Sentence examples for block substrate from inspiring English sources

These changes block substrate access to the catalytic pocket and inhibit the enzyme.

Adding back 5 mM glucose after an 18-hour exposure is not sufficient to rescue the cells when the concentration of the inhibitor was high enough to block substrate catabolism.

Different herbicide molecules can block substrate access to the active site of the ALS enzyme [ 25].

Reversible TG2 inhibitors block substrate access to the enzyme active site without covalently modifying the enzyme.

A hexapeptide (Ac-IATAAF-amide) corresponding to the entire recognition motif (P4 P2′) of TatA, the most efficient substrate for any rhomboid protease, did not block substrate proteolysis in vitro even at extreme (1 mM) concentrations.

It appears that the catalytic machinery in these enzymes is preformed, but the N- or C-terminal domain/regions sterically block substrate access, and a movement and/or cleavage in these regions is required for substrate binding.

The crystal structure of falcipain-2 was co-crystallized with inhibitor E64 (N-[N- l-3-trans-carboxyirane-2-carbonyl -l-leucyl]-agmatine), which was covaleN-[N- l-3-trans-carboxyirane-2-carbonyl -l-leucyl]-agmatineiN-[N- l-3-trans-carboxyirane-2-carbonyl -l-leucyl]-agmatine4 residues (Fig. 7).

The 10 ns MD trajectory calculated for G304R HDAC8 reveals that the R304 side chain significantly protrudes into the acetyllysine binding groove of the active site, so the bulky side chain will sterically block substrates or inhibitors from binding.

The 10 ns MD trajectory calculated for Zn2+-bound H180R HDAC8 reveals that the arginine side chain can fluctuate into the acetyllysine binding groove of the active site, so the bulky R180 side chain may sterically block substrates or inhibitors from binding even if a Zn2+ ion is weakly bound in the active site.

Instead of blocking substrate access to a pre-formed active site, the prosegment enforces a conformation in which proplasmepsin cannot form a functional active site.

These interactions also lead to decreased PLA2 activity by partially blocking substrate access to the catalytic dyad and by masking several interfacial binding surface residues important for PLA2 interaction with phospholipids.