7cat: Difference between revisions

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[[Image:7cat.gif|left|200px]]
{{Seed}}
[[Image:7cat.png|left|200px]]


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{{STRUCTURE_7cat|  PDB=7cat  |  SCENE=  }}  
{{STRUCTURE_7cat|  PDB=7cat  |  SCENE=  }}  


'''THE NADPH BINDING SITE ON BEEF LIVER CATALASE'''
===THE NADPH BINDING SITE ON BEEF LIVER CATALASE===




==Overview==
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Beef liver and human erythrocyte catalases (EC 1.11.1.6) bind NADP tenaciously [Kirkman, H. N. &amp; 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.
The line below this paragraph, {{ABSTRACT_PUBMED_3856839}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_3856839}}


==About this Structure==
==About this Structure==
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[[Category: Sicignano, A.]]
[[Category: Sicignano, A.]]
[[Category: Tanaka, N.]]
[[Category: Tanaka, N.]]
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