Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei

scientific article published on 01 January 2007

Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/PROT.21209
P698PubMed publication ID17063492

P50authorTaweewat DeemagarnQ46820924
Benjamin WisemanQ59693111
P2093author name stringPeter C Loewen
Ignacio Fita
Anabella Ivancich
Xavier Carpena
P433issue1
P921main subjectBurkholderia pseudomalleiQ140475
P304page(s)219-228
P577publication date2007-01-01
P1433published inProteinsQ7251514
P1476titleTwo alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei
P478volume66

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cites work (P2860)
Q35001145A dimeric chlorite dismutase exhibits O2-generating activity and acts as a chlorite antioxidant in Klebsiella pneumoniae MGH 78578.
Q51554987Comparative study of enzymatic activities of new KatG mutants from low- and high-level isoniazid-resistant clinical isolates of Mycobacterium tuberculosis
Q33836289Isoniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: catalase, peroxidase, and INH-NADH adduct formation activities
Q27662376Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-NAD by Catalase-peroxidases
Q46086474Mechanistic insight into the initiation step of the reaction of Burkholderia pseudomallei catalase-peroxidase with peroxyacetic acid.
Q43167115Role of the oxyferrous heme intermediate and distal side adduct radical in the catalase activity of Mycobacterium tuberculosis KatG revealed by the W107F mutant
Q54334343Stimulation of KatG catalase activity by peroxidatic electron donors
Q37972484Thirty years of heme catalases structural biology

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