Fig. 2.
Pairwise alignment of CH3H and F3′H amino acid sequences from C. sulphureus (Accession nos FJ216429 and FJ216426). Alignment was performed with ClustalW (Thompson et al., 1994, 2002). Grey-shaded boxes highlight substrate recognition site 1 (SRS1: Gotoh, 1992) and conserved P450 patterns. I, Hydrophobic membrane anchor; II, proline-rich hinge [PI]-P-G-P-X-[GP]-P (Kemper, 2004); III, oxygen-binding motif [AG]-G-X-[ED]-T-[TS]; IV, EXXR triad (Ravichandran et al., 1993); V, the P450-pattern [FW]-[SNGH]-X-[GD]-{F}-[RKHPT]-{P}-C-[LIVMFAP]-[GAD] (Prosite pattern PS00086; Hulo et al., 2006).

Pairwise alignment of CH3H and F3′H amino acid sequences from C. sulphureus (Accession nos FJ216429 and FJ216426). Alignment was performed with ClustalW (Thompson et al., 1994, 2002). Grey-shaded boxes highlight substrate recognition site 1 (SRS1: Gotoh, 1992) and conserved P450 patterns. I, Hydrophobic membrane anchor; II, proline-rich hinge [PI]-P-G-P-X-[GP]-P (Kemper, 2004); III, oxygen-binding motif [AG]-G-X-[ED]-T-[TS]; IV, EXXR triad (Ravichandran et al., 1993); V, the P450-pattern [FW]-[SNGH]-X-[GD]-{F}-[RKHPT]-{P}-C-[LIVMFAP]-[GAD] (Prosite pattern PS00086; Hulo et al., 2006).

Close
This Feature Is Available To Subscribers Only

Sign In or Create an Account

Close

This PDF is available to Subscribers Only

View Article Abstract & Purchase Options

For full access to this pdf, sign in to an existing account, or purchase an annual subscription.

Close