In this review we describe inhibition of chitinases from bacteria, fungi, plants and animals by allosamidin and its derivatives, cyclic peptides, styloguanidin and divalent cations. Most information is available for allosamidin, whose important structural features necessary for inhibition are known. At least one N-acetylallosamine sugar must be present, and the spatial arrangement of the allosamizoline moiety are important for inhibition. Less complex compounds are therefore possible as lead structures for the development of agents interfering with chitinase. There is a pronounced species specificity in chitinase inhibition by allosamidin: half-maximal values are often in the range of 0.1-1 microM (e.g. in all arthropods), being lower in nematodes (0.048, 0.0002 microM, respectively) and amoeba (0.002-0.01 microM) and quite divergent in fungi (0.01-70 microM). These differences cannot be caused by the catalytic centers of family 18 and 19 chitinases.