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Fig. 2 | Biotechnology for Biofuels and Bioproducts

Fig. 2

From: Functional analysis of the dehydratase domains of the PUFA synthase from Emiliania huxleyi in Escherichia coli and Arabidopsis thaliana

Fig. 2

Sequence and 3D structural analysis of two FabA-like dehydratase (DH) domains from Emiliania huxleyi (Eh). a Multiple sequence alignment of the DH domains of PUFA synthases and FabA from Escherichia coli (Ec). b 3D structures of EhDH1-DH2 domains. c Two types of predicted active-site residues on EhDH1-DH2 domains. The putative active sites are highlighted by a red rectangle, and the consensus amino acids are shaded. EcFabA, FabA from E.coli; EhPUFA-DH1, DH1 domain of polyunsaturated fatty acid (PUFA) synthase from Emiliania huxleyi; EhPUFA-DH2, DH2 domain of PUFA synthase from Emiliania huxleyi; SchPUFA-DH1, DH1 domain of PUFA synthase from Schizochytrium; SchPUFA-DH2, DH2 domain of PUFA synthase from Schizochytrium; ShePUFA-DH1, DH1 domain of PUFA synthase from Shewanella; ShePUFA-DH2, DH2 domain of PUFA synthase from Shewanella; TcPUFA-DH1, DH1 domain of PUFA synthase from Thraustochytrium; TcPUFA-DH2, DH2 domain of PUFA synthase from Thraustochytrium

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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