Fita I, Rossmann M G
Proc Natl Acad Sci U S A. 1985 Mar;82(6):1604-8. doi: 10.1073/pnas.82.6.1604.
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.
牛肝和人红细胞过氧化氢酶(EC 1.11.1.6)能紧密结合NADP [柯克曼,H. N. & 加埃塔尼,G. F.(1984年)《美国国家科学院院刊》81卷,4343 - 4348页]。NADP在牛肝过氧化氢酶上的位置与维氏青霉真菌过氧化氢酶的羧基末端多肽铰链相对应,该铰链将常见的过氧化氢酶结构与额外的类黄素氧还蛋白结构域相连。与几乎所有其他已知的蛋白质结合NADP、NAD和FAD结构不同,牛肝过氧化氢酶的NADP分子折叠成右手螺旋,并部分结合在两个α - 螺旋羧基末端附近。一个水分子(W7)占据靠近烟酰胺C4位置的假底物位点,并与His - 304形成氢键。尽管NADP和血红素基团彼此靠近至13.7埃以内,但没有直接相互作用。NADP的功能仍然是个谜。