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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid.

A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 50 kDa. The substrate specificity of macluralisin towards synthetic peptides and insulin B-chain is similar to that of cucumisin, a subtilisin-like proteinase from melon fruit. The enzyme is completely inhibited by diisopropylfluorophosphate. Its amino-acid composition resembles that of a serine proteinase isolated from the Cucurbitaceae. The N-terminal sequence has 33% of its residues identical to those of the sequence of fungal subtilisin-like proteinase K. Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom.[1]

References

  1. Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid. Rudenskaya, G.N., Bogdanova, E.A., Revina, L.P., Golovkin, B.N., Stepanov, V.M. Planta (1995) [Pubmed]
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