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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
31
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pubmed:dateCreated |
1992-9-10
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D11441,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86874,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86875,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86876,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86877,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86878,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86879,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M86880,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S40179,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S42124
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pubmed:abstractText |
Sequencing of an open reading frame 450 bp downstream from the yeast VPS35 gene revealed a putative peptide of 452 amino acids and 52.7 kDa. The predicted amino acid sequence has 45% identity with the 55-kDa subunit of the 6-phosphofructo-2-kinase/fructose-2,6- bisphosphatase (EC 2.7.1.105/EC 3.1.3.46) from rat liver and 42% identity with 480 amino acids in the center of the recently reported 93.5-kDa subunit of yeast 6-phosphofructo-2-kinase (EC 2.7.1.105). The product of the new yeast gene is similar to the entire sequence of the bifunctional rat liver enzyme and, unlike yeast 6-phosphofructo-2-kinase, has the histidine residue essential for fructose-2,6-bisphosphatase activity. Extracts from a chromosomal null mutant strain, fbp26::HIS3, incubated in the presence of [2-32P]fructose 2,6-P2, lacked in autoradiograms the characteristic 56-kDa labeled band observed in wild-type. The same band was intensified 3-fold over wild-type level with the FBP26 gene introduced on multicopy in the fbp26::HIS3 background. A similar increase was found for fructose-2,6-bisphosphatase activity in the same extracts. The FBP26 gene did not cause detectable increase in 6-phosphofructo-2-kinase activity when introduced on multicopy in a pfk26::LEU2 mutant, indicating that its gene product is predominantly a fructose-2,6-bisphosphatase. Growth on glucose, fructose, galactose, pyruvate, and glycerol/lactate was not impaired in strains carrying the fbp26::HIS3 allele.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7126-33
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1322693-Amino Acid Sequence,
pubmed-meshheading:1322693-Animals,
pubmed-meshheading:1322693-Base Sequence,
pubmed-meshheading:1322693-Genes, Fungal,
pubmed-meshheading:1322693-Liver,
pubmed-meshheading:1322693-Molecular Sequence Data,
pubmed-meshheading:1322693-Open Reading Frames,
pubmed-meshheading:1322693-Phosphofructokinase-2,
pubmed-meshheading:1322693-Phosphoric Monoester Hydrolases,
pubmed-meshheading:1322693-Phosphotransferases,
pubmed-meshheading:1322693-Rats,
pubmed-meshheading:1322693-Saccharomyces cerevisiae,
pubmed-meshheading:1322693-Sequence Alignment
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pubmed:year |
1992
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pubmed:articleTitle |
The yeast FBP26 gene codes for a fructose-2,6-bisphosphatase.
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pubmed:affiliation |
Division of Biology, California Institute of Technology, Pasadena 91125.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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