| Description | N(5)-(carboxyethyl)ornithine synthase (CEOS) catalyses the NADP-dependent conversion of N5-(L-1-carboxyethyl)-L-ornithine to L-ornithine pyruvate. CEOS is related to the NAD-dependent L-alanine dehydrogenases [ ]. Like formate dehydrogenase and related enzymes, CEOS is comprised of 2 domains connected by a long α-helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. These proteins have a partially conserved NAD-binding motif and active site residues that are characteristic of related enzymes such as saccharopine dehydrogenase. [, , , ]. | Name | N(5)-(carboxyethyl)ornithine synthase |
| Short Name | CEOS | Type | Family |
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