Sentence examples for binding of the aldehyde from inspiring English sources

As previously shown [ 29], substrate inhibition arises from the non-productive binding of the aldehyde to the enzyme-NADH complex.

The carboxylic acid side chain occupies a hydrophobic channel leading from the metal center and likely closely mimics the binding of the aldehyde substrate.

The fatty acid presumably mimics the binding of the aldehyde substrate; however, it is unclear how the substrate gains access to the active site because the hydrophobic channel is completely enclosed by the protein.

Assuming that Km values are an indication of affinity, the size of the residue at position 441 also appears to affect the binding of the nucleotide, although to a much lesser extent than the binding of the aldehyde, for as yet not clear reasons.

It has to be noted that the BADH activity of the enzymes in the first group is achieved not only by their much smaller Km BAL) values, which most likely reflect a much better binding of the aldehyde, but also, although not so importantly, by their significantly higher kcat BAL) values when compared with the enzymes of the second group.

The ThDP-catalyzed carboligation of aldehydes involves a multistep mechanism, which starts with the binding of the donor aldehyde to the ThDP-ylide resulting in an umpolung of the carbonyl reactivity yielding a so-called "activated aldehyde" (for details see the Supporting Information, Figure S1).

Previously solved crystal structures of cADO all feature a long-chain fatty acid bound that was presumed to occupy the binding site of the aldehyde substrate.

Bivalent binding of the corresponding linker ("aldehyde-PEG-NHS") to adjacent NH2 groups on the tip was largely suppressed by high linker concentrations.

Although spectroscopic studies of the formation of the differic-peroxide intermediate(s) appear to be complicated by multiple reactant states arising from the order of binding of aldehyde and O2, the rate constants for the formation of the activated oxygen species (II or III in Figure 1) have been measured as 0.75 and 0.2 s–1 depending on which substrate binds first.

The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.

After the printing process, all slides were incubated overnight at 4°C to allow maximum binding of antibody to the aldehyde slide surface.