1 e relative concentrations of the LFS and the alliinase.

2 equesters all of the sulfenic acid formed by alliinase action on petiveriin, and converts it entirely

3 S-oxide, only in the presence of P. alliacea alliinase and its natural substrate, S-benzyl-l-cysteine

4                                      A novel alliinase (EC 4.4.1.4) was detected and purified from th

5            The results show that the LFS and alliinase function in tandem, with the alliinase furnish

6 S and alliinase function in tandem, with the alliinase furnishing the sulfenic acid substrate on whic

7 ve thiosulfinates that are downstream of the alliinase in a manner dependent upon the relative concen

8 es, the sulfenic acid intermediate formed by alliinase-mediated breakdown of petiveriin.

9                                       At LFS:alliinase of 5:1, LFS sequesters all of the sulfenic aci

10                     However, starting at LFS:alliinase of 5:2, the LFS is unable to sequester all of

11 rvations suggest that manipulation of LFS-to-alliinase ratios in plants displaying this system may pr

12                                          The alliinase reacts with these substrates to produce S-benz

13 oncentration relative to that of P. alliacea alliinase, the LFS sequesters, to varying degrees, the s

14 ter all of the sulfenic acid produced by the alliinase, with the result that sulfenic acid that escap