Linked Life Data

8001737

Source:http://linkedlifedata.com/resource/pubmed/id/8001737

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1995-1-25
pubmed:abstractText
The animal fatty acid synthase comprises two multifunctional polypeptide chains, each containing seven discrete functional domains, juxtaposed head-to-tail such that two separate centers for fatty acid assembly are formed at the subunit interface. The kinetics and specificities of the component enzymes are well adapted to ensure that, at each of the two centers, the iterative condensation of an acetyl moiety with successive malonyl moieties and complete reduction of the beta-keto intermediates normally results in the formation of palmitic acid as the major product. Nevertheless, utilization of alternative substrates and alternative chain-terminating mechanisms can extend the range of products to include branched-chain, odd carbon-numbered, and shorter chain-length fatty acids. The potential of this multifunctional form of molecular architecture for the elaboration of more complex natural products has been further exploited in microorganisms that, by the use of different fatty acid synthase "modules" that perform variable beta-carbon processing at successive elongation steps, generate a structurally diverse family of polyketides retaining keto, hydroxyl, enoyl, or alkyl functions at specific positions in the carbon chain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1248-59
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The animal fatty acid synthase: one gene, one polypeptide, seven enzymes.
pubmed:affiliation
Children's Hospital Oakland Research Institute, California 94609.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't