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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1997-7-3
|
| pubmed:databankReference | |
| pubmed:abstractText |
The GLY1 gene of Saccharomyces cerevisiae is required for the biosynthesis of glycine for cell growth [McNeil, J. B., McIntosh, E. V., Taylor, B. V., Zhang, F-R., Tang, S. & Bognar, A. L. (1994) J. Biol. Chem. 269, 9155-9165], but its gene product has not been identified. We have found that the GLY1 protein is similar in primary structure to L-allo-threonine aldolase of Aeromonas jandiae DK-39, which stereospecifically catalyzes the interconversion of L-allo-threonine and glycine. The GLY1 gene was amplified by PCR, with a designed ribosome-binding site, cloned into pUC118, and expressed in Escherichia coli cells. The enzyme was purified to homogeneity, as judged by polyacrylamide gel electrophoresis. The enzyme has a molecular mass of about 170 kDa and consists of four subunits identical in molecular mass. The enzyme contains 2 mol pyridoxal 5'-phosphate/4 mol of subunit as a cofactor, and its absorption spectrum exhibits maxima at 280 nm and 420 nm. The enzyme catalyzes the cleavage of not only L-allo-threonine to glycine but also L-threonine. We have termed the enzyme a low-specific L-threonine aldolase to distinguish it from L-allo-threonine aldolase.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/GLY1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine Hydroxymethyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
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| pubmed:issn |
0014-2956
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
245
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
289-93
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| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9151955-Aeromonas,
pubmed-meshheading:9151955-Aldehyde-Lyases,
pubmed-meshheading:9151955-Amino Acid Sequence,
pubmed-meshheading:9151955-Base Sequence,
pubmed-meshheading:9151955-Escherichia coli,
pubmed-meshheading:9151955-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:9151955-Glycine,
pubmed-meshheading:9151955-Glycine Hydroxymethyltransferase,
pubmed-meshheading:9151955-Hydrogen-Ion Concentration,
pubmed-meshheading:9151955-Molecular Sequence Data,
pubmed-meshheading:9151955-Molecular Weight,
pubmed-meshheading:9151955-Protein Conformation,
pubmed-meshheading:9151955-Saccharomyces cerevisiae,
pubmed-meshheading:9151955-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9151955-Sequence Alignment,
pubmed-meshheading:9151955-Spectrophotometry, Atomic,
pubmed-meshheading:9151955-Stereoisomerism,
pubmed-meshheading:9151955-Temperature,
pubmed-meshheading:9151955-Threonine
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine--expression of the gene in Escherichia coli and purification and characterization of the enzyme.
|
| pubmed:affiliation |
Laboratory of Biocatalytic Chemistry, Biotechnology Research Centre, Toyama Prefectural University, Kosugi City, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|