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Article

Lysine ε-aminotransferases: kinetic constants, substrate specificities, and the variation in active site residues.

Enzyme and microbial technology - 1 Mar 2016

Seo Joo-Hyun, Kim Eun-Mi, Chae Ahram, Kim Byung-Gee

Abstract excerpt

L-Lysine ε-aminotransferase (lysAT) is an important enzyme in tailoring the terminal amino group of L-lysine or L-ornithine and can be directed to the synthesis of various value-added chemicals such as adipic acid. Three lysATs, lysAT from Saccharopolyspora erythraea NRRL 2338 (lysAT_Sery), lysAT from Nocardia farcinica IFM 10152, and lysAT from Rhodococcus jostii RHA1, were cloned, and their kinetic values and...

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PMID: 26827769
DOI: 10.1016/j.enzmictec.2015.12.001

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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