Sentence examples for alignment of catalytic from inspiring English sources

A homology model constructed from the P. falciparum POFUT2 sequence has a very similar predicted structure to H. sapiens and C. elegans POFUT2 (Supplementary Fig. 4A), sufficient to allow the GDP-fucose and TSR domain substrates to be docked into the model to reveal an alignment of catalytic residues and substrates that is reminiscent of a Michaelis complex (Supplementary Fig. 4B, C 26, 27.

Figure 1 shows a consensus phylogram based on the alignment of catalytic core sequences of DUBs, including the majority of known human USP homologs.

* - presence of auxiliary catalytic S_TK_X domain To identify the closest homologues among the potential plant SLK-like kinases, we performed multiple alignments of catalytic domains with that of human SLK and built a phylogenetic tree using the neighbour joining method.

Recent studies have begun to unravel the role of this active center architecture in maintaining the optimal catalytic facility of the enzyme through inducing proper alignment of the catalytic triad.

A dendrogram constructed from the sequence alignment of the catalytic domains was almost identical, which implies that the catalytic and ancillary domains evolved together (data not shown).

Sequence dendograms were calculated based on the multiple alignment of the catalytic domains of DAPk, DRP-1 and ZIPk, and rooted using the catalytic domain of DRAK, using the PHYML v.2.4.4 program [35].

Alignment of HIPKs' catalytic domains with several DYRKs allowed the identification of evolutionarily conserved consensus motives, including the catalytic loop with a Lys residue that contacts the primary phosphate (K221 in HIPK2), experimentally shown to be required for HIPK2 kinase activity [27], and a Tyr residue (Y354 in HIPK2) located in the context of the activation-loop [29,30].

Fig. 6 Sequence alignment of the catalytic domain in BthChi74 with those in other GH18 bacterial chitinases.

Alignment of the catalytic domain of HD-PTP with the other classical PTP sequences highlighted the presence of many divergences in critically conserved residues [1].

Statistical coupling, residue correlation and mutual information analyses along with clustering were applied to analyze the structure-based multiple sequence alignment of the catalytic domains of the Ser/Thr PK family.

The alignment of the catalytic domains among GH26 mannanases is shown in Figure 3(a).