Functional and Phylogenetic Divergence of Fungal Adenylate-Forming Reductases
Functional and Phylogenetic Divergence of Fungal Adenylate-Forming Reductases
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DOI：
10.1128/aem.01767-14
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发表时间：
2014-10-01
影响因子：
4.4
通讯作者：
Hoffmeister, Dirk
中科院分区：
文献类型：
--
作者：
Kalb, Daniel;Lackner, Gerald;Hoffmeister, Dirk
真菌l -赖氨酸生物合成的关键步骤是由形成腺苷酸的l - α -氨基己二酸还原酶催化，这些酶在腺苷化，硫代化和还原步骤中组织。然而，许多子囊菌和担子菌的基因组包含了大量的额外基因，这些基因编码相似但功能不同的酶。在这里，我们描述了在大肠杆菌中异种产生的四种还原酶的体外功能表征。Ceriporiopsis subvermispora丝氨酸还原酶Nps1具有末端铁氧化还原蛋白- nadp（+）还原酶（FNR）结构域，因此属于迄今未描述的一类真菌多结构域酶。第二类以典型的末端短链脱氢酶/还原酶结构域为特征，以Ceriporiopsis subvermispora Nps3为代表，是第一个生物化学特征的担子菌来源的l - α -氨基己二酸还原酶。黄曲霉l -酪氨酸还原酶LnaA和LnbA是一个不同的系统发育分支的成员。系统发育分析支持真菌腺苷酸形成还原酶比以前认识到的更多样化，属于四个不同的类别。
A key step in fungal L-lysine biosynthesis is catalyzed by adenylate-forming L-alpha-aminoadipic acid reductases, organized in domains for adenylation, thiolation, and the reduction step. However, the genomes of numerous ascomycetes and basidiomycetes contain an unexpectedly large number of additional genes encoding similar but functionally distinct enzymes. Here, we describe the functional in vitro characterization of four reductases which were heterologously produced in Escherichia coli. The Ceriporiopsis subvermispora serine reductase Nps1 features a terminal ferredoxin-NADP(+) reductase (FNR) domain and thus belongs to a hitherto undescribed class of fungal multidomain enzymes. The second major class is characterized by the canonical terminal short-chain dehydrogenase/reductase domain and represented by Ceriporiopsis subvermispora Nps3 as the first biochemically characterized L-alpha-aminoadipic acid reductase of basidiomycete origin. Aspergillus flavus L-tyrosine reductases LnaA and LnbA are members of a distinct phylogenetic clade. Phylogenetic analysis supports the view that fungal adenylate-forming reductases are more diverse than previously recognized and belong to four distinct classes.