Meta-cleavage product hydrolases (MCP-hydrolase) are key enzymes involved in the microbial degradation of aromatic compounds. MCP-hydrolase CumD is a dimeric enzyme produced by Pseudomonas fluorescens IP01 and is involved in the pathway for the degradation of cumene. MCP-hydrolase enzymes produce 2-hydroxypenta-2,4-dienoate and various organic acids, depending upon the C6 substituent of the substrate. CumD prefers larger C6 substituents compared to other monoalkylbenzene hydrolases, such as TodF. Hence, when CumD acts on the meta-cleavage product of cumene, 2-hydroxypenta-2,4-dienoate and isobutyric acid are the products. The understanding of the catalytic mechanism of MCP-hydrolases is neccessary to improve biological degradation of environmental pollutant aromatic compounds, which may be carcinogenic, toxic and mutagenic.
Defined by 5 residues: SER:A-34ALA:A-103PHE:A-104ASP:A-224HIS:A-252