Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1999-10-19
pubmed:abstractText
Polyketide synthases (PKSs) are bacterial multienzyme systems that synthesize a broad range of natural products. The 'minimal' PKS consists of a ketosynthase, a chain length factor, an acyl carrier protein and a malonyl transferase. Auxiliary components (ketoreductases, aromatases and cyclases are involved in controlling the oxidation level and cyclization of the nascent polyketide chain. We describe the heterologous expression and reconstitution of several auxiliary PKS components including the actinorhodin ketoreductase (act KR), the griseusin aromatase/cyclase (gris ARO/CYC), and the tetracenomycin aromatase/cyclase (tcm ARO/CYC).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Carrier Protein, http://linkedlifedata.com/resource/pubmed/chemical/Acyl-Carrier Protein..., http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde-Lyases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid Synthetase Complex..., http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/fabD protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/polyketide synthase ketoreductase, http://linkedlifedata.com/resource/pubmed/chemical/tetracenomycin F2 cyclase...
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1074-5521
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
607-15
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10467128-Acyl Carrier Protein, pubmed-meshheading:10467128-Acyl-Carrier Protein S-Malonyltransferase, pubmed-meshheading:10467128-Acyltransferases, pubmed-meshheading:10467128-Alcohol Oxidoreductases, pubmed-meshheading:10467128-Aldehyde-Lyases, pubmed-meshheading:10467128-Bacterial Proteins, pubmed-meshheading:10467128-Chromatography, High Pressure Liquid, pubmed-meshheading:10467128-Cross-Linking Reagents, pubmed-meshheading:10467128-Cyclization, pubmed-meshheading:10467128-Escherichia coli, pubmed-meshheading:10467128-Escherichia coli Proteins, pubmed-meshheading:10467128-Fatty Acid Synthetase Complex, Type II, pubmed-meshheading:10467128-Gene Expression Regulation, Enzymologic, pubmed-meshheading:10467128-Indicators and Reagents, pubmed-meshheading:10467128-Kinetics, pubmed-meshheading:10467128-Molecular Weight, pubmed-meshheading:10467128-Multienzyme Complexes, pubmed-meshheading:10467128-Mutation, pubmed-meshheading:10467128-Recombinant Proteins, pubmed-meshheading:10467128-Streptomyces
pubmed:year
1999
pubmed:articleTitle
Heterologous expression, purification, reconstitution and kinetic analysis of an extended type II polyketide synthase.
pubmed:affiliation
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't