Source:http://linkedlifedata.com/resource/pubmed/id/18077163
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2008-1-21
|
pubmed:abstractText |
Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis and a potential antibiotic target. The enzyme catalyses the condensation of (S)-aspartate semi-aldehyde (ASA) and pyruvate to form dihydrodipicolinate. Constrained diketopimelic acid derivatives have been designed as mimics of the acyclic enzyme-bound condensation product of ASA and pyruvate. Several of the compounds are shown to be active, slow-binding inhibitors with improved inhibition of DHDPS.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
1464-3405
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:day |
15
|
pubmed:volume |
18
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
460-3
|
pubmed:meshHeading | |
pubmed:year |
2008
|
pubmed:articleTitle |
Conformationally constrained diketopimelic acid analogues as inhibitors of dihydrodipicolinate synthase.
|
pubmed:affiliation |
School of Chemistry, University of Melbourne, Vic. 3010, Australia.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|