Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Prakash, P.; Pathak, N.; Hasnain, S.E.
    pheA (Rv3838c) of Mycobacterium tuberculosis encodes an allosterically regulated monofunctional prephenate dehydratase that requires both catalytic and regulatory domains for optimum activity (2005), J. Biol. Chem., 280, 20666-20671.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.51 L-Phe allosteric activator, activation above 0.1 mM Mycobacterium tuberculosis
4.2.1.51 L-Trp allosteric activator, activation above 0.1 mM Mycobacterium tuberculosis
4.2.1.51 L-Tyr allosteric activator, activation above 0.1 mM Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.51 the catalytic and regulatory domains of prephenate dehydratase are individually cloned in the NdeI/XhoI sites of pET23a vector and expressed in Escherichia coli BL21(DE3) Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.51 L-Phe at concentration up to 0.1 mM Mycobacterium tuberculosis
4.2.1.51 L-Trp at concentration up to 0.1 mM Mycobacterium tuberculosis
4.2.1.51 L-Tyr at concentration up to 0.1 mM Mycobacterium tuberculosis
4.2.1.51 NaCl enzyme activity is completely abolished in the presence of 200 mM and higher concentrations of NaCl Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.51 0.5
-
 prephenate
-
 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.51 prephenate Mycobacterium tuberculosis key regulator enzyme in L-phenylalanine biosynthesis phenylpyruvate + H2O + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.51 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.51 catalytic and regulatory domains of prephenate dehydratase, individually cloned in the NdeI/XhoI sites of pET23a vector and expressed in Escherichia coli BL21(DE3) Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.51 prephenate key regulator enzyme in L-phenylalanine biosynthesis Mycobacterium tuberculosis phenylpyruvate + H2O + CO2
-
 ?
4.2.1.51 prephenate the enzyme is absolutely dependent on the presence of catalytic as well as the regulatory domains for optimum enzyme activity. The enzyme is monofunctional and does not possess any chorismate mutase activity Mycobacterium tuberculosis phenylpyruvate + H2O + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.51 dimer
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.51 37 42
-
 Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.51 6 7
-
 Mycobacterium tuberculosis