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Structural and functional analysis of an l ‐serine O‐ phosphate decarboxylase involved in norcobamide biosynthesis
Author(s) -
Keller Sebastian,
Wetterhorn Karl M.,
Vecellio Alison,
Seeger Mark,
Rayment Ivan,
Schubert Torsten
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13543
Subject(s) - cofactor , biosynthesis , serine , chemistry , moiety , stereochemistry , biochemistry , pyridoxal phosphate , phosphate , linker , pyridoxal , lyase , enzyme , computer science , operating system
Structural diversity of natural cobamides (Cbas, B 12 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 ( Sm CobD) is a pyridoxal‐5′‐phosphate (PLP)‐containing enzyme. The structural analysis of the Sm CobD apoprotein combined with the characterization of truncated mutant proteins uncovered a role of the Sm CobD N‐terminus in efficient l ‐Ser‐P conversion.