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Literature summary extracted from

  • Rubin, J.L.; Jensen, R.A.
    Enzymology of L-tyrosine biosynthesis in mung bean (Vigna radiata [L.] Wilczek) (1979), Plant Physiol., 64, 727-734.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.13 L-tyrosine competitive inhibition Vigna radiata
1.3.1.13 p-hydroxymercurybenzoic acid
-
 Vigna radiata
1.3.1.78 L-tyrosine no inhibition Vigna radiata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.13 0.012
-
 NADP+ pretyrosine as substrate Vigna radiata
1.3.1.13 0.014
-
 NADP+ prephenate as substrate Vigna radiata
1.3.1.13 0.077
-
 prephenate
-
 Vigna radiata
1.3.1.78 additional information
-
 additional information
-
 Vigna radiata

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.13 chloroplast
-
 Vigna radiata 9507
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.13 52000
-
 gel filtration Vigna radiata
1.3.1.78 52000
-
 gel filtration Vigna radiata

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.13 prephenate + NADP+ Vigna radiata
-
 4-hydroxyphenylpyruvate + CO2 + NADPH
-
 ?
1.3.1.13 prephenate + NADP+ Burkholderia cepacia
-
 4-hydroxyphenylpyruvate + CO2 + NADPH
-
 ?
1.3.1.78 L-arogenate + NAD+ Vigna radiata
-
 L-tyrosine + NADH + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.13 Burkholderia cepacia
-
-
-
1.3.1.13 Comamonas testosteroni
-
-
-
1.3.1.13 Pseudomonas alkanolytica
-
-
-
1.3.1.13 Vigna radiata
-
 mung bean, [L.] Wilczek, originally classified as Phaseolus aureus [L.] Roxb.
-
1.3.1.78 Vigna radiata
-
 NADP-dependent prephenate and pretyrosine dehydrogenase copurified, multifunctional protein ?
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.13 partially Vigna radiata
1.3.1.78 partial, NADP-dependent prephenate and pretyrosine dehydrogenase copurified, probably multifunctional protein Vigna radiata

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.1.13 seedling
-
 Vigna radiata
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.13 321
-
-
 Vigna radiata

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.13 prephenate + NADP+
-
 Vigna radiata 4-hydroxyphenylpyruvate + CO2 + NADPH
-
 ?
1.3.1.13 prephenate + NADP+
-
 Burkholderia cepacia 4-hydroxyphenylpyruvate + CO2 + NADPH
-
 ?
1.3.1.78 L-arogenate + NAD(P)+
-
 Vigna radiata L-tyrosine + NAD(P)H + CO2
-
 ?
1.3.1.78 L-arogenate + NAD+
-
 Vigna radiata L-tyrosine + NADH + CO2
-
 ?
1.3.1.78 prephenate + NAD(P)+
-
 Vigna radiata ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.13 prephenate-pretyrosine dehydrogenase single multifunctional protein catalyzes both dehydrogenase reactions Vigna radiata

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.3.1.13 55
-
 up to 10 min inactivates the enzyme Vigna radiata

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.13 7.5
-
-
 Vigna radiata

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.13 NADP+
-
 Burkholderia cepacia
1.3.1.13 NADP+ uses either cofactor, NADP+ and NAD+ Comamonas testosteroni
1.3.1.13 NADP+ utilizes only NADP+ Pseudomonas alkanolytica
1.3.1.78 NADP+
-
 Vigna radiata