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The NADPH binding site on beef liver catalase.

Fita I, Rossmann MG
Proc Natl Acad Sci U S A 82 1604-8 (1985)
Cited: 93 times
EuropePMC logo PMID: 3856839

Abstract

Beef liver and human erythrocyte catalases (EC 1.11.1.6) bind NADP tenaciously [Kirkman, H. N. & Gaetani, G. F. (1984) Proc. Natl. Acad. Sci. USA 81, 4343-4348]. The position of NADP on beef liver catalase corresponds to the carboxyl-terminal polypeptide hinge in Penicillium vitale fungal catalase, which connects the common catalase structure to the additional flavodoxin-like domain. In contrast to nearly all other known structures of protein-bound NADP, NAD, and FAD, the NADP molecule of beef liver catalase is folded into a right-handed helix and bound, in part, in the vicinity of the carboxyl end of two alpha-helices. A water molecule (W7) occupies a pseudosubstrate site close to the C4 position of the nicotinamide and is hydrogen bonded to His-304. Although the NADP and heme groups approach each other to within 13.7 A, there is no direct interaction. The function of the NADP remains a mystery.

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Related citations provided by authors (9)

  1. The Refined Structure of Beef Liver Catalase at 2.5 Angstroms Resolution. Fita I, Silva AM, Murthy MRN, Rossmann MG Acta Crystallogr., B 42 497- (1986)
  2. Comparison of Beef Liver and Penicillium Vitale Catalases. Melik-Adamyan WR, Barynin VV, Vagin AA, Borisov VV, Vainshtein BK, Fita I, Murthy MRN, Rossmann MG J. Mol. Biol. 188 63- (1986)
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  4. Structure of Beef Liver Catalase. Murthy MRN, Reid III TJ, Sicignano A, Tanaka N, Rossmann MG J. Mol. Biol. 152 465- (1981)
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