Disease relevance of PFL_0592

• Tyrosine emission in the tryptophanless azurin from Pseudomonas fluorescens [1].
• The crystal structure has been determined by molecular replacement on the basis of the molecular model of azurin from Alcaligenes denitrificans, and refined by the method of molecular dynamics simulation and energy-restrained least-squares methods [2].

High impact information on PFL_0592

• The apparent Km value of ADH IIB for azurin, determined by steady-state kinetics, was decreased several-fold by increasing the ionic strength [3].
• Thus, the results presented here strongly suggest that azurin works as an electron-transfer mediator in a PQQ-dependent alcohol oxidase respiratory chain in P. putida HK5 [3].
• Comparison of the fluorescence spectra and the effect of temperature on the quantum yields of fluorescence of Azurin (from Pseudomonas fluorescens ATCC-13525-2) and 3-methylindole (in methylcyclohexane solution) provides substantive evidence that the tryptophan residue in azurin is completely inaccessible to solvent molecules [4].
• Conformational heterogeneity of the copper binding site in azurin. A time-resolved fluorescence study [4].
• The Azurin Pseudomones fluorescens has been crystallized in the presence of ammonium sulfate and Tris buffer at pH 7 [5].

Chemical compound and disease context of PFL_0592

• A strain of Pseudomonas fluorescens contains an azurin with no tryptophan and two tyrosines [1].

Biological context of PFL_0592

• The amino acid sequence of Pseudomonas putida azurin [6].
• Of the strains that clustered on the basis of genotype (DNA, azurin) 88% also clustered on the basis of phenotype [7].

Associations of PFL_0592 with chemical compounds

• The results are interpreted as originating from different interactions of the tryptophan with two conformers of the copper-ligand complex in azurin [4].
• Examination of the complete sequence indicated P. putida azurin contained unique Asp and Ala residues at positions 19 and 21, respectively, that have not been found in any other azurin sequence [6].

Analytical, diagnostic and therapeutic context of PFL_0592

• Crystallization and preliminary crystallographic studies of the crystals of the azurin Pseudomonas fluorescens [5].
• The low molecular weight "blue" copper protein, azurin, has been purified from Pseudomonas putida (NCIB 9869) to homogeneity using various chromatographic techniques including reverse-phase HPLC [6].

References