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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1981-2-24
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pubmed:abstractText |
Cells of the aerotolerant anaerobe Giardia lamblia respire in the presence of oxygen. Endogenous respiration is stimulated by glucose but not by other carbohydrates and Krebs cycle intermediates. Endogenous and glucose-stimulated respiration are insensitive to cyanide, malonate, and 2,4-dinitrophenol, but are inhibited by atabrin and iodoacetamide. G. lamblia produces ethanol, acetate and CO2 both aerobically and anaerobically either from endogenous reserves or exogenous glucose. Molecular hydrogen is not produced. The following enzyme activities were detected in homogenates: hexokinase, fructose-biphosphate aldolase, pyruvate kinase, phosphoenolpyruvate carboxykinase, malate dehydrogenase, malate dehydrogenase (decarboxylating), pyruvate synthase, acetyl-CoA synthetase, alcohol dehydrogenase (NADP+), NADH dehydrogenase, NADPH dehydrogenase, NADPH oxidoreductase and superoxide dismutase. The enzymes of energy and carbohydrate metabolism are nonsedimentable (109 000 x g for 30 min). Activities of lactate dehydrogenase, hydrogenase, phosphate acetyltransferase, acetate kinase, citrate synthase, succinate dehydrogenase, fumarate hydratase and catalase were below the limits of detection. The results suggest the occurrence of glycolysis, energy production by substrate level phosphorylation and a flavin, iron-sulfur protein mediated electron transport system as well as the absence of cytochrome mediated oxidative phosphorylation and functional Krebs cycle.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetate-CoA Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Acetates,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Dioxide,
http://linkedlifedata.com/resource/pubmed/chemical/Ethanol,
http://linkedlifedata.com/resource/pubmed/chemical/Ketone Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyruvates
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pubmed:status |
MEDLINE
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pubmed:author | |
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-12
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6108507-Acetate-CoA Ligase,
pubmed-meshheading:6108507-Acetates,
pubmed-meshheading:6108507-Animals,
pubmed-meshheading:6108507-Carbon Dioxide,
pubmed-meshheading:6108507-Energy Metabolism,
pubmed-meshheading:6108507-Ethanol,
pubmed-meshheading:6108507-Giardia,
pubmed-meshheading:6108507-Glycolysis,
pubmed-meshheading:6108507-Ketone Oxidoreductases,
pubmed-meshheading:6108507-Oxidoreductases,
pubmed-meshheading:6108507-Oxygen Consumption,
pubmed-meshheading:6108507-Phosphorylation,
pubmed-meshheading:6108507-Phosphotransferases,
pubmed-meshheading:6108507-Pyruvate Synthase,
pubmed-meshheading:6108507-Pyruvates
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pubmed:articleTitle |
Energy metabolism of the anaerobic protozoon Giardia lamblia.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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