2taa
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(New page: 200px<br /> <applet load="2taa" size="450" color="white" frame="true" align="right" spinBox="true" caption="2taa, resolution 3.0Å" /> '''STRUCTURE AND POSSIB...)
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Revision as of 07:02, 18 November 2007
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STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A
Overview
A complete molecular model of Taka-amylase A consisting of 478 amino acid, residues was built with the aid of amino acid sequence data. Some typical, structural features of the molecule are described. A model fitting of an, amylose chain in the catalytic site of the enzyme showed a possible, productive binding mode between substrate and enzyme. On the basis of the, difference Fourier analysis and the model fitting study, glutamic acid, (Glu230) and aspartic acid (Asp297), which are located at the bottom of, the cleft, were concluded to be the catalytic residues, serving as the, general acid and base, respectively.
About this Structure
2TAA is a Single protein structure of sequence from Aspergillus oryzae with CA as ligand. This structure superseeds the now removed PDB entry 1TAA. The following page contains interesting information on the relation of 2TAA with [Alpha-amylase]. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.
Reference
Structure and possible catalytic residues of Taka-amylase A., Matsuura Y, Kusunoki M, Harada W, Kakudo M, J Biochem (Tokyo). 1984 Mar;95(3):697-702. PMID:6609921
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