Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1982-5-27
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3833-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Purification and properties of 5,10-methenyltetrahydrofolate cyclohydrolase from Clostridium formicoaceticum.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.