Linked Life Data

18558918

Source:http://linkedlifedata.com/resource/pubmed/id/18558918

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-9-19
pubmed:abstractText
NRPSs (non-ribosomal peptide synthetases) and PKSs (polyketide synthases) require post-translational phosphopantetheinylation to become active. This reaction is catalysed by a PPTase (4'-phosphopantetheinyl transferase). The ppt gene of Penicillium chrysogenum, encoding a protein that shares 50% similarity with the stand-alone large PPTases, has been cloned. This gene is present as a single copy in the genome of the wild-type and high-penicillin-producing strains (containing multiple copies of the penicillin gene cluster). Amplification of the ppt gene produced increases in isopenicillin N and benzylpenicillin biosynthesis. A PPTase-defective mutant (Wis54-PPT(-)) was obtained. It required lysine and lacked pigment and penicillin production, but it still synthesized normal levels of roquefortine. The biosynthesis of roquefortine does not appear to involve PPTase-mediated modification of the synthesizing enzymes. The PPT(-) mutant did not require fatty acids, which indicates that activation of the fatty acid synthase is performed by a different PPTase. Complementation of Wis54-PPT(-) with the ppt gene restored lysine biosynthesis, pigmentation and penicillin production, which demonstrates the wide range of processes controlled by this gene.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1470-8728
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
415
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
317-24
pubmed:meshHeading
pubmed-meshheading:18558918-Bacterial Proteins, pubmed-meshheading:18558918-Blotting, Northern, pubmed-meshheading:18558918-Blotting, Southern, pubmed-meshheading:18558918-Chromatography, High Pressure Liquid, pubmed-meshheading:18558918-Cloning, Molecular, pubmed-meshheading:18558918-Fatty Acids, pubmed-meshheading:18558918-Fungal Proteins, pubmed-meshheading:18558918-Genome, Fungal, pubmed-meshheading:18558918-Heterocyclic Compounds with 4 or More Rings, pubmed-meshheading:18558918-Indoles, pubmed-meshheading:18558918-Lysine, pubmed-meshheading:18558918-Penicillins, pubmed-meshheading:18558918-Penicillium chrysogenum, pubmed-meshheading:18558918-Piperazines, pubmed-meshheading:18558918-Protein Processing, Post-Translational, pubmed-meshheading:18558918-Transferases (Other Substituted Phosphate Groups)
pubmed:year
2008
pubmed:articleTitle
Post-translational enzyme modification by the phosphopantetheinyl transferase is required for lysine and penicillin biosynthesis but not for roquefortine or fatty acid formation in Penicillium chrysogenum.
pubmed:affiliation
Instituto de Biotecnología de León. Parque Científico de León, Av. Real, 1, 24006, León, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't