I am a systems biologist trying to study cellular cross talk. Some computational papers have mentioned about the effect of enzyme substrate complex on the cellular cross talk. So, my question is can there be a situation inside a cell where enzyme and substrate react to forms a complex and accumulates rather than dissociating to form the product.
Yes there are some synthetic substrates to bind some aminoacids in the active center of enzymes irreversibly, which can be then detected, without given products. If you write in internet the synthetic substrates for example binding to serin, systein, hystidine you get several names. If the active center of enzyme is known then your job is easier. You have to get the syn. substrates into cell.
I believe there are many instances where this can happen. For example, if an enzyme and substrate interact yet the cofactor or post-translational modification (ion, protein, phosphorylation, etc) required for processing is not present, the complex may be present but the substrate will not be cleaved. Moreover, if an inhibitor is present (and part of the protease/substrate complex), it may allow protease/substrate complex formation, yet the substrate may not be cleaved. Finally, if the protease is not enzymatically active (due to the proform not being cleaved) but able to form a complex with its substrate, the same complex can form but without substrate cleavage. One more, if the protease and substrate form a complex but the environmental conditions e.g. pH, etc are not conducive to efficient substrate cleavage, the situation you ask about can also arise.
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