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NOS are modular enzymes with both a reductase and oxygenase domain.
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Biosynthesis occurs via large modular enzyme complexes, with each module responsible for the activation and thiolation of each amino acid, followed by peptide bond formation between activated amino acids.
A class of molecules likely involved in symbiotic interactions is produced by non-ribosomal peptide synthetase (NRPS) and polyketide synthetase (PKS) systems: multi-gene, modular enzymes that synthesize small molecules with a variety of biological functions.
The glycoside hydrolases (GHs) are modular enzymes that hydrolyse glycosidic bonds of carbohydrates, with classification based on amino acid sequence and predicted three-dimensional structure.
Comparison with prior NRPS adenylation domain structures provides insights into the assembly line dynamics of these modular enzymes.
They contain dozens of modular enzymes, each of which assembles one component of the polyketide and then passes it on to the next team enzyme.
First, they are modular enzymes that can be reassembled from their component parts.
R domains are frequently present in modular enzymes of fungi, myxobacteria and cyanobacteria (Zhu et al., 2010).
NRPSs and PKSs are multifunctional modular enzymes that assemble small molecules from monomers like pearls on a string.
Cystathionine β-synthase (CBS) is a modular enzyme which catalyzes condensation of serine with homocysteine.
Phylogenomic analysis identified nine major subfamilies of fungal NRPSs which fell into two main groups: one corresponds to NPS genes encoding primarily mono/bi-modular enzymes which grouped with bacterial NRPSs and the other includes genes encoding primarily multimodular and exclusively fungal NRPSs.
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