The next number is the sub-subclass of 24, which consists of metalloendopeptidases which contain metal ions in their active sites, in this case zinc, which help in cleaving peptide bonds.
[3] Additionally, gelatinases A (MMP2) and B (MMP9) have been proven to assist in developing new blood vessels in corneas of rats and rabbits when experiencing corneal damage.
The catalysis, associated with a zinc ion and amino acid residues, breaks the peptide bonds into polypeptides through cleavage.
Additional proteins, such as TIMP-2 and other TIMPs, work as inhibitors to regulate and control the enzymatic pathway by binding to the gelatinase active site, which prevents the breakdown of substrate.
Enzyme binding to the surface brings it in close accord with certain substrates in the pericellular space in order to regulate function of the MMPs.
[7] Gelatinases contain a catalytic domain (located in the C-terminal region), which is essential for enzymatic activity and hydrolysis of peptide bonds in substrate molecules.
These histidines are in relation to a catalytic zinc ion, playing an important role in catalyzing the hydrolysis of peptide bonds in proteins.Also in the C terminal region, there is a hemopexin-like domain, which interacts with a part of the cell membrane.
This active site aids the hydrolysis of peptide bonds in substrates, such as gelatin and collagen, due to coordination of zinc ions and amino acid residues.