Isocitrate lyase purified to homogeneity from Saccharomyces cerevisiae was composed of four identical subunits with a molecular mass of 75 kDa. The enzyme was most active at pH 7.0 in the presence of 5 mM-Mg2+. The Km value for threo-Ds-isocitrate was 1.4 mM. Isocitrate lyase was shown to be thermostable at 50 degrees C for 60 min at a high salt concentration, but rapidly lost activity at -20 degrees C or by dialysis.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Isocitrate lyase purified to homogeneity from Saccharomyces cerevisiae was composed of four identical subunits with a molecular mass of 75 kDa. The enzyme was most active at pH 7.0 in the presence of 5 mM-Mg2+. The Km value for threo-Ds-isocitrate was 1.4 mM. Isocitrate lyase was shown to be thermostable at 50 degrees C for 60 min at a high salt concentration, but rapidly lost activity at -20 degrees C or by dialysis.
|
| skos:exactMatch | |
| uniprot:name |
Yeast
|
| uniprot:author |
Fernandez M.-T.,
Fernandez R.,
Herrero P.,
Lopez-Boado Y.S.,
Moreno F.
|
| uniprot:date |
1988
|
| uniprot:pages |
41-46
|
| uniprot:title |
Purification of isocitrate lyase from Saccharomyces cerevisiae.
|
| uniprot:volume |
4
|
| dc-term:identifier |
doi:10.1002/yea.320040105
|