Cofactors

There are no Cofactors for this Enzyme

Reaction Mechanism

There are no Reaction Mechanism for this Enzyme

Reaction Parameters

• Kinetic Parameters

  Organism	KM Value [mM]	Substrate	Comment
  Penicillium chrysogenum	0.283	palmitate	recombinant enzyme, pH 7.5, 30°C

• Temperature

  Organism	Temperature Range	Comment
  Penicillium chrysogenum	32 - 42	32°C: about 40% of maximal activity, 42°C: about 40% of maximal activity
  Thermus thermophilus	50 - 90

• pH

  Organism	pH Range	Comment
  Thermus thermophilus	6 - 9
  Aromatoleum evansii	7 - 9	pH 9: 55% of maximal activity, pH 9.0: 50% of maximal activity
  Pseudomonas sp.	8.5 - 9	pH 8.5: activity maximum, pH 9.0: 50% of maximal activity

Associated Proteins

Citations

• The presence of benzene ring activating CoA ligases for aromatics degradation in the ANaerobic MEthanotrophic (ANME) archaea.
• Polyethylene Degradation by a Rhodococcous Strain Isolated from Naturally Weathered Plastic Waste Enrichment.
• Isophthalate:coenzyme A ligase initiates anaerobic degradation of xenobiotic isophthalate.
• Characterization of a phenylacetate-CoA ligase from Penicillium chrysogenum.
• Metabolic handoffs between multiple symbionts may benefit the deep-sea bathymodioline mussels.
• Phenylacetate metabolism in thermophiles: characterization of phenylacetate-CoA ligase, the initial enzyme of the hybrid pathway in Thermus thermophilus.
• Progress in structural and functional study of the bacterial phenylacetic acid catabolic pathway, its role in pathogenicity and antibiotic resistance.
• Genomic Analysis of Sphingopyxis sp. USTB-05 for Biodegrading Cyanobacterial Hepatotoxins.
• Systems Biology of Aromatic Compound Catabolism in Facultative Anaerobic Aromatoleum aromaticum EbN1^T.
• Aryl Coenzyme A Ligases, a Subfamily of the Adenylate-Forming Enzyme Superfamily.
• Polystyrene Degradation by Exiguobacterium sp. RIT 594: Preliminary Evidence for a Pathway Containing an Atypical Oxygenase.