Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-7-9
pubmed:abstractText
Enzyme activities forming extracellular products from succinate, fumarate, and malate were examined using washed cell suspensions of Pseudomonas fluorescens from chemostat cultures. Membrane-associated enzyme activities (glucose, gluconate, and malate dehydrogenases), producing large accumulations of extracellular oxidation products in carbon-excess environments, have previously been found in P. fluorescens. Investigations carried out here have demonstrated the presence in this microorganism of a malic enzyme activity which produces extracellular pyruvate from malate in carbon-excess environments. Although the three membrane dehydrogenase enzymes decrease significantly in carbon-limited chemostat cultures, malic enzyme activity was found to increase fourfold under these conditions. The regulation of malate dehydrogenase and malic enzyme by malate or succinate was similar. Malate dehydrogenase increased and malic enzyme decreased in carbon-excess cultures. The opposite effect was observed in carbon-limited cultures. When pyruvate or glucose was used as the carbon source, malate dehydrogenase was regulated similarly by the available carbon concentration, but malic enzyme activity producing extracellular pyruvate was not detected. While large accumulations of extracellular oxalacetate and pyruvate were produced in malate-excess cultures, no extracellular oxidation products were detected in succinate-excess cultures. This may be explained by the lack of detectable activity for the conversion of added external succinate to extracellular fumarate and malate in cells from carbon-excess cultures. In cells from carbon-limited (malate or succinate) cultures, very active enzymes for the conversion of succinate to extracellular fumarate and malate were detected. Washed cell suspensions from these carbon-limited cultures rapidly oxidized added succinate to extracellular pyruvate through the sequential action of succinate dehydrogenase, fumarase, and malic enzyme. Succinate dehydrogenase and fumarase activities producing extracellular products were not detected in cells from chemostat cultures using pyruvate or glucose as the carbon source. Uptake activities for succinate, malate, and pyruvate also were found to increase in carbon-limited (malate or succinate) and decrease in carbon-excess cultures. The role of the membrane-associated enzymes forming different pathways for carbon dissimilation in both carbon-limited and carbon-excess environments is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Ammonia, http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrate Dehydrogenases, http://linkedlifedata.com/resource/pubmed/chemical/Fumarate Hydratase, http://linkedlifedata.com/resource/pubmed/chemical/Fumarates, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Glucose 1-Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Glucose Dehydrogenases, http://linkedlifedata.com/resource/pubmed/chemical/Malate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Malates, http://linkedlifedata.com/resource/pubmed/chemical/Oxaloacetates, http://linkedlifedata.com/resource/pubmed/chemical/Oxaloacetic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Pyruvates, http://linkedlifedata.com/resource/pubmed/chemical/Pyruvic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Succinate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Succinates, http://linkedlifedata.com/resource/pubmed/chemical/Succinic Acid, http://linkedlifedata.com/resource/pubmed/chemical/fumaric acid, http://linkedlifedata.com/resource/pubmed/chemical/gluconate 2-dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/malic acid
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0008-4166
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
396-405
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:6426768-Ammonia, pubmed-meshheading:6426768-Carbohydrate Dehydrogenases, pubmed-meshheading:6426768-Cell Membrane, pubmed-meshheading:6426768-Citric Acid Cycle, pubmed-meshheading:6426768-Fumarate Hydratase, pubmed-meshheading:6426768-Fumarates, pubmed-meshheading:6426768-Glucose, pubmed-meshheading:6426768-Glucose 1-Dehydrogenase, pubmed-meshheading:6426768-Glucose Dehydrogenases, pubmed-meshheading:6426768-Malate Dehydrogenase, pubmed-meshheading:6426768-Malates, pubmed-meshheading:6426768-Oxaloacetates, pubmed-meshheading:6426768-Oxaloacetic Acids, pubmed-meshheading:6426768-Oxidation-Reduction, pubmed-meshheading:6426768-Pseudomonas, pubmed-meshheading:6426768-Pseudomonas fluorescens, pubmed-meshheading:6426768-Pyruvates, pubmed-meshheading:6426768-Pyruvic Acid, pubmed-meshheading:6426768-Succinate Dehydrogenase, pubmed-meshheading:6426768-Succinates, pubmed-meshheading:6426768-Succinic Acid
pubmed:year
1984
pubmed:articleTitle
Membrane enzymes associated with the dissimilation of some citric acid cycle substrates and production of extracellular oxidation products in chemostat cultures of Pseudomonas fluorescens.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't