MetaCyc Enzyme: sulfenic acid dehydrogenase

Synonyms: sulfenate dehydrogenase, lachrymatory-factor synthase

Species: Petiveria alliacea

Subunit composition of sulfenic acid dehydrogenase = [lachrymatory-factor synthase α subunit]2[lachrymatory-factor synthase γ subunit][lachrymatory-factor synthase δ subunit]

The Amazonian medicinal plant Petiveria alliacea contains a unique sulfine lachrymator, (Z)-phenylmethanethial S-oxide, which is produced by a unique lachrymatory-factor synthase. The enzyme acts on phenylmethanesulfenate, which is produced by the (Z)-phenylmethanethial S-oxide alliinase from petiveriin [Musah09].

The lachrymatory-factor synthase was isolated from root tissue of Petiveria alliacea, and chromatographically purified and characterized by SDS-PAGE [Musah09].

Unlike the enzyme from onion, which was reported to contain only one type of subunit (of 19kDa), the enzyme from Petiveria alliacea is a heterotetrameric glycoprotein comprised of two α-subunits (68.8 kD each), one γ-subunit (22.5 kD), and one δ-subunit (11.9 kD). The α subunits are glycosylated and linked together by a disulfide bridge [Musah09]. In addition, while the enzyme from onion is an isomerase that catalyzes the rearrangement of (E) 1-propenylsulfenate to (Z)-propanethial S-oxide, the enzyme from Petiveria alliacea is a dehydrogenase. Enzymatic activity was enhanced in the presence of NAD+ or NADP+, but not in the presnce of FAD of FMN | [He11].

In the absence of the enzyme, phenylmethanesulfenate dimerizes spontaneouly and forms petivericin [Musah09].

Molecular Weight: 172.0 kD (experimental) [Musah09]

pI: 5.2 [Musah09]

Gene-Reaction Schematic

Gene-Reaction Schematic

Created 01-Jul-2010 by Pujar A, Boyce Thompson Institute
Revised 04-Dec-2014 by Caspi R, SRI International

Enzymatic reaction of: phenylmethanesulfenate dehydrogenase (sulfenic acid dehydrogenase)

Inferred from experiment

Synonyms: (Z)-phenylmethanethial S-oxide synthase

EC Number: 1.1.1.M1

phenylmethanesulfenate + NAD(P)+ → (Z)-phenylmethanethial S-oxide + NAD(P)H + H+

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: (Z)-phenylmethanethial S-oxide biosynthesis

Subunit of sulfenic acid dehydrogenase: lachrymatory-factor synthase α subunit

Molecular Weight: 68.8 kD (experimental) [Musah09]

Subunit of sulfenic acid dehydrogenase: lachrymatory-factor synthase γ subunit

Molecular Weight: 22.5 kD (experimental) [Musah09]

Subunit of sulfenic acid dehydrogenase: lachrymatory-factor synthase δ subunit

Molecular Weight: 11.9 kD (experimental) [Musah09]


He11: He Q, Kubec R, Jadhav AP, Musah RA (2011). "First insights into the mode of action of a "lachrymatory factor synthase" - Implications for the mechanism of lachrymator formation in Petiveria alliacea, Allium cepa and Nectaroscordum species." Phytochemistry 72(16);1939-46. PMID: 21840558

Musah09: Musah RA, He Q, Kubec R (2009). "Discovery and characterization of a novel lachrymatory factor synthase in Petiveria alliacea and its influence on alliinase-mediated formation of biologically active organosulfur compounds." Plant Physiol 151(3);1294-303. PMID: 19692535

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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