Linked Life Data

728443

Source:http://linkedlifedata.com/resource/pubmed/id/728443

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-3-13
pubmed:abstractText
Uricase (urate:oxygen oxidoreductase, EC 1.7.3.3) of Bacillus fastidiosus was purified to homogeneity in a two-step procedure and was crystallized. The native molecule had a molecular weight of 145 000--150 000 and was composed of subunits of two kinds (Mr = 36 000 and 39 000) in a 1 : 1 ratio. The quaternary structure of the enzyme was reversibly altered, with concomitant loss of activity, at temperatures between 40 and 60 degrees C. No evidence was found for the involvement of metal ions or coenzymes in the uricase reaction. The enzyme was inhibited by various metal ions and by cyanide. The isoelectric point of the enzyme was 4.3, and pH optimum 9.5 and the optimal temperature 30--35 degrees C. Only uric acid was oxidized by the enzyme and 9-methyluric acid, xanthine, 8-azaxanthine and oxonic acid were competitive inhibitors. Uricase synthesis was repressed by allantoin and allantoate, even in the presence of uric acid, which induced synthesis of the enzyme. Molecular oxygen was an important environmental factor in the control of uricase synthesis, probably due to its effect, as cosubstrate in the uricase reaction, in assessing the cytoplasmic concentration of allantoin. The highest amounts of uricase, up to half of the intracellular soluble protein content, was found in cells growing under limited oxygen supply in media containing uric acid as the main substrate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
527
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
348-58
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Uricase of Bacillus fastidiosus. Properties and regulation of synthesis.
pubmed:publicationType
Journal Article