Fig 1.
Comparison of the nonribosomal codes of CcbC and LmbC substrate binding pockets (SBPs).
A) Structures of lincomycin and celesticetin. Amino acid precursors activated by adenylation domains (A-domains) are indicated in green. B) Pattern of eight variable amino acid residues of CcbC and LmbC nonribosomal codes. The highly conserved D and K residues at the boundaries of the nonribosomal codes are omitted. Amino acid residues are numbered according to CcbC (first row) and LmbC (last row). The consensus code of the stand-alone L-proline-specific A-domains is shown in the middle row [3]. The residues in LmbC and CcbC SBPs, which correspond to the consensus, are underlined. Colours correspond to the individual amino acid residues in the model of CcbC/LmbC SBPs (C). C) Homology models of the CcbC SBP with L-proline and the LmbC SBP with PPL [3].
Table 1.
Kinetic parameters of LmbC and LmbC single mutants for PPL and L-proline substrates.
Table 2.
Km values of CcbC, CcbC mutants and LmbC in reaction with various substrates.
Table 3.
Kinetic parameters of LmbC, CcbC and selected CcbC mutants for various substrates.