphosphoglycerate + H2O
2,3-diphosphoglycerate
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Substrates: -
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additional information
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Substrates: hydrolysis of cDPG occurs under nitrogen or hydrogen atmosphere
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additional information
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Substrates: hydrolysis of cDPG occurs under nitrogen or hydrogen atmosphere
Products: -
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additional information
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Substrates: hydrolysis of cDPG occurs under nitrogen or hydrogen atmosphere
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclic 2,3-bisphosphoglycerate + H2O
2,3-diphosphoglycerate
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Substrates: -
Products: -
Products: -
?
cyclic 2,3-bisphosphoglycerate + H2O
2,3-diphosphoglycerate
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Substrates: -
Products: -
Products: -
?
cyclic 2,3-bisphosphoglycerate + H2O
2,3-diphosphoglycerate
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Substrates: -
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
additional information
-
no activity with Mg2+, Ca2+, and Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
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complete inhibition at 1 mM, the activity can be restored by addition of 2 mM Co2+
additional information
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the enzyme shows activity in presence of O2
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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activation of the cDPG hydrolase is required in contrast to the cDPG synthase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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Michaelis-Menten kinetics determined with the single substrate model
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additional information
additional information
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steady-state kinetics
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30.5
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purified native enzyme, in presence of Co2+, pH 6.0, 60°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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the optimal growth temperature ist 62°C. Large pools of cyclic 2,3-bisphosphoglycerate (cDPG) accumulate at an incubation temperature of 50°C (below optimum). Under these conditions, cellular activity is significantly decreased, a return of the culture to the optimum growth temperature restores the 2,3-DPG pool back to original low levels and causes steady-state cDPG levels to increase again. While 13C02-pulse/12C02-chase experiments at 50°C show that the cDPG turns over, the appearance of 2,3-DPG at NMR-visible concentrations requires at least 10 h
brenda
additional information
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the optimal growth temperature ist 62°C. Large pools of cyclic 2,3-bisphosphoglycerate (cDPG) accumulate at an incubation temperature of 50°C (below optimum). Under these conditions, cellular activity is significantly decreased, a return of the culture to the optimum growth temperature restores the 2,3-DPG pool back to original low levels and causes steady-state cDPG levels to increase again. While 13C02-pulse/12C02-chase experiments at 50°C show that the cDPG turns over, the appearance of 2,3-DPG at NMR-visible concentrations requires at least 10 h
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brenda
additional information
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the optimal growth temperature ist 62°C. Large pools of cyclic 2,3-bisphosphoglycerate (cDPG) accumulate at an incubation temperature of 50°C (below optimum). Under these conditions, cellular activity is significantly decreased, a return of the culture to the optimum growth temperature restores the 2,3-DPG pool back to original low levels and causes steady-state cDPG levels to increase again. While 13C02-pulse/12C02-chase experiments at 50°C show that the cDPG turns over, the appearance of 2,3-DPG at NMR-visible concentrations requires at least 10 h
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
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a membrane-bound cDPG hydrolase is described in the organism. The properties of this isozyme differ very much from the soluble isozyme
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brenda
additional information
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a membrane-bound cDPG hydrolase is described in the organism. The properties of this isozyme differ very much from the soluble isozyme
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brenda
additional information
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a membrane-bound cDPG hydrolase is described in the organism. The properties of this isozyme differ very much from the soluble isozyme
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
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cDPG biosynthesis and hydrolysis is related to the intermediary cell carbon (C3-)metabolism in Methanobacterium thermoautotrophicum. cDPG is synthesized from 2-phosphoglycerate (2-PG) in two subsequent ATP-dependent reactions by cDPG synthase (EC 6.5.1.9). In the intermediary cell carbon metabolism of methanogenic bacteria 2-PG is produced via phosphoenolpyruvate (PEP) from pyruvate, cDPG hydrolysis occurs by the hydrolysis of the diphosphate bonding, followed by the dephosphorylation of 2,3-DPG into phosphoglycerate (3-PG). 2-PG and 3-PG are interconverted by the action of phosphoglycerate mutase
metabolism
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cDPG synthesis and hydrolysis in methanogenic bacteria are catalyzed by two different enzymes: cyclic 2,3-diphosphoglycerate (cDPG) synthetase and cDPG hydrolase. The hydrolase catalyzes the hydrolysis of cyclic 2,3-bisphosphoglycerate to 2,3-diphosphoglycerate. The reverse reaction is catalyzed by cDPG synthetase in an ATP-dependent manner. The routes of cDPG biosynthesis and degradation are interconnected
metabolism
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cDPG biosynthesis and hydrolysis is related to the intermediary cell carbon (C3-)metabolism in Methanobacterium thermoautotrophicum. cDPG is synthesized from 2-phosphoglycerate (2-PG) in two subsequent ATP-dependent reactions by cDPG synthase (EC 6.5.1.9). In the intermediary cell carbon metabolism of methanogenic bacteria 2-PG is produced via phosphoenolpyruvate (PEP) from pyruvate, cDPG hydrolysis occurs by the hydrolysis of the diphosphate bonding, followed by the dephosphorylation of 2,3-DPG into phosphoglycerate (3-PG). 2-PG and 3-PG are interconverted by the action of phosphoglycerate mutase
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metabolism
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cDPG synthesis and hydrolysis in methanogenic bacteria are catalyzed by two different enzymes: cyclic 2,3-diphosphoglycerate (cDPG) synthetase and cDPG hydrolase. The hydrolase catalyzes the hydrolysis of cyclic 2,3-bisphosphoglycerate to 2,3-diphosphoglycerate. The reverse reaction is catalyzed by cDPG synthetase in an ATP-dependent manner. The routes of cDPG biosynthesis and degradation are interconnected
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metabolism
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cDPG biosynthesis and hydrolysis is related to the intermediary cell carbon (C3-)metabolism in Methanobacterium thermoautotrophicum. cDPG is synthesized from 2-phosphoglycerate (2-PG) in two subsequent ATP-dependent reactions by cDPG synthase (EC 6.5.1.9). In the intermediary cell carbon metabolism of methanogenic bacteria 2-PG is produced via phosphoenolpyruvate (PEP) from pyruvate, cDPG hydrolysis occurs by the hydrolysis of the diphosphate bonding, followed by the dephosphorylation of 2,3-DPG into phosphoglycerate (3-PG). 2-PG and 3-PG are interconverted by the action of phosphoglycerate mutase
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metabolism
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cDPG synthesis and hydrolysis in methanogenic bacteria are catalyzed by two different enzymes: cyclic 2,3-diphosphoglycerate (cDPG) synthetase and cDPG hydrolase. The hydrolase catalyzes the hydrolysis of cyclic 2,3-bisphosphoglycerate to 2,3-diphosphoglycerate. The reverse reaction is catalyzed by cDPG synthetase in an ATP-dependent manner. The routes of cDPG biosynthesis and degradation are interconnected
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physiological function
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the function of cDPG may be multiple, cDPG has been suggested to act in storage of energy, phosphorous, or cell carbon. Furthermore, cDPG may play a role in thermostabilization of proteins in extremely thermophilic archaebacteria
physiological function
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the function of cDPG may be multiple, cDPG has been suggested to act in storage of energy, phosphorous, or cell carbon. Furthermore, cDPG may play a role in thermostabilization of proteins in extremely thermophilic archaebacteria
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physiological function
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the function of cDPG may be multiple, cDPG has been suggested to act in storage of energy, phosphorous, or cell carbon. Furthermore, cDPG may play a role in thermostabilization of proteins in extremely thermophilic archaebacteria
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additional information
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large pools of cyclic 2,3-bisphosphoglycerate (cDPG) accumulate at an incubation temperature of 50°C (below optimum). Under these conditions, cellular activity is significantly decreased, a return of the culture to the optimum growth temperature restores the 2,3-DPG pool back to original low levels and causes steady-state cDPG levels to increase again. While 13C02-pulse/12C02-chase experiments at 50°C show that the cDPG turns over, the appearance of 2,3-DPG at NMR-visible concentrations requires at least 10 h
additional information
-
large pools of cyclic 2,3-bisphosphoglycerate (cDPG) accumulate at an incubation temperature of 50°C (below optimum). Under these conditions, cellular activity is significantly decreased, a return of the culture to the optimum growth temperature restores the 2,3-DPG pool back to original low levels and causes steady-state cDPG levels to increase again. While 13C02-pulse/12C02-chase experiments at 50°C show that the cDPG turns over, the appearance of 2,3-DPG at NMR-visible concentrations requires at least 10 h
-
additional information
-
large pools of cyclic 2,3-bisphosphoglycerate (cDPG) accumulate at an incubation temperature of 50°C (below optimum). Under these conditions, cellular activity is significantly decreased, a return of the culture to the optimum growth temperature restores the 2,3-DPG pool back to original low levels and causes steady-state cDPG levels to increase again. While 13C02-pulse/12C02-chase experiments at 50°C show that the cDPG turns over, the appearance of 2,3-DPG at NMR-visible concentrations requires at least 10 h
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native membrane-bound isozyme 27.2fold by ultracentrifugation (3 steps), solubilization through treatment with 25 mM CHAPS, followed by anion exchange and hydrophobic interaction chromatography, Ba2+ salt precipitation, washing with 60% acetone, and cation exchange chromatography
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
van Alebeek, G.; Kreuwels, M.; Keltjens, J.; Vogels, G.
Methanobacterium thermoautotrophicum (strain DELTAH) contains a membrane-bound cyclic 2,3-diphosphoglycerate hydrolase
Arch. Microbiol.
161
514-520
1994
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH, Methanothermobacter thermautotrophicus DSM 1053
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brenda
van Alebeek, G.; Tafazzul, G.; Kreuwels, M.; Keltjens, J.; Vogels, G.
Cyclic 2,3-diphosphoglycerate metabolism in Methanobacterium thermoautotrophicum (strain DELTAH) characterization of the synthetase reaction
Arch. Microbiol.
162
193-198
1994
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH, Methanothermobacter thermautotrophicus DSM 1053
-
brenda
Krishna Sastry, M.; Robertson, D.; Moynihan, J.; Roberts, M.
Enzymic degradation of cyclic 2,3-diphosphoglycerate to 2,3-diphosphoglycerate in Methanobacterium thermoautotrophicum
Biochemistry
31
2926-2935
1992
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH, Methanothermobacter thermautotrophicus DSM 1053
brenda
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