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一种在细菌中合成泛酸的新方法涉及存在于尿嘧啶降解途径中的β-丙氨酸合酶。

A novel way to synthesize pantothenate in bacteria involves β-alanine synthase present in uracil degradation pathway.

机构信息

Programa de Ingeniería Genómica, Centro de Ciencias Genómicas, Universidad Nacional Autonoma de México, Cuernavaca, Morelos, México.

Departamento de Bioquímica, Instituto Nacional de Cardiología "Ignacio Chávez", Tlalpan, México.

出版信息

Microbiologyopen. 2020 Apr;9(4):e1006. doi: 10.1002/mbo3.1006. Epub 2020 Feb 29.

DOI:10.1002/mbo3.1006
PMID:32112625
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7142369/
Abstract

Pantothenate is an indispensable vitamin precursor of the synthesis of coenzyme A (CoA), a key metabolite required in over 100 metabolic reactions. β-Alanine (β-ala) is an indispensable component of pantothenate. Due to the metabolic relevance of this pathway, we assumed that orthologous genes for ß-alanine synthesis would be present in the genomes of bacteria, archaea, and eukaryotes. However, comparative genomic studies revealed that orthologous gene replacement and loss of synteny occur at high frequency in panD genes. We have previously reported the atypical plasmid-encoded location of the pantothenate pathway genes panC and panB (two copies) in R. etli CFN42. This study also revealed the unexpected absence of a panD gene encoding the aspartate decarboxylase enzyme (ADC), required for the synthesis of β-ala. The aim of this study was to identify the source of β-alanine in Rhizobium etli CFN42. In this study, we present a bioinformatic analysis and an experimental validation demonstrating that the source of β-ala in this R. etli comes from β-alanine synthase, the last enzyme of the uracil degradation pathway.

摘要

泛酸是辅酶 A（CoA）合成的必需维生素前体，CoA 是 100 多种代谢反应所需的关键代谢物。β-丙氨酸（β-ala）是泛酸的不可或缺的组成部分。由于该途径的代谢相关性，我们假设细菌、古菌和真核生物的基因组中存在β-丙氨酸合成的同源基因。然而，比较基因组研究表明，panD 基因的同源基因替代和基因同线性丢失发生的频率很高。我们之前曾报道过， pantothenate 途径基因 panC 和 panB（两个拷贝）在 R. etli CFN42 中位于质粒上的非典型位置。这项研究还揭示了编码β-丙氨酸合成所需的天冬氨酸脱羧酶（ADC）的 panD 基因的意外缺失。本研究的目的是确定 Rhizobium etli CFN42 中β-丙氨酸的来源。在这项研究中，我们进行了生物信息学分析和实验验证，证明了 R. etli 中的β-丙氨酸来源是尿嘧啶降解途径的最后一个酶β-丙氨酸合酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/828e/7142369/ae9a72dc277f/MBO3-9-e1006-g011.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/828e/7142369/93a73a3362c6/MBO3-9-e1006-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/828e/7142369/71a9c1bf3e55/MBO3-9-e1006-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/828e/7142369/08a0fa3b9d43/MBO3-9-e1006-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/828e/7142369/853c6d8e648c/MBO3-9-e1006-g009.jpg
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