Literature summary for 1.17.1.3 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.

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Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Vitis vinifera	Q4W2K4	LAR1	-

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
(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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?
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

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

Synonyms

Synonyms	Comment	Organism
LAR	-	Vitis vinifera
LAR1	-	Vitis vinifera
leucoanthocyanidin reductase	-	Vitis vinifera
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

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

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)