Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis.
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.
Born
T L
TL
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, NY 10461, USA.
Blanchard
J S
JS
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*
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