Linked Life Data

15546125

Source:http://linkedlifedata.com/resource/pubmed/id/15546125

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
2004-12-1
pubmed:abstractText
Alpha-aminoadipate reductase (AAR), the signature enzyme for lysine biosynthesis in fungi, catalyses the conversion of alpha-aminoadipate to alpha-aminoadipate-semiadehyde in the presence of ATP and NADPH. In Saccharomyces cerevisiae and Candida albicans, the LYS2-encoded AAR is posttranslationally activated by CoA and the LYS5-encoded PPTase. The fission yeast Schizosaccharomyces pombe is evolutionarily highly diverged from S. cerevisiae and C. albicans. We report here several unusual activation characteristics of Sz. pombe Lys1p and Lys7p, isofunctional to Lys2p (AAR) and Lys5p (PPTase), respectively. Unlike the Lys2p from S. cerevisiae and C. albicans, the Sz. pombe Lys1p was active when expressed in E. coli and exhibited significant AAR activity without the addition of CoA or the Sz. pombe Lys7p intron free PPTase. Somewhat higher AAR activity was obtained with the addition of CoA and the Sz. pombe Lys7p PPTase. Substitution of G910A, S913T or S913A in the Sz. pombe Lys1p activation domain (IGGHSI) resulted in no AAR activity. Similarly, substitutions of several amino acid residues in the Sz. pombe Lys7p PPTase domain (G79A, R80K and P81A in Core 1; F93W, D94E, F95W and N96D in Core 1a; G124A, V125I and D126E in Core 2; K172R, E173D and K177R in Core 3) also resulted in no activation of Lys1p and no AAR activity. The Sz. pombe Lys1p amino acid sequence showed a high degree of similarity to other fungal Lys2p proteins; however, the Lys7p amino acid sequence showed much less similarity to other bacterial, fungal and animal PPTases representing several phylogenetic groups.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0749-503X
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1279-88
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15546125-Aldehyde Oxidoreductases, pubmed-meshheading:15546125-Amino Acid Sequence, pubmed-meshheading:15546125-Bacterial Proteins, pubmed-meshheading:15546125-Base Sequence, pubmed-meshheading:15546125-DNA, Fungal, pubmed-meshheading:15546125-Enzyme Activation, pubmed-meshheading:15546125-Escherichia coli, pubmed-meshheading:15546125-L-Aminoadipate-Semialdehyde Dehydrogenase, pubmed-meshheading:15546125-Lysine, pubmed-meshheading:15546125-Molecular Sequence Data, pubmed-meshheading:15546125-Mutagenesis, Site-Directed, pubmed-meshheading:15546125-Phylogeny, pubmed-meshheading:15546125-Polymerase Chain Reaction, pubmed-meshheading:15546125-Protein Processing, Post-Translational, pubmed-meshheading:15546125-Recombinant Proteins, pubmed-meshheading:15546125-Schizosaccharomyces, pubmed-meshheading:15546125-Sequence Analysis, DNA, pubmed-meshheading:15546125-Transferases (Other Substituted Phosphate Groups)
pubmed:year
2004
pubmed:articleTitle
Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe.
pubmed:affiliation
Department of Microbiology, Miami University, Oxford, OH 45056, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.