title: Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis.
abstract: 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.
authors.affiliation: Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, NY 10461, USA.
authors.forename: T L
authors.initials: TL
authors.lastname: Born
authors.forename: J S
authors.initials: JS
authors.lastname: Blanchard
mesh_terms: D000217:Acyltransferases / Q000378:metabolism*; D000581:Amidohydrolases / Q000378:metabolism*; D000591:Amino Acid Isomerases / Q000378:metabolism*; D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism*; D003960:Diaminopimelic Acid / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D013329:Structure-Activity Relationship; D051277:Succinyldiaminopimelate Transaminase; D000637:Transaminases / Q000378:metabolism*
chemical_list: D000217:Acyltransferases; D000581:Amidohydrolases; D000591:Amino Acid Isomerases; D000594:Amino Acid Oxidoreductases; D003960:Diaminopimelic Acid; D051277:Succinyldiaminopimelate Transaminase; D000637:Transaminases; C020032:diaminopimelate dehydrogenase; C040777:succinyl-CoA-tetrahydrodipicolinate N-succinyltransferase; C054685:N-succinyl-l,l-diaminopimelic acid desuccinylase; C042032:diaminopimelate epimerase