4op4
Jump to navigation
Jump to search
Crystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound formCrystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound form
Structural highlights
FunctionDAPE_VIBCH Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls (By similarity).[HAMAP-Rule:MF_01690] |
|