TY  - JOUR
A1  - Keller, Sebastian
A1  - Wetterhorn, Karl M.
A1  - Vecellio, Alison
A1  - Seeger, Mark
A1  - Rayment, Ivan
A1  - Schubert, Torsten
T1  - Structural and functional analysis of an l-serine O-phosphate decarboxylase involved in norcobamide biosynthesis
JF  - FEBS letters : the journal for rapid publication of short reports in molecular biosciences
N2  - 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.
KW  - cobamides
KW  - ethanolamine phosphate
KW  - norcobamide biosynthesis
KW  - serine phosphate decarboxylase
Y1  - 2019
U6  - https://doi.org/10.1002/1873-3468.13543
SN  - 0014-5793
SN  - 1873-3468
VL  - 593
IS  - 21
SP  - 3040
EP  - 3053
PB  - Wiley
CY  - Hoboken
ER  -