Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1999-11-16
pubmed:abstractText
Within the past 18 months work has continued on the structure and mechanisms of enzymes involved in the diaminopimelic acid/lysine biosynthetic pathway. A novel structure has been determined for a PLP-independent epimerase, and structures with bound substrates have been solved for two other enzymes. Additionally, new studies have appeared describing the chemical mechanisms of three enzymes in the pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Isomerases, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Diaminopimelic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Succinyldiaminopimelate Transaminase, http://linkedlifedata.com/resource/pubmed/chemical/Transaminases, http://linkedlifedata.com/resource/pubmed/chemical/diaminopimelate dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/diaminopimelate epimerase, http://linkedlifedata.com/resource/pubmed/chemical/succinyl-CoA-tetrahydrodipicolinate..., http://linkedlifedata.com/resource/pubmed/chemical/succinyldiaminopimelate...
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1367-5931
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
607-13
pubmed:dateRevised
2009-8-25
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis.
pubmed:affiliation
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, NY 10461, USA.
pubmed:publicationType
Journal Article, Review