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. 2004 Mar;134(3):1123–1134. doi: 10.1104/pp.103.032706

Figure 4.

Figure 4.

Alignment of the PsKO1 putative protein with the ent-kaurene oxidases of pumpkin (CmKO1; Helliwell et al., 2000), Arabidopsis (AtKO1; Helliwell et al., 1998), and a fragment from tobacco (Nicotiana tabacum; NtKO1; Fukazawa et al., 2000) using GeneDoc conserved base presentation after ClustalW multisequence alignment. The sites of genetic lesions of the pea lh-1, lh-2, and lh-3 mutants and the Arabidopsis ga3-1 and ga3-2 in-frame stop codons are indicated. The catalytic domains A to D (Kalb and Loper, 1988) are labeled, and cytochrome P450 highly conserved amino acids of known significance are underlined. The catalytic A domain is associated with substrate binding (Poulos et al., 1985) and oxygen pocket (Atkins and Sligar, 1988; Imai et al., 1989) and traverses the distal surface of the haem (Poulos et al., 1985). The B domain contains the EXXR section of the highly conserved E,R,R triad involved in positioning the haem-binding pocket (Hasemann et al., 1995). The C domain has the PERF clan designator region (Paquette et al., 2000) that includes the third R of the E,R,R triad (Werck-Reichhart et al., 2002). The D domain has the haem-binding region associated with all cytochrome P450s with the Cys that provides the axial thiolate ligand to the haem iron (Poulos et al., 1986; Porter and Coon, 1991).