1m0p | pdb_00001m0p

Structure of Dialkylglycine Decarboxylase Complexed with 1-Amino-1-phenylethanephosphonate

spinqualitylabelsall models 1m0p, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1m0p is a 1 chain structure with sequence from "pseudomonas_cepacia"_burkholder_1950 "pseudomonas cepacia" burkholder 1950. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ELP, K, NA Related: 1m0n, 1m0o, 1m0q Activity: 2,2-dialkylglycine decarboxylase (pyruvate), with EC number 4.1.1.64 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DGDA_BURCE] The dialkylglycine decarboxylase is of interest because it normally catalyzes both decarboxylation and amino transfer. It may be more properly described as a decarboxylating aminotransferase rather than an aminotransferring decarboxylase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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