1uv4
From Proteopedia
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NATIVE BACILLUS SUBTILIS ARABINANASE ARB43A
Overview
Enzymes acting on polymeric substrates are frequently classified as exo or, endo, reflecting their preference for, or ignorance of, polymer chain, ends. Most biotechnological applications, especially in the field of, polysaccharide degradation, require either endo- or exo-acting hydrolases, or they harness the essential synergy between these two modes of action., Here, we have used genomic data in tandem with structure to modify, radically, the chain-end specificity of the Cellvibrio japonicus, exo-arabinanase CjArb43A. The structure of Bacillus subtilis, endo-arabinanase 43A (BsArb43A) in harness with chain-end recognition, kinetics of CjArb43A directed a rational design approach that led to the, conversion of the Cellvibrio enzyme from an exo to an endo mode of action., One of the ... [(full description)]
About this Structure
1UV4 is a [Single protein] structure of sequence from [Bacillus subtilis] with CA and EDO as [ligands]. Active as [Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [3.2.1.99]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A., Proctor MR, Taylor EJ, Nurizzo D, Turkenburg JP, Lloyd RM, Vardakou M, Davies GJ, Gilbert HJ, Proc Natl Acad Sci U S A. 2005 Feb 22;102(8):2697-702. Epub 2005 Feb 11. PMID:15708971
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