Sandbox Reserved 301: Difference between revisions

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E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.
E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.
=Domains=
=Domains=
Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>.
Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.
The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.


==Amino-Terminal Domain==
==Amino-Terminal Domain==
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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/Conserved_residues/1'>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 mutagensis an chemical motification revealed that Tyr300 and Glu459 to be conserved specifically to E.''coli''.
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]