Linked Life Data

2266128

Source:http://linkedlifedata.com/resource/pubmed/id/2266128

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1991-2-14
pubmed:databankReference
pubmed:abstractText
We have cloned and sequenced the Saccharomyces cerevisiae gene for S-adenosylmethionine decarboxylase. This enzyme contains covalently bound pyruvate which is essential for enzymatic activity. We have shown that this enzyme is synthesized as a Mr 46,000 proenzyme which is then cleaved post-translationally to form two polypeptide chains: a beta subunit (Mr 10,000) from the amino-terminal portion and an alpha subunit (Mr 36,000) from the carboxyl-terminal portion. The protein was overexpressed in Escherichia coli and purified to homogeneity. The purified enzyme contains both the alpha and beta subunits. About half of the alpha subunits have pyruvate blocking the amino-terminal end; the remaining alpha subunits have alanine in this position. From a comparison of the amino acid sequence deduced from the nucleotide sequence with the amino acid sequence of the amino-terminal portion of each subunit (determined by Edman degradation), we have identified the cleavage site of the proenzyme as the peptide bond between glutamic acid 87 and serine 88. The pyruvate moiety, which is essential for activity, is generated from serine 88 during the cleavage. The amino acid sequence of the yeast enzyme has essentially no homology with S-adenosylmethionine decarboxylase of E. coli (Tabor, C. W., and Tabor, H. (1987) J. Biol. Chem. 262, 16037-16040) and only a moderate degree of homology with the human and rat enzymes (Pajunen, A., Crozat, A., Jänne, O. A., Ihalainen, R., Laitinen, P. H., Stanley, B., Madhubala, R., and Pegg, A. E. (1988) J. Biol. Chem. 263, 17040-17049); all of these enzymes are pyruvoyl-containing proteins. Despite this limited overall homology the cleavage site of the yeast proenzyme is identical to the cleavage sites in the human and rat proenzymes, and seven of the eight amino acids adjacent to the cleavage site are identical in the three eukaryote enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22321-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2266128-Adenosylmethionine Decarboxylase, pubmed-meshheading:2266128-Amino Acid Sequence, pubmed-meshheading:2266128-Animals, pubmed-meshheading:2266128-Base Sequence, pubmed-meshheading:2266128-Cloning, Molecular, pubmed-meshheading:2266128-Enzyme Precursors, pubmed-meshheading:2266128-Escherichia coli, pubmed-meshheading:2266128-Genetic Vectors, pubmed-meshheading:2266128-Humans, pubmed-meshheading:2266128-Kinetics, pubmed-meshheading:2266128-Macromolecular Substances, pubmed-meshheading:2266128-Molecular Sequence Data, pubmed-meshheading:2266128-Molecular Weight, pubmed-meshheading:2266128-Plasmids, pubmed-meshheading:2266128-Protein Processing, Post-Translational, pubmed-meshheading:2266128-Rats, pubmed-meshheading:2266128-Recombinant Proteins, pubmed-meshheading:2266128-Restriction Mapping, pubmed-meshheading:2266128-Saccharomyces cerevisiae, pubmed-meshheading:2266128-Sequence Homology, Nucleic Acid, pubmed-meshheading:2266128-Spermidine
pubmed:year
1990
pubmed:articleTitle
Spermidine biosynthesis in Saccharomyces cerevisiae. Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase.
pubmed:affiliation
Section on Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, Food and Drug Administration, Bethesda, Maryland 20892.
pubmed:publicationType
Journal Article, Comparative Study