Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1978-8-14
|
| pubmed:abstractText |
3-Hexulosephosphate synthase (HPS), the key enzyme of the hexulosephosphate cycle of formaldehyde fixation, was isolated from facultative methylotroph Pseudomonas oleovorans. Enzyme was purified 100-fold. The purification procedure involved fractionation with ammonium sulfate, gel-filtration on Sephadex G-150 and chromatography on DEAE-Sephadex A-50. The purified enzyme gave single band on analytical polyacrylamide gel electrophoresis. Optimal conditions for activity of HPS are: pH 7,0, temperature 50 degrees C. The molecular weight was calculated to be 45 000 from gel-filtration experiments. HPS is active only in the presence of Mg2+ or Mn2+. Ribulose-5-phosphate is the sole acceptor of formaldehyde. Activity of the enzyme is inhibited by NADH and NADPH.
|
| pubmed:language |
rus
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0320-9725
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
43
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
782-8
|
| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading | |
| pubmed:year |
1978
|
| pubmed:articleTitle |
[Purification and properties of 3-hexulosephosphate synthase from facultative methylotroph Pseudomonas oleovorans].
|
| pubmed:publicationType |
Journal Article,
English Abstract
|