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

FEBS J. 2022 Oct;289(19):5895-5898. doi: 10.1111/febs.16475. Epub 2022 May 19.

Abstract

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. Comment on: https://doi.org/10.1111/febs.16452.

Keywords: PLP-containing enzymes; d-glutamate; enzyme promiscuity; peptidoglycan.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Isomerases* / genetics
  • Amino Acid Isomerases* / metabolism
  • Amino Acids / metabolism
  • Bacteria / metabolism
  • D-Aspartic Acid
  • Glutamic Acid / metabolism
  • Peptidoglycan / metabolism
  • Racemases and Epimerases
  • Transaminases / genetics

Substances

  • Amino Acids
  • Peptidoglycan
  • Glutamic Acid
  • D-Aspartic Acid
  • Transaminases
  • Racemases and Epimerases
  • Amino Acid Isomerases