Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin

被引:123
|
作者
Parsonage, Derek [1 ]
Karplus, P. Andrew [2 ]
Poole, Leslie B. [1 ]
机构
[1] Wake Forest Univ, Bowman Gray Sch Med, Dept Biochem, Winston Salem, NC 27157 USA
[2] Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA
关键词
antioxidants; peroxidases; redox regulation; redox-active disulfide;
D O I
10.1073/pnas.0708308105
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Typical 2-Cys peroxiredoxins (Prxs) are ubiquitous peroxidases that are involved in peroxide scavenging and/or the regulation of peroxide signaling in eukaryotes. Despite their prevalence, very few Prxs have been reliably characterized in terms of their substrate specificity profile and redox potential even though these values are important for gaining insight into physiological function. Here, we present such studies focusing on Salmonella typhimurium alkyl hydroperoxide reductase C component (StAhpC), an enzyme that has proven to be an excellent prototype of this largest and most widespread class of Prxs that includes mammalian Prx I-Prx IV. The catalytic efficiencies of StAhpC (k(cat)/K-m) are > 10(7) M-1.s(-1) for inorganic and primary hydroperoxide substrates and approximate to 100-fold less for tertiary hydroperoxides, with the difference being exclusively caused by changes in K-m. The oxidative inactivation of AhpC through reaction with a second molecule of peroxide shows parallel substrate specificity. The midpoint reduction potential of StAhpC is determined to be -178 +/- 0.4 mV, a value much higher than most other thiol-based redox proteins. The relevance of these results for our understanding of Prx and the physiological role of StAhpC is discussed.
引用
收藏
页码:8209 / 8214
页数:6
相关论文
共 50 条
  • [21] ON SUBSTRATE SPECIFICITY OF BACTERIAL EPSILON-LYSINE ACYLASE
    CHIBATA, I
    ISHIKAWA, T
    TOSA, T
    ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1964, 104 (02) : 231 - &
  • [22] Structural basis of the substrate specificity of human and bacterial kynureninase
    Phillips, R. S.
    FEBS JOURNAL, 2013, 280 : 171 - 172
  • [23] SUBSTRATE-SPECIFICITY OF BACTERIAL GLYCEROPHOSPHOLIPID - CHOLESTEROL ACYLTRANSFERASE
    BUCKLEY, JT
    BIOCHEMISTRY, 1982, 21 (26) : 6699 - 6703
  • [24] Comparison of the substrate specificity of the two bacterial desulfurization systems
    Jin Konishi
    Hideki Okada
    Kazuaki Hirasawa
    Yoshitaka Ishii
    Kenji Maruhashi
    Biotechnology Letters, 2002, 24 : 1863 - 1867
  • [25] Enzymatic properties and substrate specificity of a bacterial phosphatidylcholine synthase
    Aktas, Meriyem
    Koester, Stefan
    Kizilirmak, Sarah
    Casanova, Javier C.
    Betz, Heidi
    Fritz, Christiane
    Moser, Roman
    Yildiz, Oezkan
    Narberhaus, Franz
    FEBS JOURNAL, 2014, 281 (15) : 3523 - 3541
  • [26] Comparison of the substrate specificity of the two bacterial desulfurization systems
    Konishi, J
    Okada, H
    Hirasawa, K
    Ishii, Y
    Maruhashi, K
    BIOTECHNOLOGY LETTERS, 2002, 24 (22) : 1863 - 1867
  • [27] Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus
    Liu, Wenxia
    Liu, Aijun
    Gao, Hailong
    Wang, Quan
    Wang, Limin
    Warkentin, Eberhard
    Rao, Zihe
    Michel, Hartmut
    Peng, Guohong
    BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 2018, 1862 (12): : 2797 - 2805
  • [28] Biological organic peroxides as substrates/ inhibitors of bacterial AhpC
    de Oliveira, M. A.
    Cabrera, V. I.
    Vargas, S.
    da Silva, L. F.
    Lago, J. H. G.
    Toyama, M. H.
    Netto, L. E. Soares
    FEBS OPEN BIO, 2024, 14 : 236 - 237
  • [29] EFFECT OF BLOOD ON REDOX POTENTIAL IN BACTERIAL CULTURES
    ZADOR, S
    ACTA BIOLOGICA ACADEMIAE SCIENTIARUM HUNGARICAE, 1962, 13 (02): : 193 - &
  • [30] EFFECT OF TEMPERATURE ON REDOX POTENTIAL IN BACTERIAL CULTURES
    ZADOR, S
    ACTA BIOLOGICA ACADEMIAE SCIENTIARUM HUNGARICAE, 1961, 11 (04): : 387 - &