620-76-8

Upstream product

• 97645-23-3 prephenate^2- 
• 842-74-0 4-benzylidene-2-phenyloxazole-5(4H)-one 
• 100-52-7 benzaldehyde 

Downstream Products

• 63-91-2 L-phenylalanine 
• 20312-36-1 L-3-phenyllactic acid 
• 97645-23-3 prephenate^2- 
• 5355-63-5 3-hydroxy-4-phenyl-2-butanone 
• 62763-33-1 (+/-)-3-hydroxy-1-phenyl-2-butanone 

Relevant academic research and scientific papers

Kinetic and structural characterization of a heterohexamer 4-oxalocrotonate tautomerase from chloroflexus aurantiacus J-10-fl: Implications for functional and structural diversity in the tautomerase superfamily

4-Oxalocrotonate tautomerase (4-OT) isozymes play prominent roles in the bacterial utilization of aromatic hydrocarbons as sole carbon sources. These enzymes catalyze the conversion of 2-hydroxy-2,4-hexadienedioate (or 2-hydroxymuconate) to 2-oxo-3-hexene

A thermodynamic investigation of some reactions involving prephenic acid

Calorimetric enthalpies of reaction have been measured for the following enzyme-catalysed reactions at the temperature 298.15 K: prephenate(aq) = phenylpyruvate(aq) + carbon dioxide(aq), prephenate(aq) + NADox(aq) + H2O(1) = 4-hydroxyphenylpyruvate(aq) + NADred(aq) + carbon dioxide (aq). Here, NADox and NADred are, respectively, the oxidized and reduced forms of β-nicotinamide adenine dinucleotide. The enzymes that catalyse these respective reactions, prephenate dehydratase and prephenate dehydrogenase, were prepared by expression of the appropriate plasmids using the techniques of molecular biology. The calorimetric measurements together with the equilibrium modeling calculations lead to a standard molar enthalpy change ΔrHom = -(126 ± 5) kJ·mol-1 for the reference reaction: prephenate2-(aq) = phenylpyruvate-(aq) + HCO-3(aq). Similarly, ΔrHom = -(74 ± 3) kJ·mol-1 for the reference reaction: prephenate2-(aq) + NAD-ox(aq) + H2O(1) = 4-hydroxyphenylpyruvate- (aq) + NAD2red(aq) + HCO-3(aq) + H+aq). Both results pertain to T = 298.15 K and ionic strength I = 0. Benson estimates for the entropies lead to approximate values of the equilibrium constants K ≈ 1·1026 and K ≈ 1·1012, respectively, for the above two reference reactions.

Structural and functional characterization of a macrophage migration inhibitory factor homologue from the marine cyanobacterium prochlorococcus marinus

Macrophage migration inhibitory factor (MIF) is a multifunctional mammalian cytokine, which exhibits tautomerase and oxidoreductase activity. MIF homologues with pairwise sequence identities to human MIF ranging from 31% to 41% have been detected in vario

Kinetic and structural characterization of DmpI from Helicobacter pylori and Archaeoglobus fulgidus, two 4-oxalocrotonate tautomerase family members

The tautomerase superfamily consists of structurally homologous proteins that are characterized by a β-α-β fold and a catalytic amino-terminal proline. 4-Oxalocrotonate tautomerase (4-OT) family members have been identified and categorized into five subfa

Kinetic and Structural Analysis of Two Linkers in the Tautomerase Superfamily: Analysis and Implications

The tautomerase superfamily (TSF) is a collection of enzymes and proteins that share a simple β-α-β structural scaffold. Most members are constructed from a single-core β-α-β motif or two consecutively fused β-α-β motifs in which the N-terminal proline (Pro-1) plays a key and unusual role as a catalytic residue. The cumulative evidence suggests that a gene fusion event took place in the evolution of the TSF followed by duplication (of the newly fused gene) to result in the diversification of activity that is seen today. Analysis of the sequence similarity network (SSN) for the TSF identified several linking proteins ("linkers") whose similarity links subgroups of these contemporary proteins that might hold clues about structure-function relationship changes accompanying the emergence of new activities. A previously uncharacterized pair of linkers (designated N1 and N2) was identified in the SSN that connected the 4-oxalocrotonate tautomerase (4-OT) and cis-3-chloroacrylic acid dehalogenase (cis-CaaD) subgroups. N1, in the cis-CaaD subgroup, has the full complement of active site residues for cis-CaaD activity, whereas N2, in the 4-OT subgroup, lacks a key arginine (Arg-39) for canonical 4-OT activity. Kinetic characterization and nuclear magnetic resonance analysis show that N1 has activities observed for other characterized members of the cis-CaaD subgroup with varying degrees of efficiencies. N2 is a modest 4-OT but shows enhanced hydratase activity using allene and acetylene compounds, which might be due to the presence of Arg-8 along with Arg-11. Crystallographic analysis provides a structural context for these observations.

New methods for the selective alkylation of 3-thioxo-1,2,4-triazin-5-ones

A method for regioselective alkylation of the 3-thiono-1,2,4-triazinone 10 at the sulfur atom is reported. Subsequent Claisen rearrangements, triggered either thermally or using a palladium catalyst, deliver N-alkylated products 13, while acid-catalysed r

Characterization of a newly identified mycobacterial tautomerase with promiscuous dehalogenase and hydratase activities reveals a functional link to a recently diverged cis -3-chloroacrylic acid dehalogenase

The enzyme cis-3-chloroacrylic acid dehalogenase (cis-CaaD) is found in a bacterial pathway that degrades a synthetic nematocide, cis-1,3-dichloropropene, introduced in the 20th century. The previously determined crystal structure of cis-CaaD and its prom