结构与功能分析一种 l-丝氨酸 O-磷酸脱羧酶在 norcobamide 生物合成中的作用。
Structural and functional analysis of an l-serine O-phosphate decarboxylase involved in norcobamide biosynthesis.
机构信息
Department of Microbial Interactions, Institute of Microbiology, Friedrich Schiller University, Jena, Germany.
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, WI, USA.
出版信息
FEBS Lett. 2019 Nov;593(21):3040-3053. doi: 10.1002/1873-3468.13543. Epub 2019 Jul 30.
Structural diversity of natural cobamides (Cbas, B 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.
天然钴胺素（Cbas，维生素 B 族）的结构多样性仅限于核苷酸环。该环通过（R）-1-氨基-2-丙醇 O-2-磷酸（AP-P）连接部分与含钴的咕啉环相连。AP-P 是由 l-苏氨酸 O-3-磷酸（l-Thr-P）脱羧酶 CobD 产生的。在这里，有机卤化物呼吸型 ε-变形菌 Sulfurospirillum multivorans 的 CobD 同源物 SMUL_1544 被鉴定为一种脱羧酶，它可将 l-丝氨酸 O-磷酸（l-Ser-P）转化为乙醇胺 O-磷酸（EA-P）。EA-P 被认为是 norcobamides 连接部分的前体，norcobamides 在呼吸还原脱卤酶中作为辅因子发挥作用。SMUL_1544（SmCobD）是一种含有吡哆醛-5'-磷酸（PLP）的酶。SmCobD 脱辅基蛋白的结构分析结合截短突变蛋白的特性，揭示了 SmCobD N 端在有效 l-Ser-P 转化中的作用。
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