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Literature summary extracted from

  • Mannesse, M.L.M.; Cox, R.C.; Koops, B.C.; Verheij, H.M.; de Haas, G.H.; Egmond, M.R.; van der Hijden, H.T.W.M.; de Vlieg, J.
    Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity (1995), Biochemistry, 34, 6400-6407.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.74 A85F optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains Fusarium solani
3.1.1.74 A85F/G82A optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains Fusarium solani
3.1.1.74 A85W optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains Fusarium solani
3.1.1.74 G82A mutation has no influence on enzymatic properties Fusarium solani
3.1.1.74 S54W mutation has no influence on enzymatic Fusarium solani

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.74 Fusarium solani
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 pisi
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.74 cutin + H2O
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 Fusarium solani additional information
-
 ?
3.1.1.74 triglyceride + H2O triglycerides in which one of the primary acyl ester functions has been replaced by an alkyl grpup and the secondary acyl ester bond has been replaced by an acyl amino bond. The activity is very sensitive to the length and distribution of the acyl chains, the highest activity is found when the chains at position 1 and 3 contain three or four carbon atoms Fusarium solani ?
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 ?