A comparative genomics study of genetic products potentially encoding ladderane lipid biosynthesis

Biology Direct

Table 2 Deviations in enzyme active sites in fabB and fabF paralogues in K. stuttgartiensis, R. baltica, G. sulfurreducens in comparison to 'typical' fabB/F sequences in e.g. Kustd1386 (CAJ72131) or the structurally determined EcfabB (YP_540234).

Gene sequence	Active site amino acids from *fabB/F*sequence
Typical fabB/F sequence and function	Active site	Decarb-oxylation	Unknown	Unknown	Electronic charge on histidine ring	Decarb-oxylation	Electronic charge on histidine ring	Guides acyl chain entry into binding pocket
	Cys163s	His298*	Thr300	Thr302	Lys328*	His333*	Glu342‡	Phe392a
Kuste3606 CAJ74369	Val163	Asn298‡	Tyr300a	Gly302	Lys328*	Glu333‡	Gln342‡	Arg392*
Kuste2805 CAJ73556	Phe163a	Asn298‡	Asn300‡	Cys302s	Lys328*	Glu333‡	Gln342‡	Phe392a
Kuste3348 CAJ4109	Ser163	Ser298	Pro300i	Phe302a	Asp328‡	Asn333‡	Asn342‡	Ser392
R. baltica NP 865682	Asp163‡	His298*	Met300s	Asp302‡	Ile328	His333*	Gly342	Ser392
R. baltica NP 866153	Glu163‡	His298*	Leu300	Asp302‡	Lys328*	Asn333‡	Glu342‡	Pro392i
G. sulfurreducens NP 951518	Phe163a	Pro298i	Ala300	Ala302	Gly328	Arg333*	Ala342	-

Functional role of amino acids taken from White et al. [21]. Key; Italics = hydrophilic (polar amino acids), Bold = hydrophobic (non-polar amino acids), (*) = Basic, (‡) = Acidic or amide, (s) = Sulphur containing, (a) = Aromatic, (i) = Imino acid.

ISSN: 1745-6150