The plant Diaminopelargonic acid aminotransferase uses spermidine as its amino donor.

Biotin is an essential vitamin that is only synthesised in microorganisms, plants and fungi, so the biosynthetic pathway is of interest for antibacterial and herbicide discovery. Plants contain a single, bifunctional enzyme that catalyses two sequential steps in biotin biosynthesis, dethiobiotin synthetase-diaminopelargonic acid aminotransferase (herein referred to as BioDA). Diaminopelargonic acid aminotransferase (BioA) catalyses the pyridoxal phosphate-dependent transamination of 7-keto-8-aminopelargonic acid to produce 7,8-diaminopelargonic acid, while dethiobiotin synthetase (BioD) catalyses the subsequent step to produce dethiobiotin.

D-glufosinate as a male sterility agent for hybrid seed production.

A chemical male sterility system based on anther-localized conversion of the inactive D-enantiomer of the herbicide, glufosinate (2-amino-4-(methylphosphinyl)-butanoate) to the phytotoxic L is described. Highly pure D-glufosinate was isolated in >98% enantiomeric excess from the racemate via fermentation with a strain of Escherichia coli expressing the PAT (L-glufosinate N-acetyl transferase) gene and purification of the unreacted D-enantiomer from the broth by ion exchange. A modified (F58K, M213S) form of the D-amino acid oxidase (DAAO) (EC 1.