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Literature summary extracted from

  • Janiak, V.; Petersen, M.; Zentgraf, M.; Klebe, G.; Heine, A.
    Structure and substrate docking of a hydroxy(phenyl)pyruvate reductase from the higher plant Coleus blumei Benth (2010), Acta Crystallogr. Sect. D, 66, 593-603.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.237 expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS Coleus scutellarioides

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.237 apoenzyme and enzyme in complex with NADP+, sitting drop vapour diffusion method, mixing of 0.001 ml of 6 mg/ml protein or 15 mg/ml protein with 2 mM NADP+ in 50 mM Tris-HCl, pH 7.0, with 0.001 ml of well solution containing 30% 2-methyl-2,4-pentanediol, 0.2 M NaCl, 0.1 M Tris-HCl, pH 7.5 at 4°C, or 20% PEG 1000, 0.1 M imidazole, pH 7.5, 4 mM 4-hydroxyphenylpyruvate, 0.2 mM DTT at 26°C, leading to one-crystal clusters or tetragonal bipyramid-shaped crystals, X-ray diffraction structure determination and analysis at 1.47 A and 2.2 A, respectively, modeling Coleus scutellarioides

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.237 34113
-
 2 * 34113, sequence calculation and crystal structure Coleus scutellarioides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.237 3-(4-hydroxyphenyl)pyruvate + NADPH + H+ Coleus scutellarioides
-
 3-(4-hydroxyphenyl)lactate + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.237 Coleus scutellarioides Q65CJ7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.237 recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity and 2',5'-ADP affinity chromatography and dialysis Coleus scutellarioides

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.237 cell suspension culture
-
 Coleus scutellarioides
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.237 3,4-dihydroxyphenylpyruvate + NADH + H+
-
 Coleus scutellarioides 3-(3,4-dihydroxyphenyl)lactate + NAD+
-
 r
1.1.1.237 3,4-dihydroxyphenylpyruvate + NADPH + H+
-
 Coleus scutellarioides 3-(3,4-dihydroxyphenyl)lactate + NADP+
-
 r
1.1.1.237 3-(4-hydroxyphenyl)pyruvate + NADH + H+
-
 Coleus scutellarioides 3-(4-hydroxyphenyl)lactate + NAD+
-
 r
1.1.1.237 3-(4-hydroxyphenyl)pyruvate + NADPH + H+
-
 Coleus scutellarioides 3-(4-hydroxyphenyl)lactate + NADP+
-
 ?
1.1.1.237 3-(4-hydroxyphenyl)pyruvate + NADPH + H+ substrate bindiing structure, docking study, overview Coleus scutellarioides 3-(4-hydroxyphenyl)lactate + NADP+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.237 homodimer 2 * 34113, sequence calculation and crystal structure Coleus scutellarioides
1.1.1.237 More molecular docking study, overview Coleus scutellarioides

Synonyms

EC Number Synonyms Comment Organism
1.1.1.237 H(P)PR
-
 Coleus scutellarioides
1.1.1.237 HPPR
-
 Coleus scutellarioides
1.1.1.237 hydroxy(phenyl)pyruvate reductase
-
 Coleus scutellarioides
1.1.1.237 hydroxyphenylpyruvate reductase
-
 Coleus scutellarioides

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.237 additional information NADH as well as NADPH can serve as the electron donor Coleus scutellarioides
1.1.1.237 NADP+
-
 Coleus scutellarioides
1.1.1.237 NADPH preferred cofactor compared to NAD+, forms three hydrogen bonds to the protein via N41 to Asp256 OD2 and Ile230 O and O40 to His279 NE2 Coleus scutellarioides

General Information

EC Number General Information Comment Organism
1.1.1.237 evolution the enzyme belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases Coleus scutellarioides
1.1.1.237 additional information movement of the two domains after cosubstrate binding in order to close the inter-domain cleft for catalysis. The amino acids participating in the contacts are Leu205, Arg232 and His279 from the cosubstrate-binding domain and Ser53, Gly77 and Asp79 from the substrate-binding domain. The active site of H(P)PR is formed by the amino-acid residues Arg232 and His279, active site structure, overview Coleus scutellarioides