Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1996-2-8
|
pubmed:abstractText |
Three isozymic forms, alpha, beta, and gamma, of Drosophila melanogaster aldolase are produced from a single gene by alternative usage of the triple exons 4 (4 alpha, 4 beta, and 4 gamma) [Shaw-Lee et al. (1992) J. Biol. Chem. 267, 3959-3967; Kim et al. (1992) Mol. Cell. Biol. 12, 773-783; Kai et al. (1992) J. Biochem. 112,677-688]. The expression plasmids for the respective isozymes were transfected into Escherichia coli cells, and the isozymes alpha and beta were purified to homogeneity by a simple procedure, though isozyme gamma was only partially purified. These isozymes are active towards two substrates, fructose-1,6-bisphosphate (Fru-1,6-P2) and fructose-1-phosphate (Fru-1-P), with a preference for Fru-1,6-P2 over Fru-1-P, but they have different kcat/Km values towards these two substrates; isozyme alpha shows the highest value for Fru-1,6-P2. These isozymes show similarity in optimal pHs, thermal stability, and Km values for both Fru-1,6-P2 and Fru-1-P. They are composed of four identical subunits of 40 kDa, forming a tetramer with a molecular weight of approximately 160 kDa. The three isozymes are different in primary structure only at the carboxyl-terminal region encoded by the respective exon 4. Therefore, this region should be primarily responsible for the distinct characteristics of these isozymes.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0021-924X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
118
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
183-8
|
pubmed:dateRevised |
2007-12-19
|
pubmed:meshHeading |
pubmed-meshheading:8537310-Amino Acid Sequence,
pubmed-meshheading:8537310-Animals,
pubmed-meshheading:8537310-Drosophila melanogaster,
pubmed-meshheading:8537310-Enzyme Stability,
pubmed-meshheading:8537310-Escherichia coli,
pubmed-meshheading:8537310-Exons,
pubmed-meshheading:8537310-Fructose-Bisphosphate Aldolase,
pubmed-meshheading:8537310-Genes, Insect,
pubmed-meshheading:8537310-Isoenzymes,
pubmed-meshheading:8537310-Molecular Sequence Data,
pubmed-meshheading:8537310-Recombinant Proteins,
pubmed-meshheading:8537310-Sequence Homology, Amino Acid,
pubmed-meshheading:8537310-Species Specificity,
pubmed-meshheading:8537310-Structure-Activity Relationship,
pubmed-meshheading:8537310-Substrate Specificity,
pubmed-meshheading:8537310-Vertebrates
|
pubmed:year |
1995
|
pubmed:articleTitle |
Drosophila melanogaster aldolase: characterization of the isozymes alpha, beta, and gamma generated from a single gene.
|
pubmed:affiliation |
Department of Biochemistry, Saga Medical School.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|