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Publication Abstract from PubMed

Structural diversity of natural cobamides (Cbas, B12 vitamers) is limited to the nucleotide loop. The loop is connected to the cobalt-containing corrin ring via an (R)-1-aminopropan-2-ol O-2-phosphate (AP-P) linker moiety. AP-P is produced by the L-threonine O-3-phosphate (L-Thr-P) decarboxylase CobD. Here, the CobD homolog SMUL_1544 of the organohalide-respiring epsilonproteobacterium Sulfurospirillum multivorans was characterized as a decarboxylase that produces ethanolamine O-phosphate (EA-P) from L-serine O-phosphate (L-Ser-P). EA-P is assumed to serve as precursor of the linker moiety of norcobamides that function as cofactors in the respiratory reductive dehalogenase. SMUL_1544 (SmCobD) is a pyridoxal-5'-phosphate (PLP)-containing enzyme. The structural analysis of the SmCobD apoprotein combined with the characterization of truncated mutant proteins uncovered a role of the SmCobD N-terminus in efficient L-Ser-P conversion. This article is protected by copyright. All rights reserved.

Structural and functional analysis of an L-serine O-phosphate decarboxylase involved in norcobamide biosynthesis.,Keller S, Wetterhorn KM, Vecellio A, Seeger M, Rayment I, Schubert T FEBS Lett. 2019 Jul 19. doi: 10.1002/1873-3468.13543. PMID:31325159^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.