4op4
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Crystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound form
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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] Contents | ||||||||||||||||||||
This page was last modified 12:41, 1 March 2024.