Disease relevance of Phenylacetyl-coenzyme A

• At this time, results are interpreted to suggest that in phenylketonuria, phenylacetate exerts its neurotoxic action through its metabolic product, phenylacetyl-CoA, which could severely decrease the availability of acetyl-CoA [1].
• Genetic Characterization of the Phenylacetyl-Coenzyme A Oxygenase from the Aerobic Phenylacetic Acid Degradation Pathway of Escherichia coli [2].
• Coregulation by phenylacetyl-coenzyme A-responsive PaaX integrates control of the upper and lower pathways for catabolism of styrene by Pseudomonas sp. strain Y2 [3].
• In the denitrifying bacterium Thauera aromatica phenylacetate is oxidized, under anoxic conditions, to the common intermediate benzoyl-CoA via the intermediates phenylacetyl-CoA and phenylglyoxylate (benzoylformate) [4].
• The enzyme phenylacetyl-CoA: 6-Aminopenicillanic acid acyltransferase of Penicillium chrysogenum was evaluated by direct bioassay against Micrococcus luteus ATCC 9341 [5].

High impact information on Phenylacetyl-coenzyme A

• PhlD exhibits broad substrate specificity, accepting C(4)-C(12) aliphatic acyl-CoAs and phenylacetyl-CoA as the starters to form C6-polyoxoalkylated alpha-pyrones from sequential condensation with malonyl-CoA [6].
• The paaK gene codes for a phenylacetyl-CoA ligase that catalyzes the activation of PA to phenylacetyl-CoA (PA-CoA) [7].
• We show here that the paaABCDE genes of the paa cluster responsible for phenylacetate degradation in Escherichia coli W encode a five-component oxygenase that hydroxylates phenylacetyl-coenzyme A (CoA), the first intermediate of the pathway [2].
• The PaaX repressor, a link between penicillin G acylase and the phenylacetyl-coenzyme A catabolon of Escherichia coli W [8].
• One, termed ACS I, uses acetyl-CoA and isobutyryl-CoA but not indoleacetyl-CoA or phenylacetyl-CoA as substrates, while the other, ACS II, utilizes all four CoA derivatives [9].

Chemical compound and disease context of Phenylacetyl-coenzyme A

• Reactions performed in the presence of Escherichia coli penicillin acylase did not generated active products when phenylacetyl-CoA was the substrate; they did with octanoyl-CoA [5].

Biological context of Phenylacetyl-coenzyme A

• Amplification of phl in an autonomous replicating plasmid led to an 8-fold increase in phenylacetyl-CoA ligase activity and a 35% increase in penicillin production [10].

Anatomical context of Phenylacetyl-coenzyme A

• The Golgi vesicles isolated from the protoplasts of high-yield mutant showed activities of enzymes of the pathway of benzylpenicillin biosynthesis i.e., delta-/L-alpha-aminoadipyl/-L-cysteinyl-D-valine synthetase, isopenicillin N synthetase, phenylacetyl: coenzyme A ligase, and acyl-exchange activity [11].

Associations of Phenylacetyl-coenzyme A with other chemical compounds

• Direct evaluation of phenylacetyl-CoA: 6-aminopenicillanic acid acyltransferase of Penicillium chrysogenum by bioassay [5].
• Amplification and disruption of the phenylacetyl-CoA ligase gene of Penicillium chrysogenum encoding an aryl-capping enzyme that supplies phenylacetic acid to the isopenicillin N-acyltransferase [10].

Gene context of Phenylacetyl-coenzyme A

• With ACS II, the apparent Km value for phenylacetyl-CoA was 4 microM [9].
• The phenylacetyl-CoA ligase encoded by the phl gene is therefore involved in penicillin production, although a second aryl-CoA ligase appears to contribute partially to phenylacetic acid activation [10].

References