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Title: Methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum

Abstract

Methylenetetrahydrofolate dehydrogenase is widely distributed and has been found in every cell type investigated. The NAD-specific enzyme has been purified to homogeneity from Clostridium formicoaceticum and the NADP-specific enzyme has been obtained from Clostridium thermoaceticum. Other sources of the NADP-specific enzyme are Streptococcus species, Escherichia coli, Clostridium cylindrosporum, Salmonella typhimurium, yeast, liver from various animals, calf thymus, and plants. The NAD-specific enzyme has been demonstrated in Acetobacterium woodii, some methane bacteria, and in Ehrlich ascites tumor cells. Of considerable interest are the observations that in porcine and ovine livers, as well as in yeast, methylenetetrahydrofolate dehydrogenase purified to homogeneity also contains methylenetetrahydrofolate cyclohydrolase and formyltetrahydrofolate synthetase activities. Now it appears that the purified methylenetetrahydrofolate dehydrogenase from C. thermoaceticum also has cyclohydrolase but not synthetase activity. Methylenetetrahydrofolate dehydrogenase has been discussed previously in this series, as has methenyltetrahydrofolate cyclohydrolase. In C. formicoaceticum and C. thermoaceticum these tetrahydrofolate-dependent enzymes participate in a sequence of metabolic reactions by which carbon dioxide is reduced to the methyl group of 5-methyltetrahydrofolate which in turn is utilized for the synthesis of acetate. This pathway provides the mechanism for disposing of reducing equivalents generated in glycolysis.

Authors:
; ; ;
Publication Date:
OSTI Identifier:
6303358
Resource Type:
Journal Article
Journal Name:
Methods Enzymol.; (United States)
Additional Journal Information:
Journal Volume: 66
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CLOSTRIDIUM; PHYSIOLOGY; HYDROLASES; ENZYME ACTIVITY; STRUCTURAL CHEMICAL ANALYSIS; ANAEROBIC DIGESTION; BIOLOGICAL PATHWAYS; METABOLISM; MOLECULAR BIOLOGY; BACTERIA; BIOCONVERSION; DIGESTION; ENZYMES; MANAGEMENT; MICROORGANISMS; PROCESSING; WASTE MANAGEMENT; WASTE PROCESSING; 550200* - Biochemistry; 550700 - Microbiology; 551000 - Physiological Systems

Citation Formats

Ljungdahl, L G, O'Brien, W E, Moore, M R, and Liu, M T. Methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum. United States: N. p., 1980. Web. doi:10.1016/0076-6879(80)66513-6.
Ljungdahl, L G, O'Brien, W E, Moore, M R, & Liu, M T. Methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum. United States. https://doi.org/10.1016/0076-6879(80)66513-6
Ljungdahl, L G, O'Brien, W E, Moore, M R, and Liu, M T. 1980. "Methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum". United States. https://doi.org/10.1016/0076-6879(80)66513-6.
@article{osti_6303358,
title = {Methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum and methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase (combined) from Clostridium thermoaceticum},
author = {Ljungdahl, L G and O'Brien, W E and Moore, M R and Liu, M T},
abstractNote = {Methylenetetrahydrofolate dehydrogenase is widely distributed and has been found in every cell type investigated. The NAD-specific enzyme has been purified to homogeneity from Clostridium formicoaceticum and the NADP-specific enzyme has been obtained from Clostridium thermoaceticum. Other sources of the NADP-specific enzyme are Streptococcus species, Escherichia coli, Clostridium cylindrosporum, Salmonella typhimurium, yeast, liver from various animals, calf thymus, and plants. The NAD-specific enzyme has been demonstrated in Acetobacterium woodii, some methane bacteria, and in Ehrlich ascites tumor cells. Of considerable interest are the observations that in porcine and ovine livers, as well as in yeast, methylenetetrahydrofolate dehydrogenase purified to homogeneity also contains methylenetetrahydrofolate cyclohydrolase and formyltetrahydrofolate synthetase activities. Now it appears that the purified methylenetetrahydrofolate dehydrogenase from C. thermoaceticum also has cyclohydrolase but not synthetase activity. Methylenetetrahydrofolate dehydrogenase has been discussed previously in this series, as has methenyltetrahydrofolate cyclohydrolase. In C. formicoaceticum and C. thermoaceticum these tetrahydrofolate-dependent enzymes participate in a sequence of metabolic reactions by which carbon dioxide is reduced to the methyl group of 5-methyltetrahydrofolate which in turn is utilized for the synthesis of acetate. This pathway provides the mechanism for disposing of reducing equivalents generated in glycolysis.},
doi = {10.1016/0076-6879(80)66513-6},
url = {https://www.osti.gov/biblio/6303358}, journal = {Methods Enzymol.; (United States)},
number = ,
volume = 66,
place = {United States},
year = {Tue Jan 01 00:00:00 EST 1980},
month = {Tue Jan 01 00:00:00 EST 1980}
}