The conundrum in enzymatic reactions related to biosynthesis of D-amino acids in bacteria

被引：4

作者：

Pollegioni, Loredano ^{[1
]}

Molla, Gianluca ^{[1
]}

机构：

[1] Univ Insubria, Dipartimento Biotecnol & Sci Vita, Prot Factory 2 0, Varese, Italy

来源：

FEBS JOURNAL | 2022年 / 289卷 / 19期

关键词：

D-glutamate; enzyme promiscuity; peptidoglycan; PLP-containing enzymes; CELL-WALL; ELUCIDATION;

D O I：

10.1111/febs.16475

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

D-Amino acids (D-AAs) are key components of the peptidoglycan matrix in bacterial cells. Various bacterial species are known to produce D-AAs by using different enzymes, such as highly specific and broad-spectrum racemases. Miyamoto et al. studied the biosynthesis of D-glutamate in the hyperthermophile and anaerobic Gram-negative bacterium, Thermotoga maritima, which does not possess a broad-spectrum racemase. The investigated TM0831 enzyme catalyzes both a D-amino acid aminotransferase reaction producing D-glutamate and an amino acid racemase activity aimed at generating D-aspartate and D-glutamate from the corresponding L-enantiomers. TM0831 represents an example of natural molecular evolution process favoring the enzyme versatility.

引用

页码：5895 / 5898

页数：4

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