The current version of GMEnzy contains 186 GMEs. Most of GMEs in GMEnzy are novel sequences. The lengths of the GME sequences range from 35 to 879 amino acids. The majority (98.4%) of the GMEs have calculated pIs that range from 5 to 11, with most of these being basic, rather than acidic.

In GMEnzy the truncation and mutagenesis method accounts for most (80%, 150/184) of the cases. The domain assembly method includes 18% (34/186) of the cases, while the fusion to peptides modification only contains 1% (2/186) of the cases.

Finally, about 27% (50/186) of the entries in the database are GMEs that exhibit ideal or improved properties, such as increased lytic activity or an extended lytic spectrum, after modification. Our data suggest that among these approaches, domain assembly modification exhibits 91% (34/38) positive results, and is the best method for genetic modification (other than the fusion to peptides technique, which has only two cases).

Bacteria are the most commonly used expression host, according the data in our database. Bacteria are hosts in more than 99% of all cases, while only one case used S. cerevisiae.

Additionally, to facilitate rapid purification, most (73%, 136/184) of the GMEs are normally expressed as fusion proteins with either histidine (His) or glutathione-S-transferase (GST) purification tags (Figure 6), as well as data not disclosed. Ion-exchange chromatography and size exclusion chromatography purification techniques represent 19% (35/184) and 1% (2/184) of all GMEs respectively. The traditional ammonium sulfate precipitation method has almost been abandoned, as only one case in our database uses it to purify a GME.