Studies of a novel cysteine sulfoxide lyase from Petiveria alliacea: the first heteromeric alliinase.

Abstract:

:A novel alliinase (EC 4.4.1.4) was detected and purified from the roots of the Amazonian medicinal plant Petiveria alliacea. The isolated enzyme is a heteropentameric glycoprotein composed of two alpha-subunits (68.1 kD each), one beta-subunit (56.0 kD), one gamma-subunit (24.8 kD), and one delta-subunit (13.9 kD). The two alpha-subunits are connected by a disulfide bridge, and both alpha- and beta-subunits are glycosylated. The enzyme has an isoelectric point of 4.78 and pH and temperature optima of 8.0 and approximately 52 degrees C, respectively. Its activation energy with its natural substrate S-benzyl-l-cysteine sulfoxide is 64.6 kJ mol(-1). Kinetic studies showed that both K(m) and V(max) vary as a function of substrate structure, with the most preferred substrates being the naturally occurring P. alliacea compounds S-benzyl-l-cysteine sulfoxide and S-2-hydroxyethyl-l-cysteine sulfoxide. The alliinase reacts with these substrates to produce S-benzyl phenylmethanethiosulfinate and S-(2-hydroxyethyl) 2-hydroxyethanethiosulfinate, respectively.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Musah RA,He Q,Kubec R,Jadhav A

doi

10.1104/pp.109.142430

subject

Has Abstract

pub_date

2009-11-01 00:00:00

pages

1304-16

issue

3

eissn

0032-0889

issn

1532-2548

pii

pp.109.142430

journal_volume

151

pub_type

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