Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-1-10
pubmed:abstractText
In the anaerobic fungus Neocallimastix sp. L2 fermentation of glucose proceeds via the Embden-Meyerhof-Parnas pathway. Enzyme activities leading to the formation of succinate, lactate, ethanol, and formate are associated with the cytoplasmic fraction. The enzymes 'malic enzyme,' NAD(P)H:ferredoxin oxidoreductase, pyruvate:ferredoxin oxidoreductase, hydrogenase, acetate:succinate CoA transferase and succinate thiokinase leading to the formation of H2,CO2, acetate, and ATP are localized in microbodies. Thus, these organelles are identified as hydrogenosomes. In addition, the microbodies contain the O2-scavenging enzymes NADH- and NADPH oxidase, while NAD(P)H peroxidase, catalase, or superoxide dismutase could not be detected. In cell-free extracts from zoospores of Neocallimastix sp. L2 the specific activities of hydrogenosomal enzymes as well as the quantities of these proteins are 2- to 6-fold higher than in mycelium extracts. These findings suggest that hydrogenosomes perform an important role--especially in zoospores--as H2-evolving, ATP-generating and O2-scavenging organelles.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A-Transferases, http://linkedlifedata.com/resource/pubmed/chemical/D-malate dehydrogenase..., http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase, http://linkedlifedata.com/resource/pubmed/chemical/Hydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Ketone Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Malate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphofructokinase-1, http://linkedlifedata.com/resource/pubmed/chemical/Phosphopyruvate Hydratase, http://linkedlifedata.com/resource/pubmed/chemical/Pyruvate Synthase, http://linkedlifedata.com/resource/pubmed/chemical/Succinate-CoA Ligases, http://linkedlifedata.com/resource/pubmed/chemical/ferredoxin-NAD reductase
pubmed:status
MEDLINE
pubmed:issn
0302-8933
pubmed:author
pubmed:issnType
Print
pubmed:volume
160
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
388-96
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8257282-Adenylate Kinase, pubmed-meshheading:8257282-Animals, pubmed-meshheading:8257282-Camelids, New World, pubmed-meshheading:8257282-Centrifugation, Density Gradient, pubmed-meshheading:8257282-Chytridiomycota, pubmed-meshheading:8257282-Coenzyme A-Transferases, pubmed-meshheading:8257282-Feces, pubmed-meshheading:8257282-Fermentation, pubmed-meshheading:8257282-Glucose, pubmed-meshheading:8257282-Glycolysis, pubmed-meshheading:8257282-Hexokinase, pubmed-meshheading:8257282-Hydrogenase, pubmed-meshheading:8257282-Ketone Oxidoreductases, pubmed-meshheading:8257282-Magnetic Resonance Spectroscopy, pubmed-meshheading:8257282-Malate Dehydrogenase, pubmed-meshheading:8257282-Microbodies, pubmed-meshheading:8257282-Microscopy, Electron, pubmed-meshheading:8257282-Oxidoreductases, pubmed-meshheading:8257282-Phosphofructokinase-1, pubmed-meshheading:8257282-Phosphopyruvate Hydratase, pubmed-meshheading:8257282-Pyruvate Synthase, pubmed-meshheading:8257282-Spectrophotometry, pubmed-meshheading:8257282-Succinate-CoA Ligases
pubmed:year
1993
pubmed:articleTitle
Characterization of hydrogenosomes and their role in glucose metabolism of Neocallimastix sp. L2.
pubmed:affiliation
Department of Microbiology, University of Groningen, The Netherlands.
pubmed:publicationType
Journal Article