Coexistence of two D‐lactate‐utilizing systems in Pseudomonas putida KT2440
Coexistence of two D‐lactate‐utilizing systems in Pseudomonas putida KT2440
复制标题
恶臭假单胞菌 KT2440 中两种乳酸利用系统的共存
DOI：
10.1111/1758-2229.12429
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发表时间：
2016
影响因子：
3.3
通讯作者：
Ping Xu
中科院分区：
文献类型：
--
作者：
Yingxin Zhang;Tianyi Jiang;Binbin Sheng;Yangdanyu Long;Chao Gao;Cuiqing Ma;Ping Xu
根际微生物对乳酸等有机酸的利用是有利的，恶臭假单胞菌（PseudomonasputidaKT 2440）是研究最广泛的根际模式生物之一。P。putidaKT 2440基因组含有NAD依赖性乳酸脱氢酶编码基因，但该基因的突变在乳酸利用中不起作用。相反，发现P. putidaKT 2440通过多结构域NAD非依赖性乳酸脱氢酶和乙醇酸氧化酶进行，该酶具有含有几个Fe-S簇结合基序（Fe-Sd-iLDH）和乙醇酸氧化酶的C末端结构域，其广泛分布于各种微生物中。经鉴定，Fe-Sd-iLDH和乙醇酸氧化酶均为膜结合蛋白。Fe-Sd-iLDH和乙醇酸氧化酶都不是组成型表达的，但它们都可以被P中乳酸的任一对映体诱导。putidaKT 2440。这项研究显示了一个案例，其中环境微生物含有两种类型的酶特异性福特-乳酸利用。
It is advantageous for rhizosphere‐dwelling microorganisms to utilize organic acids such as lactate.Pseudomonas putidaKT2440 is one of the most widely studied rhizosphere‐dwelling model organisms. TheP. putidaKT2440 genome contains an NAD‐dependentd‐lactate dehydrogenase encoding gene, but mutation of this gene does not play a role ind‐lactate utilization. Instead, it was found thatd‐lactate utilization inP. putidaKT2440 proceeds via a multidomain NAD‐independentd‐lactate dehydrogenase with a C‐terminal domain containing several Fe‐S cluster‐binding motifs (Fe‐Sd‐iLDH) and glycolate oxidase, which is widely distributed in various microorganisms. Both Fe‐Sd‐iLDH and glycolate oxidase were identified to be membrane‐bound proteins. Neither Fe‐Sd‐iLDH nor glycolate oxidase is constitutively expressed but both of them can be induced by either enantiomer of lactate inP. putidaKT2440. This study shows a case in which an environmental microbe contains two types of enzymes specific ford‐lactate utilization.