Optically active amines and amino acids play an important role in the pharmaceutical, agrochemical, and chemical industries. They are frequently used as synthons for the preparation of various pharmaceutically active substances and agrochemicals, but also as resolving agents to obtain chiral carboxylic acids. Consequently, there is a need for efficient methods to obtain the desired enantiomer of a given target structure in optically pure form. Beside a range of chemical methods using for example, asymmetric synthesis with transition metal catalysts, enzymes represent a useful alternative to access this important class of compounds. This review covers biocatalytic approaches using hydrolases (i.e. lipases, amidases), monoamine oxidase and other enzymes. Special focus is given on the application of ω-transaminases with emphasis on concepts to allow efficient asymmetric synthesis starting from prostereogenic ketones.