Modified acyl-ACP desaturase

Chemistry: molecular biology and microbiology – Plant cell or cell line – per se ; composition thereof;... – Plant cell or cell line – per se – contains exogenous or...

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4351723, 435189, 4352401, 4352402, 4352404, 435243, 4352523, 43525411, 4352551, 4353201, 536 232, C12N 1500, C12N 902, C12N 500, C12N 100

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057053910

ABSTRACT:
Disclosed is a methods for modifying the chain length and double bond positional specificities of a soluble plant fatty acid desaturase. More specifically, the method involves modifying amino acid contact residues in the substrate binding channel of the soluble fatty acid desaturase which contact the fatty acid. Specifically disclosed is the modification of an acyl-ACP desaturase. Amino acid contact residues which lie within the substrate binding channel are identified, and subsequently replaced with different residues to effect the modification of activity.

REFERENCES:
patent: 5443974 (1995-08-01), Hitz et al.
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Fox, B.G., et al., Stearoyl-acyl carrier protein .DELTA.9 desaturase from Ricinus communis is a diiron-oxo protein, Proc. Natl. Acad. Sci. USA 90: 2486-2490 (1993).
Nordlund, P. and Eklund, H. Di-iron-carboxylate proteins. Curr. Opin. Struct. Biol. 5: 758-766 (1995).
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Rosenzweig, A.C., et al., Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature 366: 537-540 (1993).
Shanklin, J., et al., Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase. Biochemistry 33: 12787-12794 (1994).

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