1m0p
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1m0p.gif|left|200px]] | [[Image:1m0p.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1m0p", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1m0p| PDB=1m0p | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Structure of Dialkylglycine Decarboxylase Complexed with 1-Amino-1-phenylethanephosphonate''' | '''Structure of Dialkylglycine Decarboxylase Complexed with 1-Amino-1-phenylethanephosphonate''' | ||
| Line 23: | Line 20: | ||
==Reference== | ==Reference== | ||
Aminophosphonate inhibitors of dialkylglycine decarboxylase: structural basis for slow binding inhibition., Liu W, Rogers CJ, Fisher AJ, Toney MD, Biochemistry. 2002 Oct 15;41(41):12320-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12369820 12369820] | Aminophosphonate inhibitors of dialkylglycine decarboxylase: structural basis for slow binding inhibition., Liu W, Rogers CJ, Fisher AJ, Toney MD, Biochemistry. 2002 Oct 15;41(41):12320-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12369820 12369820] | ||
| - | [[Category: 2,2-dialkylglycine decarboxylase (pyruvate)]] | ||
[[Category: Burkholderia cepacia]] | [[Category: Burkholderia cepacia]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 31: | Line 27: | ||
[[Category: Toney, M D.]] | [[Category: Toney, M D.]] | ||
[[Category: 3d-structure]] | [[Category: 3d-structure]] | ||
| - | [[Category: | + | [[Category: Decarboxylase]] |
| - | [[Category: | + | [[Category: Pyridoxal phosphate]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:29:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:29, 2 May 2008
Structure of Dialkylglycine Decarboxylase Complexed with 1-Amino-1-phenylethanephosphonate
Overview
The kinetics of inhibition of dialkylglycine decarboxylase by five aminophosphonate inhibitors are presented. Two of these [(R)-1-amino-1-methylpropanephosphonate and (S)-1-aminoethanephosphonate] are slow binding inhibitors. The inhibitors follow a mechanism in which a weak complex is rapidly formed, followed by slow isomerization to the tight complex. Here, the tight complexes are bound 10-fold more tightly than the weak, initial complexes. The slow onset inhibition occurs with t(1/2) values of 1.3 and 0.55 min at saturating inhibitor concentrations for the AMPP and S-AEP inhibitors, respectively, while dissociation of these inhibitor complexes occurs with t(1/2) values of 13 and 4.6 min, respectively. The X-ray structures of four of the inhibitors in complex with dialkylglycine decarboxylase have been determined to resolutions ranging from 2.6 to 2.0 A, and refined to R-factors of 14.5-19.5%. These structures show variation in the active site structure with inhibitor side chain size and slow binding character. It is proposed that the slow binding behavior originates in an isomerization from an initial complex in which the PLP pyridine nitrogen-D243 OD2 distance is approximately 2.9 A to one in which it is approximately 2.7 A. The angles that the C-P bonds make with the p orbitals of the aldimine pi system are correlated with the reactivities of the analogous amino acid substrates, suggesting a role for stereoelectronic effects in Schiff base reactivity.
About this Structure
1M0P is a Single protein structure of sequence from Burkholderia cepacia. Full crystallographic information is available from OCA.
Reference
Aminophosphonate inhibitors of dialkylglycine decarboxylase: structural basis for slow binding inhibition., Liu W, Rogers CJ, Fisher AJ, Toney MD, Biochemistry. 2002 Oct 15;41(41):12320-8. PMID:12369820 Page seeded by OCA on Sat May 3 00:29:33 2008
