Sentence examples for expanding substrate specificity from inspiring English sources

These results demonstrate that positions 111 and 166 are not involved in expanding substrate specificity, consistent with their location more distal to the macrolide-binding site.

In particular, we discuss tailoring the lignin substrate for microbial utilization, host selection for biological funneling, ligninolytic enzyme microbe synergy, metabolic engineering, expanding substrate specificity for biological funneling, and process integration, each of which presents key challenges.

These include altering the reaction mechanism of the enzyme to catalyse new reactions, switching substrate specificity, expanding substrate specificity, and improving substrate specificity, such as enantioselectivity in kinetic resolutions.

This may be exploited in order to improve catalysis and to expand substrate specificity and thus significantly advance enzymatic plastic polymer degradation.

Here, we identify the molecular basis for expanded substrate specificity in MphI, a macrolide kinase (Mph) that does not confer resistance to erythromycin, in contrast to other known Mphs.

Mutation of a gatekeeper residue, tryptophan 37, in E. coli lipoic acid ligase (LplA), expands substrate specificity such that unnatural probes much larger than lipoic acid can be recognized.

Knowledge of the enzyme active-site environment has been the basis for exploration of catalysis of non-natural substrates and of mutagenesis of the phosphate-binding site to expand substrate specificity.

Heterologous expression of a PNO of the generalist arctiid Grammia geneura produced an N-oxygenizing enzyme that shows noticeably expanded substrate specificity compared with the related enzyme of the specialist Tyria jacobaeae.

While recombinant DNA technology has produced many examples where natural proteins have been engineered with properties that are desirable for biotechnology, such as improved stability or expanded substrate specificity, these structures all derive from sequences whose ancestors can be traced back to nature[19], [20], [21].

Moreover, as the electron donor of HoxEFUYH is NADH, the expressed HoxEFUYH expanded the substrate specificity of the hydrogen-evolving hydrogenase in E. coli.

Phosphorylation of Thr-177 expands the substrate specificity of CaM KI and is not merely an "on-off" switch for kinase activity.