Table 1 Residues of importance for catalytic activity, structure or correct folding. Residues for which the importance has been previously determined are shown in Fig. 2, giving their numbers, their role and the bibliographic reference of the appropriate mutation study.
From: Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution
Nb. in Fig. 2 | Importance: | Position is homologous to: | Reference: |
|---|---|---|---|
1 | structure | Arg62 (R) in TycB1 | [34] |
2 | folding | Arg67 (R) in TycB1 | [34] |
3 | folding | His146 in TycB1 (1st His of active site His-motif) | [34] |
4 | catalytic activity | His126 (2nd His of the active site His-motif) in VibH | [14,33,34] |
5 | structure | Asp130 (D) in VibH | [14,33,34] |
6 | catalytic activity | Gly131 (G of the active site His-motif) in VibH | [33] |
7 | folding | Trp202 (W) in TycB1 | [34] |
8 | structure | Arg263 (R) in VibH = Arg278 (R) in EntF | [14,33] |
9 | catalytic activity | Trp264 (W) in VibH according to Keating et al., but absent in LCL, DCL and Starter C domains | [14] |
10 | catalytic activity | Asn335 (N) in VibH | [33] |