Abstract:

Aspartate kinase (aspartokinase, AK) is a rate-limiting enzyme controlling the carbon and nitrogen flux into
the biosynthesis pathways of amino acids of the aspartic acid family in microorganisms. It is a key enzyme to determine
the ability to obtain aromatic aspartic amino acids. This article describes recent progress in understanding the importance
of aspartatekinase, the general structure of aspartatekinases from different species, features of their binding sites and their
regulatory mechanisms. Moreover, future research trends in this area are foreseen. The aim of this review is to provide
further understanding of the mechanism of metabolic regulation of aspartatekinase and accordingly promote the industrial
development of aspartic acid family amino acids.

Key words: aspartatekinase, biosynthetic pathway, binding sites, regulatory mechanisms