Sandbox Reserved 301: Difference between revisions
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==Central (a/b) Barrel Catalytic Domain== | ==Central (a/b) Barrel Catalytic Domain== | ||
Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene> <ref name="Abad"/>. | Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene> <ref name="Abad"/>. | ||
These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. coli Branching Enzyme in order for the enzymatic activity to be functional <ref name="Abad"/>. | These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. coli Branching Enzyme in order for the enzymatic activity to be functional<ref name="Abad"/>. | ||
=References= | =References= | ||
<references/> | <references/> | ||
<ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme] | <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme] | ||
