KEGG ENZYME: 4.2.1.139

ENZYME: 4.2.1.139

Entry

EC 4.2.1.139                Enzyme

Name

pterocarpan synthase;
medicarpin synthase;
medicarpan synthase;
7,2'-dihydroxy-4'-methoxyisoflavanol dehydratase;
2',7-dihydroxy-4'-methoxyisoflavanol dehydratase;
DMI dehydratase;
DMID;
2'-hydroxyisoflavanol 4,2'-dehydratase;
PTS (gene name);
4'-methoxyisoflavan-2',4,7-triol hydro-lyase [(-)-medicarpin-forming]

Class

Lyases;
Carbon-oxygen lyases;
Hydro-lyases

Sysname

(4R)-4,2'-dihydroxyisoflavan hydro-lyase (pterocarpan-forming)

Reaction(IUBMB)

a (4R)-4,2'-dihydroxyisoflavan = a pterocarpan + H2O [RN:R12307]

Reaction(KEGG)

R12307 > R07738

Substrate

(4R)-4,2'-dihydroxyisoflavan [CPD:C21738]

Product

pterocarpan [CPD:C22071];
H2O [CPD:C00001]

Comment

The enzyme catalyses the formation of the additional ring in pterocarpan, the basic structure of phytoalexins produced by leguminous plants, including (-)-medicarpin, (+)-medicarpin, (-)-maackiain and (+)-maackiain. The enzyme requires that the hydroxyl group at C-4 of the substrate is in the (4R) configuration. The configuration of the hydrogen atom at C-3 determines whether the pterocarpan is the (+)- or (-)-enantiomer. The enzyme contains amino acid motifs characteristic of dirigent proteins.

History

EC 4.2.1.139 created 2013, modified 2019

Pathway

ec00943

Isoflavonoid biosynthesis

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

Orthology

K25075

pterocarpan synthase

Genes

GMX:	100500621(PTS1) 100817155(PTS3) 100817686(PTS4)

GSJ:	114399619 114399676 114406806 114406807

PVU:	PHAVU_001G145600g

VRA:	106757395 106757413 106757427

VAR:	108328428 108328436

VUN:	114178337 114193911

VUM:	124823009 124844910 124844911 124844912

CCAJ:

109797846

APRC:

113863229

MTR:	11418495 11421669 11424576

TPRA:

123892723

CAM:

101491323

PSAT:

127126201

VVO:

131612504

LJA:

130742227

ADU:

107492865

AIP:

107645384

AHF:	112696146 112758883

» show all

Reference

1 [PMID:7805842]

Authors

Guo L, Dixon RA, Paiva NL

Title

The 'pterocarpan synthase' of alfalfa: association and co-induction of vestitone reductase and 7,2'-dihydroxy-4'-methoxy-isoflavanol (DMI) dehydratase, the two final enzymes in medicarpin biosynthesis.

Journal

FEBS Lett 356:221-5 (1994)
DOI:10.1016/0014-5793(94)01267-9

Reference

2 [PMID:8071365]

Authors

Guo L, Dixon RA, Paiva NL.

Title

Conversion of vestitone to medicarpin in alfalfa (Medicago sativa L.) is catalyzed by two independent enzymes. Identification, purification, and characterization of vestitone reductase and 7,2'-dihydroxy-4'-methoxyisoflavanol dehydratase.

Journal

J Biol Chem 269:22372-8 (1994)

Reference

3 [PMID:28394400]

Authors

Uchida K, Akashi T, Aoki T

Title

The Missing Link in Leguminous Pterocarpan Biosynthesis is a Dirigent Domain-Containing Protein with Isoflavanol Dehydratase Activity.

Journal

Plant Cell Physiol 58:398-408 (2017)
DOI:10.1093/pcp/pcw213

Sequence

[gmx:100500621] [lja:130742227]