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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1982-5-27
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pubmed:abstractText |
Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) from Clostridium formicoaceticum has been purified to a specific activity of 469 mumol min-1 mg-1 at 35 degrees C, pH 7.2. The purified enzyme is homogeneous as judged by polyacrylamide disc gel electrophoresis, sedimentation velocity, and gel filtration profiles. The molecular weight is 41,000 +/- 200 as determined by sedimentation equilibrium centrifugation. A subunit molecular weight of approximately 25,500 was obtained using sodium dodecyl sulfate-gel electrophoresis. The enzyme apparently is a dimer. The Stokes radius determined by gel filtration is 29.6 A. The apparent Km at pH 7.2 and 35 degrees C for 5,10-methenyltetrahydrofolate is 0.19 mM. The pure enzyme does not contain any 10-formyltetrahydrofolate synthetase or 5,10-methylenetetrahydrofolate dehydrogenase activities.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
257
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3833-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7061514-Amino Acids,
pubmed-meshheading:7061514-Aminohydrolases,
pubmed-meshheading:7061514-Clostridium,
pubmed-meshheading:7061514-Kinetics,
pubmed-meshheading:7061514-Methenyltetrahydrofolate Cyclohydrolase,
pubmed-meshheading:7061514-Molecular Weight,
pubmed-meshheading:7061514-Protein Conformation,
pubmed-meshheading:7061514-Tetrahydrofolates
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pubmed:year |
1982
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pubmed:articleTitle |
Purification and properties of 5,10-methenyltetrahydrofolate cyclohydrolase from Clostridium formicoaceticum.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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