Crystallization and preliminary X-ray diffraction studies of catalase–peroxidase from<i>Synechococcus</i>PCC 7942

Wada, Keita; Tada, Toshiji; Nakamura, Yoshihiro; Kinoshita, Takayoshi; Tamoi, Masahiro; Shigeoka, Shigeru; Nishimura, Keiichiro

doi:10.1107/s0907444901017735

Cited by 40 publications

(56 citation statements)

References 12 publications

(14 reference statements)

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“…Attempts to crystallize HPI from E. coli had commenced unsuccessfully in 1987, and success with the M. tuberculosis enzyme was no better. Persistence was finally rewarded in 2001 and 2002 with preliminary reports of the crystallization of catalase-peroxidases from the halophilic archaebacterium Haloarcula marismortui [48], from the cyanobacterium Synechococcus [49] and the Gram-negative bacterium Burkholderia pseudomallei [50], and of the C-terminal domain of HPI of E. coli [51]. The structure of the H. marismortui enzyme (HmCPx) at 2.0 Å was reported first [52], followed by the structure of the B. pseudomallei enzyme (BpKatG) at 1.7 Å [53].…”

Section: Catalase-peroxidase Structuresmentioning

confidence: 99%

Diversity of structures and properties among catalases

Chelikani

Fita

Loewen

2004

Cellular and Molecular Life Sciences (CMLS)

1,361

868

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Section: Catalase-peroxidase Structuresmentioning

confidence: 99%

Diversity of structures and properties among catalases

Chelikani

Fita

Loewen

2004

Cellular and Molecular Life Sciences (CMLS)

1,361

868

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“…Today the crystal structures of four bacterial CPs have been defined (see Protein Data Bank at RCSB for details, Wada et al, 2002;Bertrand et al, 2004). Structural analysis revealed that the proximal and distal heme pockets in the N-terminal domains contain conserved amino acids at almost identical positions as in the other class I peroxidases APx and CcP.…”

Section: Introductionmentioning

confidence: 99%

Phylogenetic distribution of catalase-peroxidases: Are there patches of order in chaos?

Passardi

Zámocký

Favet

et al. 2007

Gene

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“…The crystal structures of KatG from four different organisms, including Haloarcula morismortui (23,24), Synechococcus PCC7492 (25), Burkholderia pseudomallei (BpKatG) (26,27), and M. tuberculosis (28), along with the structures of the predominant INH-resistant variant S315T of MtKatG (7) and its homologue in BpKatG, S324T (22) 426 , is essential for catalase activity, but not peroxidase activity. 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).…”

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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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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Crystallization and preliminary X-ray diffraction studies of catalase–peroxidase fromSynechococcusPCC 7942

Cited by 40 publications

References 12 publications

Diversity of structures and properties among catalases

Diversity of structures and properties among catalases

Phylogenetic distribution of catalase-peroxidases: Are there patches of order in chaos?

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

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