Arylformamidase Function Slide 5: Difference between revisions

Latest revision as of 23:33, 9 June 2008

- Catalytic triad identified in paper - Ser154, Asp251, and His281.

- To assess functional similarity, conservation of the catalytic triad was analysed.

DALI alignment showing conservation of the catalytic triad between 2C7B and 2PBL.

- Similar level of conservation as noted between 2PBL and arylformamidase.

@@ Line 1: / Line 1: @@
-== Thermostable? ==
+== Evidence from Similar Structures ==
-'''Structural similarity'''
+- Catalytic triad identified in paper - Ser154, Asp251, and His281.
-  No:  Chain   Z    rmsd lali nres  %id  Description
+- To assess functional similarity, conservation of the catalytic triad was analysed.
-:  2pbl-A 52.4  0.0  262   262  100   MOLECULE: PUTATIVE ESTERASE/LIPASE/THIOESTERASE;
-:  2c7b-A 23.4  3.0  231   294   16   MOLECULE: CARBOXYLESTERASE;
-:  1jji-A 23.0  3.1  233   311   15   MOLECULE: CARBOXYLESTERASE;
-:  1evq-A 21.4  2.9  225   308   18   MOLECULE: SERINE HYDROLASE;
-'''Sequence similarity'''
+[[Image:Catalytic triad conversation.PNG|centre|framed|'''DALI alignment showing conservation of the catalytic triad between 2C7B and 2PBL.''']]
-[[Image:HSL_alignment.png|centre|framed|'''Alignment with thermophillic HSL family members identified by Byun 2007.''']]
+- Similar level of conservation as noted between 2PBL and arylformamidase.
-'''Ecology''' - an aquatic organism widely present throughout world's oceans.
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