KEGG ENZYME: 1.1.1.318

ENZYME: 1.1.1.318

Entry

EC 1.1.1.318                Enzyme

Name

eugenol synthase;
LtCES1;
EGS1;
EGS2

Class

Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor

Sysname

eugenol:NADP+ oxidoreductase (coniferyl ester reducing)

Reaction(IUBMB)

eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+ [RN:R09930]

Reaction(KEGG)

R09930 > R10248;
(other) R10249

Substrate

eugenol [CPD:C10453];
carboxylate [CPD:C00060];
NADP+ [CPD:C00006]

Product

coniferyl ester [CPD:C20224];
NADPH [CPD:C00005];
H+ [CPD:C00080]

Comment

The enzyme acts in the opposite direction. The enzymes from the plants Ocimum basilicum (sweet basil) [1,3], Clarkia breweri and Petunia hybrida [4] only accept coniferyl acetate and form eugenol. The enzyme from Pimpinella anisum (anise) forms anol (from 4-coumaryl acetate) in vivo, although the recombinant enzyme can form eugenol from coniferyl acetate [5]. The enzyme from Larrea tridentata (creosote bush) also forms chavicol from a coumaryl ester and can use NADH [2].

History

EC 1.1.1.318 created 2012

Pathway

ec00940

Phenylpropanoid biosynthesis

ec01110

Biosynthesis of secondary metabolites

Orthology

K17055

eugenol synthase

Reference

1 [PMID:16782809]

Authors

Koeduka T, Fridman E, Gang DR, Vassao DG, Jackson BL, Kish CM, Orlova I, Spassova SM, Lewis NG, Noel JP, Baiga TJ, Dudareva N, Pichersky E

Title

Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester.

Journal

Proc Natl Acad Sci U S A 103:10128-33 (2006)
DOI:10.1073/pnas.0603732103

Sequence

[ag:ABD17321]

Reference

2 [PMID:17624297]

Authors

Vassao DG, Kim SJ, Milhollan JK, Eichinger D, Davin LB, Lewis NG

Title

A pinoresinol-lariciresinol reductase homologue from the creosote bush (Larrea tridentata) catalyzes the efficient in vitro conversion of p-coumaryl/coniferyl alcohol esters into the allylphenols chavicol/eugenol, but not the propenylphenols p-anol/isoeugenol.

Journal

Arch Biochem Biophys 465:209-18 (2007)
DOI:10.1016/j.abb.2007.06.002

Reference

3 [PMID:17912370]

Authors

Louie GV, Baiga TJ, Bowman ME, Koeduka T, Taylor JH, Spassova SM, Pichersky E, Noel JP

Title

Structure and reaction mechanism of basil eugenol synthase.

Journal

PLoS One 2:e993 (2007)
DOI:10.1371/journal.pone.0000993

Sequence

[ag:ABD17321]

Reference

4 [PMID:18208524]

Authors

Koeduka T, Louie GV, Orlova I, Kish CM, Ibdah M, Wilkerson CG, Bowman ME, Baiga TJ, Noel JP, Dudareva N, Pichersky E

Title

The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages.

Journal

Plant J 54:362-74 (2008)
DOI:10.1111/j.1365-313X.2008.03412.x

Reference

5 [PMID:18987218]

Authors

Koeduka T, Baiga TJ, Noel JP, Pichersky E

Title

Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain.

Journal

Plant Physiol 149:384-94 (2009)
DOI:10.1104/pp.108.128066

Other DBs

ExplorEnz - The Enzyme Database:

1.1.1.318

IUBMB Enzyme Nomenclature:

1.1.1.318

ExPASy - ENZYME nomenclature database:

1.1.1.318

BRENDA, the Enzyme Database:

1.1.1.318

DBGET integrated database retrieval system