3kxp | pdb_00003kxp

Crystal Structure of E-2-(Acetamidomethylene)succinate Hydrolase

spinqualitylabelsall models 3kxp, resolution 2.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kxp is a 12 chain structure with sequence from Mesorhizobium loti. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.26Å Ligands: CL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AAMHY_RHILO Catalyzes the final reaction in the degradation of vitamin B6 from (E)-2-(acetamidomethylene)succinate (E-2AMS) to produce succinic semialdehyde, acetate, ammonia and carbon dioxide. 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 gene identification and kinetic characterization of (E)-2-(acetamidomethylene)succinate (E-2AMS) hydrolase has recently been described. This enzyme catalyzes the final reaction in the degradation of vitamin B(6) and produces succinic semialdehyde, acetate, ammonia, and carbon dioxide from E-2AMS. The structure of E-2AMS hydrolase was determined to 2.3 A using SAD phasing. E-2AMS hydrolase is a member of the alpha/beta hydrolase superfamily and utilizes a serine/histidine/aspartic acid catalytic triad. Mutation of either the nucleophilic serine or the aspartate resulted in inactive enzyme. Mutation of an additional serine residue in the active site causes the enzyme to be unstable and is likely structurally important. The structure also provides insight into the mechanism of hydrolysis of E-2AMS and identifies several potential catalytically important residues. Structure Determination and Characterization of the Vitamin B(6) Degradative Enzyme (E)-2-(Acetamidomethylene)succinate Hydrolase (,).,McCulloch KM, Mukherjee T, Begley TP, Ealick SE Biochemistry. 2010 Feb 16;49(6):1226-35. PMID:20099871 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA