The catalase-peroxidase of Mycobacterium intracellulare: nucleotide sequence analysis and expression in Escherichia coli

Morris, Sheldon L.; Nair, Jaygopal; Rouse, David A.

doi:10.1099/00221287-138-11-2363

Cited by 40 publications

(30 citation statements)

References 27 publications

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“…Besides their different catalytic behaviour these enzymes also differ in their reduction by dithionite, the narrow pH range for maximal activity, inactivation by hydrogen peroxide and their insensitivity to %amino-1,2,4-triazole. Most of the catalase-peroxidases are tetramers isolated from bacteria (Claiborne and Fridovich, 1979 ;Nadler et al, 1986;Hochman and Goldberg, 1991 ;Yumoto et al, 1990;Morris et al, 1992;Brown-Peterson and Salin, 1993). Those of B L K~~U S stearothermophi1u.s (Loprasert et al, 1988), Comamon c i~ cwizprunsoris (Nies and Schlegel,1 982), Mycobactevium tuIx~rcdosis (Diaz and Wayne, 1974) and Streptomyces cyaneus (Mliki and Zimmermann, 1992) exist as dimers.…”

Section: K E Y W~r D~smentioning

confidence: 99%

Purification and Characterization of an Intracellular Catalase‐Peroxidase from Penicillium Simplicissimum

Fraaije

Roubroeks

Hagen

et al. 1996

European Journal of Biochemistry

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The first dimeric catalase-peroxidase of eucaryotic origin, an intracellular hydroperoxidase from Penicillium simplicissimum which exhibited both catalase and peroxidase activities, has been isolated. The enzyme has an apparent molecular m of about 170 kDa and is composed of two identical subunits. The purified protein has a pH optimum for catalase activity at 6.4 and for peroxidase at 5.4. Both activities are inhibited by cyanide and azide whereas 3-amino-l,2,4-triazole has no effect. 3,3'-Diaminobenzidine, 3,3'-dimethoxybenzidine, guaiacol, 2,6-dimethoxyphenol and 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) all serve as substrates. The optical spectrum of the purified enzyme shows a Soret band at 407 nm. Reduction by dithionite results in the disappearance of the Soret band and formation of three absorption maxima at 440, 562 and 595 nm. The prosthetic group was identified as a protoheme IX and EPR spectroscopy revealed the presence of a histidine residue as proximal ligand.In addition to the catalase-peroxidase, an atypical catalase which is active over a broad pH range was also partially purified from P sinzplicissimum. This catalase is located in the periplasm and contains a chlorin-type heme as prosthetic group. K e y w~r d~s :catalase-peroxidase ; peroxidase ; EPR ; chlorin-type heme ; Penicillium .rirnplicissimunz.Catalases are ubiquitous enzymes which have bcen isolated from a broad rangc of procaryotic and eucaryotic organisms. Most catalases described so far are tetramers with molecular masses ranging over 220-270 kDa with each subunit containing a protoheme as prosthetic group. These typical catalases are activc in the pH range 5 -10 and are specifically inactivated by 3-amino-I ,2,4-triazole.More recently, some intracellular hydroperoxidases have been described that have properties deviating from the above enzymes. Enzymes of this new class of hydroperoxidases exhibit both catalase a s well as significant peroxidase activity and are therefore called catalase-peroxidases. Besides their different catalytic behaviour these enzymes also differ in their reduction by dithionite, the narrow pH range for maximal activity, inactivation by hydrogen peroxide and their insensitivity to %amino-1,2,4-triazole. Most of the catalase-peroxidases are tetramers isolated from bacteria (Claiborne and Fridovich, 1979 ;Nadler et al., 1986; Hochman and Goldberg, 1991 ;Yumoto et al., 1990;Morris et al., 1992;Brown-Peterson and Salin, 1993). Those of B L K~~U S stearothermophi1u.s (Loprasert et al., 1988), Comamon c i~ cwizprunsoris (Nies and Schlegel, 1 982), Mycobactevium tuIx~rcdosis (Diaz and Wayne, 1974) and Streptomyces cyaneus (Mliki and Zimmermann, 1992) exist as dimers. Furthermore, monomeric calalase-peroxidases have been purified from two halophilic archaebacteria (Fukumori et d . , 1985 ; Cendrin et al., 1994). Until now the tetrameric catalase-peroxidase from the Courc.sponderzce fo W.

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Section: K E Y W~r D~smentioning

confidence: 99%

Purification and Characterization of an Intracellular Catalase‐Peroxidase from Penicillium Simplicissimum

Fraaije

Roubroeks

Hagen

et al. 1996

European Journal of Biochemistry

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“…Genes encoding catalase-peroxidase (katG) from slow-growing mycobacteria, such as M. tuberculosis (16) and M. intracellulare (24), have been cloned and sequenced. Polymorphism associated with the katG region has been reported for M. tuberculosis.…”

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confidence: 99%

katGI and katGII encode two different catalases-peroxidases in Mycobacterium fortuitum

et al. 1997

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It has been suggested that catalase-peroxidase plays an important role in several aspects of mycobacterial metabolism and is a virulence factor in the main pathogenic mycobacteria. In this investigation, we studied genes encoding for this protein in the fast-growing opportunistic pathogen Mycobacterium fortuitum. Nucleotide sequences of two different catalase-peroxidase genes (katGI and katGII) of M. fortuitum are described. They show only 64% homology at the nucleotide level and 55% identity at the amino acid level, and they are more similar to catalases-peroxidases from different bacteria, including mycobacteria, than to each other. Both proteins were found to be expressed in actively growing M. fortuitum, and both could also be expressed when transformed into Escherichia coli and M. aurum. We detected the presence of a copy of IS6100 in the neighboring region of a katG gene in the M. fortuitum strain in which this element was identified (strain FC1). The influence of each katG gene on isoniazid (isonicotinic acid hydrazide; INH) susceptibility of mycobacteria was checked by using the INH-sensitive M. aurum as the host. Resistance to INH was induced when katGI was transformed into INH-sensitive M. aurum, suggesting that this enzyme contributes to the natural resistance of M. fortuitum to the drug. This is the first report showing two different genes encoding same enzyme activity which are actively expressed within the same mycobacterial strain.Mycobacterium is an old bacterial genus which includes species from a broad range of ecological niches (14). Pathogenicity ranges from strict specificity for humans or animals, such as Mycobacterium tuberculosis, M. leprae, or M. paratuberculosis, to specificity for saprophytes, such as M. smegmatis and M. phlei. Occupying an intermediate position is M. fortuitum, which can be isolated from clinical samples as an opportunistic pathogen and from environmental sources as a saprophyte (38).The level of adaptation that bacteria have to their environment is possibly related to the number of genes that they are able to activate as a consequence of detection of changes in its environment. The genomic length of the intracellular restricted mycobacterium M. leprae is smaller than that of other mycobacteria (6,11,28). This possibly indicates that M. leprae requires fewer genes for survival within its host due to the stability of its environment.Mycobacteria are considered archetypical intracellular pathogens because of their capacity to invade and multiply within macrophages, and they have evolved mechanisms for evading macrophage-mediated killing. An important mechanism employed by macrophages is the production of toxic reactive oxygen intermediates (5, 27). Catalases-peroxidases are enzymes which are used by bacteria to protect themselves against reactive oxygen intermediates, and hence they are likely to be important for survival within macrophages (27).Catalase-peroxidase plays a crucial enzymatic role in mycobacterial metabolism by increasing the chance of survival inside mac...

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“…The gene encoding the M. intracellulare KatG catalase-peroxidase (heat labile, HPI T-catalase) was cloned and expressed in E. coli (Morris et al, 1992). They found that the presence of another catalase activity appeared to be involved in antagonizing isoniazid activity.…”

Section: The Mechanism Of Resistance To Isoniazidmentioning

confidence: 99%

“…The katE gene of M. avium, encoding an HPII-type, heat-stable, M-type catalase-peroxidase has been cloned (Milano et al, 1996) as has the katG gene of M. intracellulare, encoding a HPI-type, heat-labile and T-type catalase (Morris et al, 1992).…”

Section: Mycobacterial Catalase-peroxidasesmentioning

confidence: 99%

Mycobacterial catalases, peroxidases, and superoxide dismutases and their effects on virulence and isoniazid-susceptibility in mycobacteria - a review

Bartoš¹,

Falkinham²,

Pavlík³

2004

Vet. Med. - Czech

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Mycobacteria are intracellular bacterial parasites which survive and proliferate inside of macrophages for long periods of time. Because mycobacterial survival in macrophages is required for virulence, a great deal of effort has been focused on identifying the genetic and physiologic determinants of intracellular survival and growth. A number of factors, among them catalases, peroxidases, and superoxide dismutase have been suggested as agents permi�ing mycobacteria to overcome the intracellular defences of macrophages. The characteristic features of mycobacterial catalase/peroxidases and superoxide dismutase, their distribution within the genus Mycobacterium, and their mutual interactions in the inactivation of toxic oxygen products are reviewed. Focus is placed on evidence of the role of mycobacterial catalase-peroxidase and superoxide dismutase in virulence and on the role of catalaseperoxidase in susceptibility to isonicotinic acid hydrazide.

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The catalase-peroxidase of Mycobacterium intracellulare: nucleotide sequence analysis and expression in Escherichia coli

Cited by 40 publications

References 27 publications

Purification and Characterization of an Intracellular Catalase‐Peroxidase from Penicillium Simplicissimum

Purification and Characterization of an Intracellular Catalase‐Peroxidase from Penicillium Simplicissimum

katGI and katGII encode two different catalases-peroxidases in Mycobacterium fortuitum

Mycobacterial catalases, peroxidases, and superoxide dismutases and their effects on virulence and isoniazid-susceptibility in mycobacteria - a review

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