Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking

BMC Structural Biology

Table 1 Docking of 1-phenylethyl butyrate

	Docking into:
	X-ray structures		Substrate-imprinted structures
Structure	(R)-PEB	(S)-PEB	(R)-PEB	(S)-PEB
Candida antarctica lipase B
Experimental data	+	-	+	-
1LBS^a	+	-	+	+
1LBT^a	+	+	+	-
1TCA	+	-	+	-
1TCB	-	-	+	-
1TCC	+	-	+	-
No. false predictions	1	1	0	1
Candida antarctica lipase B, W104A mutant
Experimental data	+	+	+	+
1LBSW104A^a	+	-	+	+
1LBTW104A^a	-	-	+	+
1TCAW104A	+	-	+	+
1TCBW104A	+	-	+	+
1TCCW104A	+	-	+	+
No. false predictions	1	5	0	0

Docking of (R)-PEB and (S)-PEB into five X-ray structures of CALB and five structure models of a W104A mutant of CALB using FlexX. The substrates were docked into the non-optimised X-ray structures and the substrate-imprinted structures. "+" and "-" indicate that the docking results predict (R)-PEB or (S)-PEB to be a substrate or a non-substrate. Correct predictions are indicated by bold and large font type. Experimental data [36] is included for comparison. ^aStructure was resolved with an inhibitor bound.

ISSN: 1472-6807