Enzymatic degradation of cyclic 2,3-diphosphoglycerate to 2,3-diphosphoglycerate in Methanobacterium thermoautotrophicum

2,3-Diphosphoglycerate (2,3-DPG) has been found to be the product of the enzymatic degradation of cyclic 2,3-diphosphoglycerate (cDPG) in the archaebacterium Methanobacterium thermoautotrophicum delta H. Although 2,3-DPG has not previously been detected as a major soluble component of M. thermoautot...

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Published in:Biochemistry (Easton) Vol. 31; no. 11; pp. 2926 - 2935
Main Authors: Sastry, Musti V. Krishna, Robertson, Diane E, Moynihan, James A, Roberts, Mary F
Format: Journal Article
Language:English
Published: Washington, DC American Chemical Society 24-03-1992
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Abstract 2,3-Diphosphoglycerate (2,3-DPG) has been found to be the product of the enzymatic degradation of cyclic 2,3-diphosphoglycerate (cDPG) in the archaebacterium Methanobacterium thermoautotrophicum delta H. Although 2,3-DPG has not previously been detected as a major soluble component of M. thermoautotrophicum, large pools accumulated at an incubation temperature of 50 degrees C (below the optimum growth temperature of 62 degrees C). Under these conditions, cellular activity was significantly decreased; a return of the culture to the optimum growth temperature restored the 2,3-DPG pool back to original low levels and caused steady-state cDPG levels to increase again. While 13CO2-pulse/12CO2-chase experiments at 50 degrees C showed that the cDPG turned over, the appearance of 2,3-DPG at NMR-visible concentrations required at least 10 h. Production of 2,3-DPG in vivo was prevented by exposure of the cells to O2. The enzyme responsible for this hydrolysis of cDPG was purified by affinity chromatography and appears to be a 33-kDa protein. Activity was detected in the presence of oxygen and was enhanced by a solution of 1 M KCl, 25 mM MgCl2, and dithiothreitol. Both Km and Vmax have been determined at 37 degrees C; kinetics also indicate that in vitro the product, 2,3-DPG, is an inhibitor of cDPG hydrolysis. These findings are discussed in view of a proposed role for cDPG in methanogens.
AbstractList 2,3-Diphosphoglycerate (2,3-DPG) has been found to be the product of the enzymatic degradation of cyclic 2,3-diphosphoglycerate (cDPG) in the archaebacterium Methanobacterium thermoautotrophicum delta H. Although 2,3-DPG has not previously been detected as a major soluble component of M. thermoautotrophicum, large pools accumulated at an incubation temperature of 50 degrees C (below the optimum growth temperature of 62 degrees C). Under these conditions, cellular activity was significantly decreased; a return of the culture to the optimum growth temperature restored the 2,3-DPG pool back to original low levels and caused steady-state cDPG levels to increase again. While 13CO2-pulse/12CO2-chase experiments at 50 degrees C showed that the cDPG turned over, the appearance of 2,3-DPG at NMR-visible concentrations required at least 10 h. Production of 2,3-DPG in vivo was prevented by exposure of the cells to O2. The enzyme responsible for this hydrolysis of cDPG was purified by affinity chromatography and appears to be a 33-kDa protein. Activity was detected in the presence of oxygen and was enhanced by a solution of 1 M KCl, 25 mM MgCl2, and dithiothreitol. Both Km and Vmax have been determined at 37 degrees C; kinetics also indicate that in vitro the product, 2,3-DPG, is an inhibitor of cDPG hydrolysis. These findings are discussed in view of a proposed role for cDPG in methanogens.
2,3-Diphosphoglycerate (2,3-DPG) has been found to be the product of the enzymatic degradation of cyclic 2,3-diphosphoglycerate (cDPG) in the archaebacterium Methanobacterium thermoautotrophicum Delta H. The enzyme responsible for hydrolysis of cDPG was purified by affinity chromatography and appears to be a 33-kDa protein. Activity was detected in the presence of oxygen and was enhanced by a solution of 1 M KCl, 25 mM MgCl sub(2), and dithiothreitol. Both K sub(m) and V sub(max) have been determined at 37 degree C; kinetics also indicate that in vitro the product, 2,3-DPG, is an inhibitor of cDPG hydrolysis.
2,3-Diphosphoglycerate (2,3-DPG) has been found to be the product of the enzymatic degradation of cyclic 2,3-diphosphoglycerate (cDPG) in the archaebacterium Methanobacterium thermoautotrophicum {Delta}H. Although 2,3-DPG has not previously been detected as a major soluble component of M. thermoautotrophicum, large pools accumulated at an incubation temperature of 50C. Under these conditions, cellular activity was significantly decreased; a return of the culture to the optimum growth temperature restored the 2,3-DPG pool back to original low levels and caused steady-state cDPG levels to increase again. While {sup 13}CO{sub 2}-pulse/{sup 12}CO{sub 2}-chase experiments at 50C showed that the cDPG turned over, the appearance of 2,3-DPG at NMR-visible concentrations required at least 10 h. Production of 2,3-DPG in vivo was prevented by exposure of the cells to O{sub 2}. the enzyme responsible for this hydrolysis of cDPG was purified by affinity chromatography and appears to be a 33-kDa protein. Activity was detected in the presence of oxygen and was enhanced by a solution of 1 M KCl, 25 mM MgCl{sub 2}, and dithiothreitol. Both K{sub m} and V{sub max} have been determined at 37C; kinetics also indicate that in vitro the product, 2,3-DPG, is an inhibitor of cDPG hydrolysis. These findings are discussed in view of a proposed role for cDPG in methanogens.
Author Sastry, Musti V. Krishna
Roberts, Mary F
Robertson, Diane E
Moynihan, James A
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Issue 11
Keywords Temperature
Archaeobacteria
Enzyme
Environmental factor
2,3-Diphosphoglycerate
Enzymatic activity
Cyclic compound
Methanobacteriaceae
Enzymatic digestion
Bacteria
Kinetic parameter
Methanobacteriales
Methanobacterium thermoautotrophicum
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Snippet 2,3-Diphosphoglycerate (2,3-DPG) has been found to be the product of the enzymatic degradation of cyclic 2,3-diphosphoglycerate (cDPG) in the archaebacterium...
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SubjectTerms 2,3-Diphosphoglycerate
550601 - Medicine- Unsealed Radionuclides in Diagnostics
BACTERIA
Bacteriology
BIOCHEMICAL REACTION KINETICS
BIODEGRADATION
Biological and medical sciences
CARBOHYDRATES
CARBON 12
CARBON 13
CARBON COMPOUNDS
CARBON DIOXIDE
CARBON ISOTOPES
CARBON OXIDES
CHALCOGENIDES
CHEMICAL REACTIONS
CHEMICAL SHIFT
Chromatography, Affinity
cyclic 2,3-diphosphoglycerate
DECOMPOSITION
Diphosphoglyceric Acids - metabolism
ENZYMATIC HYDROLYSIS
ESTERS
EVEN-EVEN NUCLEI
EVEN-ODD NUCLEI
Fundamental and applied biological sciences. Psychology
Hydrolases - chemistry
Hydrolases - isolation & purification
Hydrolases - metabolism
HYDROLYSIS
ISOTOPES
KINETICS
LIGHT NUCLEI
LIPIDS
LYSIS
MAGNETIC RESONANCE
Magnetic Resonance Spectroscopy
Metabolism. Enzymes
Methanobacterium - enzymology
METHANOGENIC BACTERIA
Microbiology
MICROORGANISMS
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
OXIDES
Oxygen - pharmacology
OXYGEN COMPOUNDS
PHOSPHOLIPIDS
Potassium Chloride - pharmacology
RADIOLOGY AND NUCLEAR MEDICINE
REACTION KINETICS
RESONANCE
SOLVOLYSIS
Spectrophotometry
STABLE ISOTOPES
Temperature
Title Enzymatic degradation of cyclic 2,3-diphosphoglycerate to 2,3-diphosphoglycerate in Methanobacterium thermoautotrophicum
URI http://dx.doi.org/10.1021/bi00126a012
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Volume 31
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