Comparative study of catalase-peroxidases (KatGs)

Singh, Rahul; Wiseman, B.; Deemagarn, Taweewat; Jha, Vikash Kumar; Switala, Jacek; Loewen, P.C.

doi:10.1016/j.abb.2007.12.008

Cited by 106 publications

(81 citation statements)

References 86 publications

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“…These structures have provided many insights into KatG structure and function and confirmed the considerable similarity in structure between BpKatG and MtKatG consistent with the similarity in enzymatic properties (16). Unfortunately, they have not led to an identification of the binding sites for the two substrates, INH and NAD ϩ , which would potentially enhance our understanding of the INH activation process.…”

Section: Isonicotinic Acid Hydrazide (Isoniazid or Inh)mentioning

confidence: 89%

“…A multiplicity of methods has been employed to directly and indirectly assay INH activation, including the determination of INH oxidation to isonicotinic acid (9, 10), the HPLC assay of INH disappearance (11), the inactivation of InhA in a mixture of InhA and KatG (7,12,13,14), the HPLC detection of IN⅐NAD (4, 15), and the direct measurement of IN⅐NAD using its characteristic absorbance at 326 nm (6,7,12,15,16). Reports of INH activation in mixtures lacking an external oxidant (4,5,6,9,12,14,15) initially suggested that the peroxidatic process may not be required, but the mixtures of INH, NADH, and KatG would have supported NADH reduction of molecular oxygen to superoxide and low levels of H 2 O 2 (15) to activate the peroxidase reaction.…”

Section: Isonicotinic Acid Hydrazide (Isoniazid or Inh)mentioning

confidence: 99%

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Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-NAD by Catalase-peroxidases

Wiseman

Carpena

Feliz

et al. 2010

Journal of Biological Chemistry

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Activation of the pro-drug isoniazid (INH) as an anti-tubercular drug in Mycobacterium tuberculosis Isonicotinic acid hydrazide (isoniazid or INH)3 is a widely used anti-tubercular pro-drug that requires activation in a reaction involving the catalase-peroxidase KatG of Mycobacterium tuberculosis (MtKatG) (1) whereby the hydrazine group is removed and the isonicotinyl portion is added to NAD ϩ to generate isonicotinyl-NAD or IN⅐NAD (see Fig. 1). Once formed, IN⅐NAD inhibits the synthesis of mycolic acids, and therefore, the growth of M. tuberculosis, by binding to the longchain enoyl acyl carrier protein reductase (InhA) (2). Despite understanding the role of IN⅐NAD in the inhibition of mycolic acid synthesis and knowing that KatG is required for INH activation in vivo, uncertainties about the mechanism of its formation remain.The involvement of MtKatG in INH activation suggested that the peroxidatic process had a role, and this provided a focus for several studies employing external oxidants such as peroxyacetic acid (3), t-butyl hydroperoxide (4 -6) and low levels of H 2 O 2 (7, 6) to activate the peroxidatic pathway for INH oxidation and activation. In addition, EPR studies have demonstrated that INH can serve as an electron source to reduce peroxidatic intermediates, including specific Trp ⅐ radical species following peroxyacetic acid oxidation of MtKatG (3,8).A multiplicity of methods has been employed to directly and indirectly assay INH activation, including the determination of INH oxidation to isonicotinic acid (9, 10), the HPLC assay of INH disappearance (11), the inactivation of InhA in a mixture of InhA and KatG (7,12,13,14), the HPLC detection of IN⅐NAD (4, 15), and the direct measurement of IN⅐NAD using its characteristic absorbance at 326 nm (6,7,12,15,16). Reports of INH activation in mixtures lacking an external oxidant (4,5,6,9,12,14,15) initially suggested that the peroxidatic process may not be required, but the mixtures of INH, NADH, and KatG would have supported NADH reduction of molecular oxygen to superoxide and low levels of H 2 O 2 (15) to activate the peroxidase reaction.Despite the considerable evidence that a peroxidatic process is involved in IN⅐NAD synthesis, attempts to rationalize the reaction entirely in terms of the peroxidatic pathway generally produced models that were incomplete from the standpoint of electron balance (5,7,10) or that involved hypothetical intermediates not characterized in any other system (5, 6). For example, a common scheme shows the isonicotinyl radical, generated in a peroxidatic reaction, reacting with NAD ϩ to yield IN⅐NAD, when such a reaction would actually yield the IN⅐NAD ϩ ⅐ radical (Fig. 1). The need to reduce this radical in an oxidizing environment suggests that more than a simple peroxidatic pathway is involved in the INH activation process. This rationale leads to superoxide, O 2. , a known reducing agent with

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Section: Isonicotinic Acid Hydrazide (Isoniazid or Inh)mentioning

confidence: 89%

Section: Isonicotinic Acid Hydrazide (Isoniazid or Inh)mentioning

confidence: 99%

Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-NAD by Catalase-peroxidases

Wiseman

Carpena

Feliz

et al. 2010

Journal of Biological Chemistry

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“…To illustrate the usefulness of these vectors for genetic studies, we generated a mutation in the X. fastidiosa cpeB gene. The cpeB ORF shows strong amino acid sequence similarity to known catalases/peroxidases, which are some of the enzymes responsible for detoxifying H 2 O 2 (17,37). Sensitivity to hydrogen peroxide is easy to examine in vitro by using a disk diffusion inhibition assay, making the cpeB gene a suitable choice for testing our chromosomal complementation system.…”

Section: Resultsmentioning

confidence: 99%

Chromosome-Based Genetic Complementation System forXylella fastidiosa

Matsumoto

Young

Igo³

2009

Appl Environ Microbiol

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Xylella fastidiosa is a xylem-limited, gram-negative bacterium that causes Pierce's disease of grapevine. Here, we describe the construction of four vectors that facilitate the insertion of genes into a neutral site (NS1) in the X. fastidiosa chromosome. These vectors carry a colE1-like (pMB1) replicon and DNA sequences from NS1 flanking a multiple-cloning site and a resistance marker for one of the following antibiotics: chloramphenicol, erythromycin, gentamicin, or kanamycin. In X. fastidiosa, vectors with colE1-like (pMB1) replicons have been found to result primarily in the recovery of double recombinants rather than single recombinants. Thus, the ease of obtaining double recombinants and the stability of the resulting insertions at NS1 in the absence of selective pressure are the major advantages of this system. Based on in vitro and in planta characterizations, strains carrying insertions within NS1 are indistinguishable from wild-type X. fastidiosa in terms of growth rate, biofilm formation, and pathogenicity. To illustrate the usefulness of this system for complementation analysis, we constructed a strain carrying a mutation in the X. fastidiosa cpeB gene, which is predicted to encode a catalase/peroxidase, and showed that the sensitivity of this mutant to hydrogen peroxide could be overcome by the introduction of a wild-type copy of cpeB at NS1. Thus, this chromosome-based complementation system provides a valuable genetic tool for investigating the role of specific genes in X. fastidiosa cell physiology and virulence.Xylella fastidiosa is a slow growing, endophytic xanthomonad that is the causative agent of Pierce's disease of grapevine (for reviews, see references 2 and 15). X. fastidiosa is transmitted from infected plants to susceptible plant species, like grapevines, by xylem-feeding insects, such as spittlebugs and sharpshooters. Once inside the xylem, X. fastidiosa impedes the flow of sap within the grapevine, thereby producing the symptoms exhibited by X. fastidiosa-infected plants. These symptoms, which include marginal leaf scorch, leaf abscission, petioles that remain attached to the stem after the laminae have fallen off (matchsticks), areas of green epidermis on an otherwisebrown stem (green islands), desiccated fruits, and dieback of the vine, can be easily distinguished from water stress (38, 39). The distinctive symptoms of Pierce's disease are thought to arise from the plant's response to bacterial invasion and the production of virulence factors by X. fastidiosa following colonization of the xylem tissue.Two different genetic approaches have been taken to identify factors that contribute to X. fastidiosa virulence. One approach involves generating a random transposon (Tn5) insertion mutant library (10). This approach led to the identification of many genes whose functions appear necessary for full virulence (11,20,22). A second approach uses site-directed gene disruption (8) to target candidate virulence genes based on their similarity to genes of other gram-negative pathogens. The res...

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“…Specific activities of each purified catalase-GST as well as that of a GST control were determined spectrophotometrically by following the loss of H 2 O 2 at A 240 over time (42). All three catalases were active, and KatG's in vitro specific activity was about 4-fold higher than those of KatB and KatE (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…However, DC3000 contains only three of these catalase genes: katB (PSPTO_3582), katE (PSPTO_5263), and katG (PSPTO_4530) (4). KatB and KatE are monofunctional catalases, whose substrate is exclusively H 2 O 2 , while KatG is a bifunctional catalase, also known as hydroperoxidase, which exhibits both catalase and peroxidase activity (42). Bifunctional catalases are able to use organic peroxides as substrates as well as H 2 O 2 .…”

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confidence: 99%

Pseudomonas syringae Catalases Are Collectively Required for Plant Pathogenesis

et al. 2012

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ABSTRACTThe bacterial pathogenPseudomonas syringaepv. tomato DC3000 must detoxify plant-produced hydrogen peroxide (H2O2) in order to survive in its host plant. Candidate enzymes for this detoxification include the monofunctional catalases KatB and KatE and the bifunctional catalase-peroxidase KatG of DC3000. This study shows that KatG is the major housekeeping catalase of DC3000 and provides protection against menadione-generated endogenous H2O2. In contrast, KatB rapidly and substantially accumulates in response to exogenous H2O2. Furthermore, KatB and KatG have nonredundant roles in detoxifying exogenous H2O2and are required for full virulence of DC3000 inArabidopsis thaliana. Therefore, the nonredundant ability of KatB and KatG to detoxify plant-produced H2O2is essential for the bacteria to survive in plants. Indeed, a DC3000 catalase triple mutant is severely compromised in its ability to growin planta, and its growth can be partially rescued by the expression ofkatB,katE, orkatG. Interestingly, our data demonstrate that although KatB and KatG are the major catalases involved in the virulence of DC3000, KatE can also provide some protectionin planta. Thus, our results indicate that these catalases are virulence factors for DC3000 and are collectively required for pathogenesis.

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Comparative study of catalase-peroxidases (KatGs)

Cited by 106 publications

References 86 publications

Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-NAD by Catalase-peroxidases

Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-NAD by Catalase-peroxidases

Chromosome-Based Genetic Complementation System forXylella fastidiosa

Pseudomonas syringae Catalases Are Collectively Required for Plant Pathogenesis

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