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Literature summary extracted from

  • Mauge, C.; Granier, T.; dEstaintot, B.L.; Gargouri, M.; Manigand, C.; Schmitter, J.M.; Chaudiere, J.; Gallois, B.
    Crystal structure and catalytic mechanism of leucoanthocyanidin reductase from Vitis vinifera (2010), J. Mol. Biol., 397, 1079-1091.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.1.3 expression of His-tagged LAR1 in Escherichia coli Vitis vinifera

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.1.3 LAR1 in complex with or without NADPH and one of its natural products, (+)-catechin, X-ray diffraction structure determination and analysis at 1.75-2.72 A resolution Vitis vinifera

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.1.3 additional information Vitis vinifera leucoanthocyanidin reductase catalyzes the NADPH-dependent reduction of 2R,3S,4S-flavan-3,4-diols into 2R,3S-flavan-3-ols ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.3 Vitis vinifera Q4W2K4 LAR1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.3 recombinant His-tagged LAR1 from Escherichia coli by nickel affinity chromatography Vitis vinifera

Reaction

EC Number Reaction Comment Organism Reaction ID
1.17.1.3 (2R,3S)-catechin + NADP+ + H2O = 2,3-trans-3,4-cis-leucocyanidin + NADPH + H+ two-step catalytic mechanism involving the formation of an enzyme-bound quinone methide intermediate prior to reduction, overview. A concerted dehydration precedes an NADPH-mediated hydride transfer at C4. The dehydration step involves a Lys-catalyzed deprotonation of the phenolic OH7 through a bridging water molecule and a His-catalyzed protonation of the benzylic hydroxyl at C4. The resulting quinone methide serves as an electrophilic target for hydride transfer at C4. The role of the lysine is to promote the formation of this intermediate by catalyzing the deprotonation of a phenolic hydroxyl Vitis vinifera
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.3 additional information leucoanthocyanidin reductase catalyzes the NADPH-dependent reduction of 2R,3S,4S-flavan-3,4-diols into 2R,3S-flavan-3-ols Vitis vinifera ?
-
 ?
1.17.1.3 additional information the coenzyme and substrate binding pocket is preformed in the apoprotein and not markedly altered upon NADPH binding, ternary complex structure, substrate binding site structure, overview. Ordering of a short 3_10 helix associated with substrate binding, His122 and Lys140 act as acid-base catalysts Vitis vinifera ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.1.3 ? x * 46943.3, recombinant enzyme, mass spectrometry Vitis vinifera
1.17.1.3 More three-dimensional structure and structure comparisons, overview Vitis vinifera

Synonyms

EC Number Synonyms Comment Organism
1.17.1.3 LAR
-
 Vitis vinifera
1.17.1.3 LAR1
-
 Vitis vinifera
1.17.1.3 leucoanthocyanidin reductase
-
 Vitis vinifera
1.17.1.3 More LAR belongs to the short-chain dehydrogenase/reductase superfamily and to the PIP (pinoresinol-lariciresinol reductase, isoflavone reductase, and phenylcoumaran benzylic ether reductase) family Vitis vinifera

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.3 NADPH dependent on, binding site structure, overview Vitis vinifera

General Information

EC Number General Information Comment Organism
1.17.1.3 physiological function leucoanthocyanidin reductase catalyzes the NADPH-dependent reduction of 2R,3S,4S-flavan-3,4-diols into 2R,3S-flavan-3-ols, a subfamily of flavonoids that is important for plant survival and for human nutrition Vitis vinifera