1yz3: Difference between revisions

Revision as of 10:10, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1yz3.png

Template:STRUCTURE 1yz3

Structure of human pnmt complexed with cofactor product adohcy and inhibitor SK&F 64139Structure of human pnmt complexed with cofactor product adohcy and inhibitor SK&F 64139

Template:ABSTRACT PUBMED 16279783

About this StructureAbout this Structure

1YZ3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural, mutagenic, and kinetic analysis of the binding of substrates and inhibitors of human phenylethanolamine N-methyltransferase., Wu Q, Gee CL, Lin F, Tyndall JD, Martin JL, Grunewald GL, McLeish MJ, J Med Chem. 2005 Nov 17;48(23):7243-52. PMID:16279783

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-'''Structure of human pnmt complexed with cofactor product adohcy and inhibitor SK&F 64139'''
+===Structure of human pnmt complexed with cofactor product adohcy and inhibitor SK&F 64139===
-==Overview==
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-The X-ray structure of human phenylethanolamine N-methyltransferase (hPNMT) complexed with its product, S-adenosyl-L-homocysteine (4), and the most potent inhibitor reported to date, SK&amp;F 64139 (7), was used to identify the residues involved in inhibitor binding. Four of these residues, Val53, Lys57, Glu219 and Asp267, were replaced, in turn, with alanine. All variants had increased Km values for phenylethanolamine (10), but only D267A showed a noteworthy (20-fold) decrease in its kcat value. Both WT hPNMT and D267A had similar kcat values for a rigid analogue, anti-9-amino-6-(trifluoromethyl)benzonorbornene (12), suggesting that Asp267 plays an important role in positioning the substrate but does not participate directly in catalysis. The Ki values for the binding of inhibitors such as 7 to the E219A and D267A variants increased by 2-3 orders of magnitude. Further, the inhibitors were shown to bind up to 50-fold more tightly in the presence of S-adenosyl-L-methionine (3), suggesting that the binding of the latter brings about a conformational change in the enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_16279783}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Inhibitor complex]]
 [[Category: Product]]
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