Disease relevance of arcA

• Crystal structures representing the Michaelis complex and the thiouronium reaction intermediate of Pseudomonas aeruginosa arginine deiminase [1].
• Inhibition of human peripheral blood mononuclear cell proliferation by Streptococcus pyogenes cell extract is associated with arginine deiminase activity [2].
• Structural and functional analysis of the gene cluster encoding the enzymes of the arginine deiminase pathway of Lactobacillus sake [3].
• The arginine deiminase pathway in Rhizobium etli: DNA sequence analysis and functional study of the arcABC genes [4].
• In an FNR-positive E. coli strain, the ANR-dependent promoter of the arcDABC operon, which encodes the enzymes of the arginine deiminase pathway, was not expressed [5].

High impact information on arcA

• L-arginine deiminase (ADI) catalyzes the irreversible hydrolysis of L-arginine to citrulline and ammonia [1].
• Asp280 and Asp166 engage in ionic interactions with the guanidinium group in the C406A ADI [1].
• Structural insight into arginine degradation by arginine deiminase, an antibacterial and parasite drug target [6].
• A catalytic triad, Cys-His-Glu/Asp (arranged in a different manner from that of the thiol proteases), seen in the other arginine-modifying enzymes is also conserved in ADI, as well as many other residues involved in substrate binding [6].
• The arcDABC operon of Pseudomonas aeruginosa encodes the enzymes of the arginine deiminase pathway and is induced by oxygen limitation [7].

Chemical compound and disease context of arcA

• L-canavanine is a time-controlled mechanism-based inhibitor of Pseudomonas aeruginosa arginine deiminase [8].
• Anaerobic growth of Pseudomonas aeruginosa on arginine depends on the arcDABC operon encoding the enzymes of the arginine deiminase pathway [9].
• NH2-terminal sequencing of the protein revealed that it was identical to the previously characterized streptococcal acid glycoprotein (SAGP); this protein possesses between 31.5 and 39.0% amino acid identity with arginine deiminase (AD) from Mycoplasma hominis, Mycoplasma arginini, Pseudomonas putida, and Pseudomonas aeruginosa [2].
• In the absence of oxygen and nitrate, Pseudomonas aeruginosa metabolizes arginine via the arginine deiminase pathway, which allows slow growth on rich media [10].

Biological context of arcA

• We have determined the nucleotide sequences of the arcA and arcC genes [11].
• The arcA open reading frame specifies a polypeptide of 46.3 kDa [11].
• Deletion of either intergenic region in the P. aeruginosa chromosome led to the loss of the arcA or arcAB transcript, respectively [9].
• R. etli arcA mutants, with polar effects on arcB and arcC, were constructed by insertion mutagenesis [4].
• Gene inactivation was shown by loss of the fnrA transcript and detection of an arginine deiminase (EC 3.5.3.6)-negative phenotype in the mutants [12].

Associations of arcA with chemical compounds

• The other mutant (C6) and its revertant (C6Rv) were derived from PAO6261, a mutant of PAO1 with a deletion in the anr gene (anaerobic regulation of arginine deiminase and nitrate reduction) that controls anaerobic respiration in P. aeruginosa [13].
• Attention is then directed to the limited fermentative capacity of P. aeruginosa with discussion of the arginine deiminase pathway and the role of pyruvate fermentation [14].
• It is concluded that the ArcD protein is a transport system that catalyzes an electroneutral exchange between arginine and ornithine to allow high-efficiency energy conversion in the arginine deiminase pathway [10].

Regulatory relationships of arcA

• The arginine decarboxylase is induced by arginine which also induces the three enzymes of the arginine deiminase pathway but only in stress conditions such as a shift from aerobic growth conditions to very low oxygen tension [15].

Other interactions of arcA

• The arcA mutation was highly cotransducible with arcB [16].
• Halobacterium halobium (salinarium) is able to grow fermentatively via the arginine deiminase pathway, which is mediated by three enzymes and one membrane-bound arginine-ornithine antiporter [17].
• Constructed agu arc double mutants (blocked in the arginine decarboxylase and arginine deiminase pathways) used arginine efficiently as the sole carbon and nitrogen source [18].

References