3vm5 | pdb_00003vm5

Recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris

spinqualitylabelsall models 3vm5, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vm5 is a 1 chain structure with sequence from Oryzias latipes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The medaka fish alpha-amylase was expressed and purified. The expression systems were constructed using methylotrophic yeast Pichia pastoris, and the recombinant proteins were secreted into the culture medium. Purified recombinant alpha-amylase exhibited starch hydrolysis activity. The optimal pH, denaturation temperature, and K(M) and V(max) values were determined; chloride ions were essential for enzyme activity. The purified protein was also crystallized and examined by X-ray crystallography. The structure has the (alpha/beta)(8) barrel fold, as do other known alpha-amylases, and the overall structure is very similar to the structure of vertebrate (human and pig) alpha-amylases. A novel expression plasmid was developed. Using this plasmid, high-throughput construction of an expression system by homologous recombination in P. pastoris cells, previously reported for membrane proteins, was successfully applied to the secretory protein. Structural and functional characterization of recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris.,Mizutani K, Toyoda M, Otake Y, Yoshioka S, Takahashi N, Mikami B Biochim Biophys Acta. 2012 May 18. PMID:22613096 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase User:Gabriel Pons/Sandbox 2

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