KEGG   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
CCAJ: 109797846
APRC: 113862134 113863229
MTR: MTR_7g093820 MTR_7g093830 MTR_7g093850
CAM: 101491323
LJA: Lj1g3v4383290.1(Lj1g3v4383290.1)
ADU: 107492865
AIP: 107645384
 » 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
Other DBs
ExplorEnz - The Enzyme Database: 4.2.1.139
IUBMB Enzyme Nomenclature: 4.2.1.139
ExPASy - ENZYME nomenclature database: 4.2.1.139
BRENDA, the Enzyme Database: 4.2.1.139

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