@article{KellerWetterhornVecellioetal.2019,
  author    = {Keller, Sebastian and Wetterhorn, Karl M. and Vecellio, Alison and Seeger, Mark and Rayment, Ivan and Schubert, Torsten},
  title     = {Structural and functional analysis of an l-serine O-phosphate decarboxylase involved in norcobamide biosynthesis},
  series = {FEBS letters : the journal for rapid publication of short reports in molecular biosciences},
  volume    = {593},
  journal   = {FEBS letters : the journal for rapid publication of short reports in molecular biosciences},
  number    = {21},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {0014-5793},
  doi       = {10.1002/1873-3468.13543},
  pages     = {3040 -- 3053},
  year      = {2019},
  abstract  = {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.},
  language  = {en}
}