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Mishra et al. [ 1] contributed to the substrate specificity annotations of transporters by developing SVM models that discriminate between amino acid, anion, cation, electron, protein/mRNA, sugar, and other transporters.
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These variables significantly contributing to the substrate degradation have been identified and modeled through contour plots and surfaces in 2 and 3 dimensions (2D, 3D).
Our results suggested that both R3H and RRM domains were essential for the high affinity of long poly(A) substrate, but the R3H domain did not contribute to the substrate recognition of PARN.
This mechanism of reducing the transition-state barrier is likely to also contribute to the substrate specificity observed for transporters (Zhang and Han 2016).
Obviously, these variances contribute to the substrate specificity differences observed.
Some DNAJs bind to substrates themselves, contributing to the substrate folding mechanism of the common HSP70 chaperones.
Such structural differences might contribute to the substrate specificity of RsHTMT.
More detailed mutagenic study will have to be done to fully understand the factors contributing to the substrate specificity.
These variations may contribute to the substrate specificity by subtly altering the geometry of the P+1 pocket.
The CLK family, and related members of the CMGC group, conserve several distinctive residues in the substrate-binding site that contribute to the substrate specificity of CMGC kinases.
The fasciclin domain binds sugar moieties of cell-surface glycoproteins [ 58], the HisI domain binds phosphoribosyl AMP [ 77], and the glutamine synthetase N-terminal domain contributes to the substrate binding pocket of the enzyme [ 59].
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