Disease relevance of catA

• The catA gene, encoding the major CatA from a root-colonizing isolate Pseudomonas putida (Pp), was cloned by complementation into a catalase (Cat)-deficient Escherichia coli (Ec) strain UM2 [1].
• The relationship between the pheB gene and other C12O-encoding genes has been shown: comparison of the pheB sequence with sequences of catA of Alcaligenes calcoaceticus, tfdC of A. eutrophus and clcA of P. putida demonstrated that there are conserved residues in all the four protein products of these genes [2].
• Crude extracts of Escherichia coli cells carrying the catA gene downstream from the lac promoter showed the enzyme activity [3].

High impact information on catA

• The catA genes catA1 and catA2 encoding CD I and CD II, respectively, were cloned from a gene library of this bacterium [4].
• This contrasts with the gene arrangement in other bacteria, in which catA lies several kilobases upstream from catB [5].
• Properties of Tn5 mutants confirmed earlier suggestions that catR is a transcriptional activator and indicated that catA is activated by CatR independently of its activation of catBC [5].
• A comparison of the DNA sequences of various catA genes from other sources revealed their common ancestry, whereas a comparison of the amino acid sequences of the enzymes revealed clear reflection of substrate specificity [3].
• Catechol 1,2-dioxygenase catalyzes the oxygenative ring cleavage of catechol to form cis,cis-muconic acid and is encoded by a catA gene [3].

Associations of catA with chemical compounds

• Benzoate dioxygenase (BenA, BenD) and catechol 1,2-dioxygenase (CatA) were induced by benzoate [6].

Analytical, diagnostic and therapeutic context of catA

• We have cloned a catA gene from Pseudomonas putida mt-2 using a PCR product of amino acid sequence-based primers as a probe [3].

References