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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1983-1-19
pubmed:abstractText
The enzymatic conversion of the D-erythro-dihydroneopterin triphosphate [H2-neopterin-(P)3] to sepiapterin occurs via a nonphosphorylated intermediate as shown by others. We have developed a high-performance liquid chromatography assay for this intermediate and have found that the intermediate (X) and two related compounds (X1 and X2) can be formed nonenzymatically under certain conditions from H2-neopterin-(P)3. The reaction is catalyzed by tris(hydroxymethyl)aminomethane, dependent upon H2-neopterin-(P)3 concentration, significant at temperatures greater than 80 degrees C, and maximal between pH 8.5 and 9.5 (as determined at 25 degrees C). All three compounds were purified, and it was found that both X and X1 can serve as substrates for the enzymatic, NADPH-dependent synthesis of sepiapterin. From the kinetics of formation from H2-neopterin-(P)3 and the similarity of the ultraviolet spectra, it is clear that X, X1, and X2 are closely related compounds. None of the three compounds is reduced by NaBH4; only X1 is sensitive to periodate oxidation. All three can be oxidized with iodine to give rise to highly fluorescent compounds that in turn can be reduced by NaBH4 to give rise to the respective parent compounds. These latter observations indicate that X, X1, and X2 are dihydropterins. These results are discussed relative to the proposed structures for enzymatically produced X. The methods described for the nonenzymatic synthesis of X and its purification should allow preparation of large amounts of X for future study.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3892-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Biosynthesis, nonenzymatic synthesis, and purification of the intermediate in synthesis of sepiapterin in Drosophila.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't