Diversity of structures and properties among catalases

被引:1213
作者
Chelikani, P
Fita, I
Loewen, PC [1 ]
机构
[1] Univ Manitoba, Dept Microbiol, Winnipeg, MB R3T 2N2, Canada
[2] Consejo Super Invest Cient, Inst Biol Mol Barcelona, Barcelona, Spain
关键词
Catalase; peroxidase; crystal structure; heme; dimanganese;
D O I
10.1007/s00018-003-3206-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
More than 300 catalase sequences are now available, divided among monofunctional catalases (> 225), bifunctional catalase-peroxidases (> 50) and manganese-containing catalases (> 25). When combined with the recent appearance of crystal structures from at least two representatives from each of these groups (nine from the monofunctional catalases), valuable insights into the catalatic reaction mechanism in its various forms and into catalase evolution have been gained. The structures have revealed an unusually large number of modifications unique to catalases, a result of interacting with reactive oxygen species. Biochemical and physiological characterization of catalases from many different organisms has revealed a surprisingly wide range of catalatic efficiencies, despite similar sequences. Catalase gene expression in micro-organisms generally is controlled either by sensors of reactive oxygen species or by growth phase regulons, although the detailed mechanisms vary considerably.
引用
收藏
页码:192 / 208
页数:17
相关论文
共 123 条
[1]   CHARACTERIZATION OF A MANGANESE-CONTAINING CATALASE FROM THE OBLIGATE THERMOPHILE THERMOLEOPHILUM-ALBUM [J].
ALLGOOD, GS ;
PERRY, JJ .
JOURNAL OF BACTERIOLOGY, 1986, 168 (02) :563-567
[2]   MECHANISM OF ONE-ELECTRON OXIDATION OF NAD(P)H AND FUNCTION OF NADPH BOUND TO CATALASE [J].
ALMARSSON, O ;
SINHA, A ;
GOPINATH, E ;
BRUICE, TC .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1993, 115 (16) :7093-7102
[3]   Ligand diffusion in the catalase from Proteus mirabilis:: A molecular dynamics study [J].
Amara, P ;
Andreoletti, P ;
Jouve, HM ;
Field, MJ .
PROTEIN SCIENCE, 2001, 10 (10) :1927-1935
[4]   Unique presence of a manganese catalase in a hyperthermophilic archaeon, Pyrobaculum calidifontis VA1 [J].
Amo, T ;
Atomi, H ;
Imanaka, T .
JOURNAL OF BACTERIOLOGY, 2002, 184 (12) :3305-3312
[5]   High-resolution structure and biochemical properties of a recombinant Proteus mirabilas catalase depleted in iron [J].
Andreoletti, P ;
Sainz, G ;
Jaquinod, M ;
Gagnon, J ;
Jouve, HM .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 2003, 50 (02) :261-271
[6]   Three-dimensional structure of the enzyme dimanganese catalase from Thermus thermophilus at 1 Å resolution [J].
Antonyuk, SV ;
Melik-Adamyan, VR ;
Popov, AN ;
Lamzin, VS ;
Hempstead, PD ;
Harrison, PM ;
Artymyuk, PJ ;
Barynin, VV .
CRYSTALLOGRAPHY REPORTS, 2000, 45 (01) :105-116
[7]   The katX gene, which codes for the catalase in spores of Bacillus subtilis, is a forespore-specific gene controlled by σF, and KatX is essential for hydrogen peroxide resistance of the germinating spore [J].
Bagyan, I ;
Casillas-Martinez, L ;
Setlow, P .
JOURNAL OF BACTERIOLOGY, 1998, 180 (08) :2057-2062
[8]   Crystal structure of manganese catalase from Lactobacillus plantarum [J].
Barynin, VV ;
Whittaker, MM ;
Antonyuk, SV ;
Lamzin, VS ;
Harrison, PM ;
Artymiuk, PJ ;
Whittaker, JW .
STRUCTURE, 2001, 9 (08) :725-738
[9]  
Berthet S, 1997, PROTEIN SCI, V6, P481
[10]   A PEROXIDE ASCORBATE-INDUCIBLE CATALASE FROM HAEMOPHILUS-INFLUENZAE IS HOMOLOGOUS TO THE ESCHERICHIA-COLI KATE GENE-PRODUCT [J].
BISHAI, WR ;
SMITH, HO ;
BARCAK, GJ .
JOURNAL OF BACTERIOLOGY, 1994, 176 (10) :2914-2921