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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1989-1-5
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pubmed:abstractText |
High-molecular-mass proteins from pea (Pisum sativum) mitochondrial matrix retained on an XM-300 Diaflo membrane ('matrix extract') exhibited high rates of glycine oxidation in the presence of NAD+ and tetrahydropteroyl-L-glutamic acid (H4 folate) as long as the medium exhibited a low ionic strength. Serine hydroxymethyltransferase (SHMT) (4 x 53 kDa) and the four proteins of the glycine-cleavage system, including a pyridoxal phosphate-containing enzyme ('P-protein'; 2 x 97 kDa), a carrier protein containing covalently bound lipoic acid ('H-protein'; 15.5 kDa), a protein exhibiting lipoamide dehydrogenase activity ('L-protein'; 2 x 61 kDa) and an H4 folate-dependent enzyme ('T-protein'; 45 kDa) have been purified to apparent homogeneity from the matrix extract by using gel filtration, ion-exchange and phenyl-Superose fast protein liquid chromatography. Gel filtration on Sephacryl S-300 in the presence of 50 mM-KCl proved to be the key step in disrupting this complex. During the course of glycine oxidation catalysed by the matrix extract a steady-state equilibrium in the production and utilization of 5,10-methylene-H4 folate was reached, suggesting that glycine cleavage and SHMT are linked together via a soluble pool of H4 folate. The rate of glycine oxidation catalysed by the matrix extract was sensitive to the NADH/NAD+ molar ratios, because NADH competitively inhibited the reaction catalysed by lipoamide dehydrogenase.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-1259444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-16662139,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-16662959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-16665241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-3080433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-3090936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-3619448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-4289245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-4338934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-4342337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-4414614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-5862401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-5901047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-6750353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-6863283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-7036682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-7053363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-7400147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3143355-7440562
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5,10-methylenetetrahydrofolate,
http://linkedlifedata.com/resource/pubmed/chemical/5,6,7,8-tetrahydrofolic acid,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Aminomethyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine Decarboxylase Complex...,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine Dehydrogenase...,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine Hydroxymethyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxymethyl and Formyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pyruvate Dehydrogenase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Tetrahydrofolates,
http://linkedlifedata.com/resource/pubmed/chemical/Thioctic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/dihydrolipoic acid,
http://linkedlifedata.com/resource/pubmed/chemical/glycine cleavage system
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
255
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
169-78
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:3143355-Amino Acid Oxidoreductases,
pubmed-meshheading:3143355-Aminomethyltransferase,
pubmed-meshheading:3143355-Carrier Proteins,
pubmed-meshheading:3143355-Chromatography, Gel,
pubmed-meshheading:3143355-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3143355-Glycine,
pubmed-meshheading:3143355-Glycine Decarboxylase Complex H-Protein,
pubmed-meshheading:3143355-Glycine Dehydrogenase (Decarboxylating),
pubmed-meshheading:3143355-Glycine Hydroxymethyltransferase,
pubmed-meshheading:3143355-Hydroxymethyl and Formyl Transferases,
pubmed-meshheading:3143355-Mitochondria,
pubmed-meshheading:3143355-Multienzyme Complexes,
pubmed-meshheading:3143355-NAD,
pubmed-meshheading:3143355-Oxidation-Reduction,
pubmed-meshheading:3143355-Plant Proteins,
pubmed-meshheading:3143355-Plants,
pubmed-meshheading:3143355-Pyruvate Dehydrogenase Complex,
pubmed-meshheading:3143355-Tetrahydrofolates,
pubmed-meshheading:3143355-Thioctic Acid,
pubmed-meshheading:3143355-Transferases
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pubmed:year |
1988
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pubmed:articleTitle |
Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase.
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pubmed:affiliation |
Département de Recherche Fondamentale, Centre d'Etudes Nucléaires et Université Joseph Fourier, Grenoble, France.
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pubmed:publicationType |
Journal Article
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